query: where is collagen found in the human body

pos: Collagen Collagen Collagen is the main structural protein in the extracellular space in the various connective tissues in the body. As the main component of connective tissue, it is the most abundant protein in mammals, making 25% to 35% of the whole-body protein content. Collagen consists of amino acids wound together to form triple-helices l of elongated fibrils. It is mostly found in fibrous tissues such as tendons, ligaments and skin. Depending upon the degree of mineralization, collagen tissues may be either rigid (bone) or compliant (tendon) or have a gradient from rigid to compliant (cartilage). It is also abundant in

pos: Artificial cartilage synthetic cartilage to be used in joint spaces, high mechanical strength under compression needs to be an intrinsic property of the material. There are three types of cartilage in the human body: fibrocartilage, hyaline cartilage and elastic cartilage. Each type of cartilage has varying concentrations of components such as proteoglycans, collagen and water which determine its functional properties and location in the body. Fibrocartilage is most often found in the intervertebral discs, elastic cartilage is found in the external ear and hyaline cartilage is found on many joint surfaces in the body. Replacement of hyaline cartilage (articular cartilage) is the

pos: Precambrian body plans synthesis of collagen. Collagen is the most abundant protein in mammals and is an essential molecule in the formation of bones, skin and other connective tissue. Different types of collagen have been found in all multicellular organisms, including sponges. It has been found that sponges do have a gene sequence coding for collagen type IV which is a diagnostic feature of the basal lamina It has also been found that 29 types of collagen have been found to exist in humans. This vast group can further be divided into several families according to their primary structures and supramolecular organization. Among

pos: Collagen This refers to the compound's early use in the process of boiling the skin and tendons of horses and other animals to obtain glue. Collagen occurs in many places throughout the body. Over 90% of the collagen in the human body, however, is type I. So far, 28 types of collagen have been identified and described. They can be divided into several groups according to the structure they form: The five most common types are: The collagenous cardiac skeleton which includes the four heart valve rings, is histologically, elastically and uniquely bound to cardiac muscle. The cardiac skeleton also includes

pos: Collagen Collagen Collagen is the main structural protein in the extracellular space in the various connective tissues in the body. As the main component of connective tissue, it is the most abundant protein in mammals, making 25% to 35% of the whole-body protein content. Collagen consists of amino acids wound together to form triple-helices l of elongated fibrils. It is mostly found in fibrous tissues such as tendons, ligaments and skin. Depending upon the degree of mineralization, collagen tissues may be either rigid (bone) or compliant (tendon) or have a gradient from rigid to compliant (cartilage). It is also abundant in

pos: Type I collagen by enzymes outside the cell. Once these molecules are processed, they arrange themselves into long, thin fibrils that cross-link to one another in the spaces around cells. The cross-links result in the formation of very strong mature type I collagen fibers. See Collagen, type I, alpha 1#Clinical significance Type I collagen Type I collagen is the most abundant collagen of the human body which forms large, eosinophilic fibers known as collagen fibers. It is present in scar tissue, the end product when tissue heals by repair, as well as tendons, ligaments, the endomysium of myofibrils, the organic part of bone,

pos: Scurvy ascorbic acid is required as a cofactor for prolyl hydroxylase and lysyl hydroxylase. These two enzymes are responsible for the hydroxylation of the proline and lysine amino acids in collagen. Hydroxyproline and hydroxylysine are important for stabilizing collagen by cross-linking the propeptides in collagen. Collagen is a primary structural protein in the human body, necessary for healthy blood vessels, muscle, skin, bone, cartilage, and other connective tissues. Defective connective tissue leads to fragile capillaries, resulting in abnormal bleeding, bruising, and internal hemorrhaging. Collagen is an important part of bone, so bone formation is also affected. Teeth loosen, bones break more

pos: Collagen, type I, alpha 1 are associated with the following conditions: Collagen, type I, alpha 1 Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the "COL1A1" gene. COL1A1 encodes the major component of type I collagen, the fibrillar collagen found in most connective tissues, including cartilage. Collagen is a protein that strengthens and supports many tissues in the body, including cartilage, bone, tendon, skin and the white part of the eye (sclera). The COL1A1 gene produces a component of type I collagen, called the pro-alpha1(I) chain. This chain combines with another pro-alpha1(I)

pos: Type I collagen Type I collagen Type I collagen is the most abundant collagen of the human body which forms large, eosinophilic fibers known as collagen fibers. It is present in scar tissue, the end product when tissue heals by repair, as well as tendons, ligaments, the endomysium of myofibrils, the organic part of bone, the dermis, the dentin and organ capsules. The COL1A1 gene produces the pro-alpha1(I) chain. This chain combines with another pro-alpha1(I) chain and also with a pro-alpha2(I) chain (produced by the COL1A2 gene) to make a molecule of type I procollagen. These triple-stranded, rope-like procollagen molecules must be processed

pos: Collagen, type I, alpha 1 Collagen, type I, alpha 1 Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the "COL1A1" gene. COL1A1 encodes the major component of type I collagen, the fibrillar collagen found in most connective tissues, including cartilage. Collagen is a protein that strengthens and supports many tissues in the body, including cartilage, bone, tendon, skin and the white part of the eye (sclera). The COL1A1 gene produces a component of type I collagen, called the pro-alpha1(I) chain. This chain combines with another pro-alpha1(I) chain and also with a pro-alpha2(I)

pos: Acne increase natural collagen production in the skin and to increase skin volume and decrease the depth of acne scars. Examples of fillers used for this purpose include hyaluronic acid; poly(methyl methacrylate) microspheres with collagen; human and bovine collagen derivatives, and fat harvested from the person's own body (autologous fat transfer). Microneedling is a procedure in which an instrument with multiple rows of tiny needles is rolled over the skin to elicit a wound healing response and stimulate collagen production to reduce the appearance of atrophic acne scars in people with darker skin color. Notable adverse effects of microneedling include postinflammatory

pos: Collagen, type XXIII, alpha 1 be found in the epidermis and other epithelia such as those in tongue, gut and lung, but also in the brain, the kidney and the cornea. It has been shown that in prostate collagen XXIII expression is associated with tumor progression. The functions of collagen XXIII are still unknown, although it is believed that they could be similar to other transmembrane proteins, such as collagen XIII. Collagen XXIII was first identified and isolated from rat prostate carcinoma cells by Jacqueline Banyard, Lere Bao and Bruce R. Zetter in 2003. They also identified this protein in human tissue. They concluded that

pos: Collagen as a healing aid for burn patients for reconstruction of bone and a wide variety of dental, orthopedic, and surgical purposes. Both human and bovine collagen is widely used as dermal fillers for treatment of wrinkles and skin aging. Some points of interest are: As the skeleton forms the structure of the body, it is vital that it maintains its strength, even after breaks and injuries. Collagen is used in bone grafting as it has a triple helical structure, making it a very strong molecule. It is ideal for use in bones, as it does not compromise the structural integrity

pos: Human body as multicellular organisms which reside in the gastrointestinal tract and on the skin. Not all parts of the body are made from cells. Cells sit in an extracellular matrix that consists of proteins such as collagen, surrounded by extracellular fluids. Of the 70 kg weight of an average human body, nearly 25 kg is non-human cells or non-cellular material such as bone and connective tissue. Cells in the body function because of DNA. DNA sits within the nucleus of a cell. Here, parts of DNA are copied and sent to the body of the cell via RNA. The RNA is

pos: Collagen, type VII, alpha 1 disease called epidermolysis bullosa acquisita. Type VII collagen is also found in the retina; its function in this organ is unknown. COL7A1 is located on the short arm of human chromosome 3, in the chromosomal region denoted 3p21.31. The gene is approximately 31,000 base pairs in size and is remarkable for the extreme fragmentation of its coding sequence into 118 exons. COL7A1 is transcribed into an mRNA of 9,287 base pairs. In the skin, the type VII collagen protein is synthesized by keratinocytes and dermal fibroblasts. The symbol for the orthologous gene in the mouse is Col7a1. The inherited disease,

pos: Cortisol is found in muscles, tendons, and joints, as well as throughout the entire body. Cortisol down-regulates the synthesis of collagen. Cortisol raises the free amino acids in the serum by inhibiting collagen formation, decreasing amino acid uptake by muscle, and inhibiting protein synthesis. Cortisol (as opticortinol) may inversely inhibit IgA precursor cells in the intestines of calves. Cortisol also inhibits IgA in serum, as it does IgM; however, it is not shown to inhibit IgE. Cortisol and the stress response have known deleterious effects on the immune system. High levels of perceived stress and increases in cortisol have been found

pos: TachoSil reaction to horse proteins or human blood products are not good candidates for use of TachoSil. TachoSil TachoSil is a collagen sponge coated with the human coagulation factors fibrinogen and thrombin. It is used during surgery to stop local bleeding on internal organs (hemostasis). The sponge is manufactured from horse tendons. TachoSil reacts upon contact with blood, other body fluids or saline to form a clot that glues it to the tissue surface. Hemostasis is reached in a few minutes, and the sponge is absorbed by the body within several weeks. Some patients experience hypersensitivity or allergic reactions. In rare

pos: Glucosepane evidence, that the most likely mechanism of getting from the α-dicarbonyl to glucosepane is through the intramolecular aldimine 6-(3,4-dihydroxy-6-oxo-3,4,5,6-tetrahydro-2H-azepinium-1-yl) norleucine. The ring is hypothesized to form by a nucleophilic attack of N on C-6 carbonyl, followed by elimination of a water (2). This then condenses with the arginine side chain to yield glucosepane in nucleophilic addition-elimination reactions of the nitrogens of arginine and the electrophilic carbonyls on the ring, eliminating two waters. Glycation processes that lead to AGEs particularly affect long-lived proteins in the human body, such as collagen in the skin and crystallin in the eyes. Skin collagen, for

pos: Vitamin C of vitamin C, since without this vitamin, collagen made by the body is too unstable to perform its function. Scurvy leads to the formation of brown spots on the skin, spongy gums, and bleeding from all mucous membranes. The spots are most abundant on the thighs and legs, and a person with the ailment looks pale, feels depressed, and is partially immobilized. In advanced scurvy there are open, suppurating wounds and loss of teeth and, eventually, death. The human body can store only a certain amount of vitamin C, and so the body stores are depleted if fresh supplies are

pos: Photoaging inadequate to cause sunburn can thus facilitate the degradation of skin collagen and lead to presumably, eventual photoaging. Thus, collagen production is reduced in photoaged skin due to the process of constant degradation of collagen mediated by MMPs. In addition, the presence of damaged collagen would also down-regulate the synthesis of new collagen. The impaired spreading and attachment of fibroblasts onto degraded collagen could be one of the contributing factors to the inhibition of collagen synthesis. UV radiation decreases the expression of both retinoic acid receptors and retinoid X receptors in human skin, thereby resulting in a complete loss of

pos: TachoSil TachoSil TachoSil is a collagen sponge coated with the human coagulation factors fibrinogen and thrombin. It is used during surgery to stop local bleeding on internal organs (hemostasis). The sponge is manufactured from horse tendons. TachoSil reacts upon contact with blood, other body fluids or saline to form a clot that glues it to the tissue surface. Hemostasis is reached in a few minutes, and the sponge is absorbed by the body within several weeks. Some patients experience hypersensitivity or allergic reactions. In rare cases, it could turn into severe hypersensitive reaction. Those who are prone to having a systemic

pos: Connective tissue disease component of ligaments (tissues that attach bone to bone) and skin. In patients with connective tissue disease, it is common for collagen and elastin to become injured by inflammation (ICT). Many connective tissue diseases feature abnormal immune system activity with inflammation in tissues as a result of an immune system that is directed against one's own body tissues (autoimmunity). Diseases in which inflammation or weakness of collagen tends to occur are also referred to as collagen diseases. Collagen vascular diseases can be (but are not necessarily) associated with collagen and blood vessel abnormalities and that are autoimmune in nature. See

pos: Pyridinoline Pyridinoline Pyridinoline, also known as Hydroxylysylpyridinoline, is a fluorescent cross-linking compound of collagen fibers. Crosslinks in collagen and elastin are derived from lysyl and hydroxylysyl residues, a process catalyzed by lysyl oxidase. Fujimoto and colleagues first described the isolation and characterization of a fluorescent material in bovine Achilles tendon collagen and termed it pyridinoline. It is reported to be present in collagen of bone and cartilage, but is absent in collagen of skin. It is not present in newly synthesized collagen and is formed from aldimine cross-links during maturation of collagen fibers. Pyridinoline and deoxypyridinoline were found to be released

pos: Collagen, type XI, alpha 2 Collagen, type XI, alpha 2 Collagen alpha-2(XI) chain is a protein that in humans is encoded by the "COL11A2" gene. The COL11A2 gene produces one component of this type of collagen, called the pro-alpha2(XI) chain. Type XI collagen adds structure and strength to the tissues that support the body's muscles, joints, organs and skin (the connective tissue). Type XI collagen is normally found in cartilage as well as the fluid that fills the eyeball, the inner ear, and the center portion of the discs between the vertebrae in the spine (nucleus pulposus). Type XI collagen also helps maintain the spacing

pos: Collagen VI amino acids. The first two alpha chains subunits of collagen VI have a molecular weight of 140-150 KDa and the third polypeptide chain is larger with a molecular weight of 250-300kDa. Collagen VI is also found in the skin, lungs, blood vessels, cornea and intervertebral disc. It also forms part of the peripheral nerves, brain, myocardium and adipose tissue. There has been recent discoveries of Collagen VI including Col6formula_14, Col6formula_15 and Col6formula_16. Defects are associated with Bethlem myopathy and Ullrich congenital muscular dystrophy. Collagen VI Collagen VI is a form of collagen primarily associated with the extracellular matrix of skeletal

pos: Trichobilharzia regenti which are capable of keratin and collagen degradation. Experiments with laboratory prepared recombinant form of the cysteine peptidase cathepsin B2 of "T. regenti" (TrCB2) confirmed its ability to cleave skin proteins (collagen, keratin and elastin). After penetration the skin, cercariae transform to schistosomula and start a migration through the host’s body. They avoid penetration into blood capillaries and rather prefer entering peripheral nerves in host’s limbs. Schistosomula are found in peripheral nerves of ducks and mice as soon as 1.5 and 1 day post infection (DPI), respectively. In both types of hosts, schistosomula exhibit a high affinity to the central

pos: Lumican it bind to collagen molecules within a collagen fibril, thus helping keep adjacent fibrils apart. Lumican is a major keratan sulfate proteoglycan of the cornea but is ubiquitously distributed in most mesenchymal tissues throughout the body. Lumican is involved in collagen fibril organization and circumferential growth, corneal transparency, and epithelial cell migration and tissue repair. Corneal transparency is possible due to the exact alignment of collagen fibers by lumican (and keratocan) in the intrafibrillar space. Mice that have the lumican gene knocked out (Lum-/-) develop opacities of the cornea in both eyes and fragile skin. The lumican (LUM) gene was

pos: Self-healing hydrogels skin components. Biological Hydrogels: Biological hydrogels are derived from preexisting components of body tissues such as collagen, hyaluronic acid (HA), or fibrin. Collagen, HA, and fibrin are components that occur naturally in the extracellular matrix of mammals. Collagen is the main structural component in tissues and it already contains cell-signaling domains that can promote cell growth. In order to mechanically enhance collagen into a hydrogel, it must be chemically crosslinked, crosslinked using UV light or temperature, or mixed with other polymers. Collagen hydrogels would be nontoxic and biocompatible. Hybrid Hydrogels: Hybrid hydrogels combine synthetic and biological materials and take advantage

pos: Collagen the construction of the artificial skin substitutes used in the management of severe burns and wounds. These collagens may be derived from bovine, equine, porcine, or even human sources; and are sometimes used in combination with silicones, glycosaminoglycans, fibroblasts, growth factors and other substances. Collagen is one of the body’s key natural resources and a component of skin tissue that can benefit all stages of the wound healing process. When collagen is made available to the wound bed, closure can occur. Wound deterioration, followed sometimes by procedures such as amputation, can thus be avoided. Collagen is a natural product and

pos: Collagen hereditary link. Collagen is one of the long, fibrous structural proteins whose functions are quite different from those of globular proteins, such as enzymes. Tough bundles of collagen called "collagen fibers" are a major component of the extracellular matrix that supports most tissues and gives cells structure from the outside, but collagen is also found inside certain cells. Collagen has great tensile strength, and is the main component of fascia, cartilage, ligaments, tendons, bone and skin. Along with elastin and soft keratin, it is responsible for skin strength and elasticity, and its degradation leads to wrinkles that accompany aging. It

pos: Matrix metalloproteinase (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense. They were first described in vertebrates (1962), including humans, but have since been found in invertebrates and plants. They are distinguished from other endopeptidases by their dependence on metal ions as cofactors, their ability to degrade extracellular matrix, and their specific evolutionary DNA sequence. MMPs were described initially by Jerome Gross and Charles Lapiere (1962), who observed enzymatic activity (collagen triple helix degradation) during tadpole tail metamorphosis (by placing a tadpole tail in a collagen matrix plate). Therefore, the enzyme was named interstitial collagenase (MMP-1). Later, it was purified from human skin (1968),

pos: Surgical management of fecal incontinence procedure can be carried out under local anesthetic on an out patient basis. Many different materials have been used as perianal injectable bulking agents, including: autologous fat (fat tissue transferred from elsewhere in the body), Teflon, bovine glutaraldehyde cross-linked collagen (collagen from cows), carbon-coated zirconium beads, polydimethylsiloxane elastomer, dextranomer/non-animal stabilised hyaluronic acid, hydrogel cross-linked with polyacrylamide, porcine dermal collagen (collagen from pig skin), and synthetic calcium hydroxylapatite ceramic microspheres. Dextranomer in stabilised hyaluronic acid improves continence for a little over half of patients in the short term. However, future trials are required. Dextranomer is marketed as Solesta, bio-compatible Silicone is

pos: Anatomical terms of muscle Anatomical terms of muscle Muscles are described using unique anatomical terminology according to their actions and structure. There are three types of muscle tissue in the human body: skeletal, smooth, and cardiac. Skeletal striated muscle, or "voluntary muscle", primarily joins to bone with tendons. Skeletal muscle enables movement of the bones of the human skeleton and maintains posture. Smooth muscle tissue is found in parts of the body where it conveys action without conscious intent. The majority of this type of muscle tissue is found in the digestive and urinary systems where it acts by propelling forward food, chyme, and

neg: Kniest dysplasia The fetus had an abnormal spine, shortened long bones and a left clubfoot. After running postmortem tests and ultrasound, the researchers believed that the fetus suffered from hypochondrogenesis. Hypochondrogenesis is caused when type II collagen is abnormally formed due to a mutation in the COL2A1 gene. Normally, the cartilaginous notochord develops into the bony vertebrae in a human body. The COL2A1 gene results in malformed type II collagen, which is essential in the transition from collagen to bone. This is the first time that researchers found a persistent notochord in a human body due to a COL2A1 mutation. It is

neg: Dermal fibroblast tests found that fibrin adhesives even at its intended medical concentration (29 mg/mL at the wound site) had shear strength of only 17.6 kiloPascals. Furthermore, another study performed at the University of California determined that the modulus (the stress/strain) of fibrin adhesives was on average 53.56 kPA. To seal together tissues the human body uses collagen and elastin to obtain superior shear strength. Type I collagen which includes collagen strands bundled into strong fibrils has a unique tri-helical structure which increases the proteins structural integrity. In fact, a study performed by the Department of Medicine in University College London experimentally

neg: Lysine of this article, lysine will refer to the biologically active enantiomer L-lysine, where the α-carbon is in the S configuration. The human body cannot synthesize lysine, so it is essential in humans and must be obtained from the diet. In organisms that synthesise lysine, it has two main biosynthetic pathways, the diaminopimelate and α-aminoadipate pathways, which employ different enzymes and substrates and are found in different organisms. Lysine catabolism occurs through one of several pathways, the most common of which is the saccharopine pathway. Lysine plays several roles in humans, most importantly proteinogenesis, but also in the crosslinking of collagen

neg: Fibrillogenesis represents the most abundant collagen found within various collagen fibrils There are immense differences in the types of collagen fibrils that exist within the body. For instance, fibrils within the tendon vary in width and are banded into aggregates that form fibril bundles that resist forces of tension within one dimension. Similarly, fibrils that form the translucent corneal stromal matrix form orthogonal sheets and withstand the force of traction in two dimensions. Remarkably, these two structurally different collagen fibrils are speculated to be formed from the same molecules with Collagen I being the primary collagen found within both structures. There

neg: Capsular contracture Capsular contracture Capsular contracture is a response of the immune system to foreign materials in the human body. Medically, it occurs mostly in context of the complications from breast implants and artificial joint prosthetics. The occurrence of capsular contraction follows the formation of capsules of tightly-woven collagen fibers, created by the immune response to the presence of foreign objects surgically installed to the human body, e.g. breast implants, artificial pacemakers, orthopedic prostheses; biological protection by isolation and toleration. Capsular contracture occurs when the collagen-fiber capsule shrinks, tightens and compresses the breast implant, much like the collapse of a bubble gum

neg: Collagen, type II, alpha 1 Collagen, type II, alpha 1 Collagen, type II, alpha 1 (primary osteoarthritis, spondyloepiphyseal dysplasia, congenital), also known as COL2A1, is a human gene that provides instructions for the production of the pro-alpha1(II) chain of type II collagen. This gene encodes the alpha-1 chain of type II collagen, a fibrillar collagen found in cartilage and the vitreous humor of the eye. Mutations in this gene are associated with achondrogenesis, chondrodysplasia, early onset familial osteoarthritis, SED congenita, Langer-Saldino achondrogenesis, Kniest dysplasia, Stickler syndrome type I, and spondyloepimetaphyseal dysplasia Strudwick type. In addition, defects in processing chondrocalcin, a calcium binding protein that is

neg: Alport syndrome by mutations in "COL"4A3, "COL4A4", and "COL4A5", three of six human genes involved in basement membrane (type IV) collagen biosynthesis. Mutations in any of these genes prevent the proper production or assembly of the specialised type IV collagen '345' network found in the glomerulus, which is an important structural component of basement membranes in the kidney, inner ear, and eye. It is also found in other locations, including the alveoli of the lungs. Basement membranes are thin, sheet-like structures that separate and support cells in many tissues. Type IV collagen '112' type is found in both vertebrates and invertebrates, and

neg: Extracellular matrix the most abundant protein in the human body and accounts for 90% of bone matrix protein content. Collagens are present in the ECM as fibrillar proteins and give structural support to resident cells. Collagen is exocytosed in precursor form (procollagen), which is then cleaved by procollagen proteases to allow extracellular assembly. Disorders such as Ehlers Danlos Syndrome, osteogenesis imperfecta, and epidermolysis bullosa are linked with genetic defects in collagen-encoding genes. The collagen can be divided into several families according to the types of structure they form: Elastins, in contrast to collagens, give elasticity to tissues, allowing them to stretch when

neg: Heat shock protein 47 Heat shock protein 47 Heat shock protein 47, also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen. This protein is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. HSP47 is expressed by cells present in Endoplasmic Reticulum. These cells synthesize and secrete type I and type II collagen. The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients

neg: Dense regular connective tissue Dense regular connective tissue Dense regular connective tissue provides connection between different tissues in the human body. The collagen fibers in dense regular connective tissue are bundled in a parallel fashion. Dense regular connective tissue (DRCT) is divided into white fibrous connective tissue and yellow fibrous connective tissue, both of which occur in two forms: cord arrangement and sheet arrangement. In cord arrangement bundles of collagen and matrix are distributed in regular alternate patterns. In sheet arrangement collagen bundles and matrix are distributed in irregular patterns, sometimes in the form of a network. It is similar to areolar tissue, but

neg: Matrix (biology) glycoprotein in the ECM of most animal cells is collagen, which forms strong fibers outside the cells. In fact, collagen accounts for about 40% of the total protein in the human body. The collagen fibers are embedded in a network woven from proteoglycans. A proteoglycan molecule consists of a small core protein with many carbohydrate chains covalently attached, so that it may be up to 95% carbohydrate. Large proteoglycan complexes can form when hundreds of proteoglycans become noncovalently attached to a single long polysaccharide molecule. Some cells are attached to the ECM by still other ECM glycoproteins such as fibronectin.

neg: Lapa do Santo specific body parts when analyzed against Food Utility Index (FUI). The game was not dismembered in the killing site, but brought as entire piece to the dwelling camp. Carbon and nitrogen stable isotope analysis on bone collagen is widely used in archaeology for reconstructing ancient diets. A total of 17 human bones and 51 faunal bones from the early Holocene deposits of Lapa do Santo were analysed with this technique. Due to poor preservation conditions only eight human from Lapa do Santo and 22 faunal samples from Lagoa Santa provided collagen with an acceptable C:N ratio between 2.9 and 3.6.

neg: Glutaric aciduria type 1 a necessary cofactor for the utilization of lysine in collagen synthesis. Collagen, the most abundant protein in the human body, requires great amounts of lysine, the most abundant amino acids in proteins. Ascorbic acid, the main hydroxyl radical quencher, works as the cofactor providing the hydroxyl radical required to collagen cross-linking; lysine thus becomes hydroxylysine. GA1 worsens during stresses and catabolic episodes, such as fasts and infections. Endogenous catabolism of proteins could be an important route for glutaric acid production. It thus follows that collagen breakdown (and protein breakdown in general) should be prevented by all possible means. Ascorbic acid

neg: Polycaprolactone the Food and Drug Administration (FDA) in specific applications used in the human body as (for example) a drug delivery device, suture (sold under the brand name Monocryl or generically), or adhesion barrier.] PCL is used in the rapidly growing field of human esthetics following the recent introduction of a PCL-based microsphere dermal filler belonging to the collagen stimulator class (Ellansé). Through the stimulation of collagen production, PCL-based products are able to correct facial ageing signs such as volume loss and contour laxity, providing an immediate and long-lasting natural effect. It is being investigated as a scaffold for tissue repair

neg: Fibrillogenesis Fibrillogenesis Fibrillogenesis is the development of fine fibrils normally present in collagen fibers of connective tissue. It is derived from the Greek "fibrillo" (meaning fibrils, or pertaining to fibrils) and "genesis" (to create, the process by which something is created). The assembly of collagen fibrils, fibrillogenesis appears to be a self-assembly process although there is much speculation about the specifics of the mechanism through which the body produces collagen fibrils. In the body, collagen fibrils are composed of several types of collagen as well as macromolecules. Collagen I is the most abundant structural macromolecule within the vertebrate body and also

neg: Scar free healing wounds is due to the role of fibroblast cells. Fibroblasts are responsible for the synthesis of the ECM and collagen. In the fetus, fibroblasts are able to migrate at a faster rate than those found in the adult wound. Fetal fibroblasts can also proliferate and synthesize collagen simultaneously, in comparison to adult fibroblasts where collagen synthesis is delayed. It is this delay in both collagen deposition and migration, which is likely to contribute to formation of a scar in the adult. Proteins and cell surface receptors found in the ECM differ in fetal and adult wound healing. This is due

neg: Biglycan has been reported that biglycan interacts more strongly with collagen type II than collagen type I. Biglycan has been reported to compete with decorin for the same binding site on collagen. Biglycan has been shown to interact with SGCA. Biglycan is a particularly important proteoglycan for binding to lipoprotein in human blood vessels, thus being a significant cause of atherosclerosis. Biglycan Biglycan is a small leucine-rich repeat proteoglycan (SLRP) which is found in a variety of extracellular matrix tissues, including bone, cartilage and tendon. In humans, biglycan is encoded by the "BGN" gene which is located on the X chromosome.

neg: Bone resorption in the resorption process. High levels of calcium, magnesium, phosphate and products of collagen will be released into the extracellular fluid as the osteoclasts tunnel into the mineralized bone. Osteoclasts are prominent in the tissue destruction found in psoriatic arthritis and rheumatological disorders. The human body is in a constant state of bone remodeling. Bone remodelling is a process which maintains bone strength and ion homeostasis by replacing discrete parts of old bone with newly synthesized packets of proteinaceous matrix. Bone is resorbed by osteoclasts, and is deposited by osteoblasts in a process called ossification. Osteocyte activity plays a key

neg: Alport syndrome disease and 'nephritis'. Alport syndrome is caused by an inherited defect in type IV collagen—a structural material that is needed for the normal function of different parts of the body. Since type IV collagen is found in the ears, eyes, and kidneys, this explains why Alport syndrome affects different seemingly unrelated parts of the body (ears, eyes, kidneys, etc.). These descriptions refer to 'classic' Alport syndrome, which usually causes significant disease from young adult or late childhood life. Some individuals, usually with milder mutations or 'carrier' status, develop disease later, or show only some of the features of classic disease.

neg: Knobloch syndrome that a cone-rod pattern of dysfunction is also a feature. Knobloch syndrome is caused by mutations in an autosomal recessive inherited gene. These mutations have been found in the COL18A1 gene that instructs for the formation of a protein that builds collagen XVIII. This type of collagen is found in the basement membranes of various body tissues. Its deficiency in the eye is thought to be responsible for affecting normal eye development. There are two types of Knobloch syndrome and the case has been made for a third. When caused by mutations in the COL18A1 gene it is called Knobloch

neg: Hydroxyproline hydroxyproline comprises roughly 4% of all amino acids found in animal tissue, an amount greater than seven other amino acids that are translationally incorporated. Hydroxyproline is a major component of the protein collagen, comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. They permit the sharp twisting of the collagen helix. In the canonical collagen Xaa-Yaa-Gly triad (where Xaa and Yaa are any amino acid), a proline occupying the Yaa position is hydroxylated to give a Xaa-Hyp-Gly sequence. This modification of the proline residue increases the stability of the collagen triple helix. It was

neg: Composition of the human body arsenic, an element normally considered a toxin in higher amounts, is essential in ultratrace quantities, in mammals such as rats, hamsters, and goats. Some elements (silicon, boron, nickel, vanadium) are probably needed by mammals also, but in far smaller doses. Bromine is used abundantly by some (though not all) lower organisms, and opportunistically in eosinophils in humans. One study has found bromine to be necessary to collagen IV synthesis in humans. Fluorine is used by a number of plants to manufacture toxins (see that element) but in humans only functions as a local (topical) hardening agent in tooth enamel, and

neg: Collagen, type III, alpha 1 studies have reported on mosaicism, where one of the parents carries the mutation in some of her or his cells, but not in all cells, and appears phenotypically healthy, but has more than one affected offspring. Inactivation of the murine Col3a1 gene led to a shorter life span in homozygous mutant mice. The mice died prematurely from a rupture of major arteries mimicking the human vEDS phenotype. Collagen, type III, alpha 1 Collagen alpha-1(III) chain also known as alpha 1 chain of type III collagen is a protein that in humans is encoded by the "COL3A1" gene. Three of these

neg: Osteoarthritis collagen (uCTX-II) as a prognostic marker for knee osteoarthritis progression and serum cartilage oligomeric matrix protein (COMP) levels as a prognostic marker for incidence of both knee and hip osteoarthritis. A review of biomarkers in hip osteoarthritis also found associations with uCTX-II. Procollagen type II C-terminal propeptide (PIICP) levels reflect type II collagen synthesis in body and within joint fluid PIICP levels can be used as a prognostic marker for early osteoarthritis. One problem with using a specific type II collagen biomarker from the breakdown of articular cartilage is that the amount of cartilage is reduced (worn away) over time

neg: Osteogenesis imperfecta Type-I collagen. This deficiency arises from an amino acid substitution of glycine to bulkier amino acids in the collagen triple helix structure. The larger amino acid side-chains create steric hindrance that creates a bulge in the collagen complex, which in turn influences both the molecular nanomechanics and the interaction between molecules, which are both compromised. As a result, the body may respond by hydrolyzing the improper collagen structure. If the body does not destroy the improper collagen, the relationship between the collagen fibrils and hydroxyapatite crystals to form bone is altered, causing brittleness. Another suggested disease mechanism is that the

neg: Collagen, type XXIII, alpha 1 at the nucleotide level, human and rat collagen XXIII alpha 1 show 76% identity. Furthermore, cellular localization of collagen XXIII was determined by immunofluorescence staining, using an antibody that recognizes the carboxyl terminus of the protein. It was demonstrated that the carboxyl terminus of collagen XXIII is present on the cell surface. Human collagen α1(XXIII), which is a homotrimer, contains 540 amino acids distributed in: Collagen XXIII belongs to the transmembranous subfamily of collagens. Proteins which are included in this group present an amino-terminal cytoplasmic domain followed by a membrane-spanning hydrophobic domain and at least one extracellular triple-helical collagenous domain

neg: Precambrian body plans the many types of collagens, only the fibrillar and the basement membrane (type IV) collagens have been found in the sponges and cnidarians, which are the two earliest branching metazoan lineages. Studies have focused on the origin of fibrillar collagen molecules. In Sponges, there exist three clades of fibrillar molecules, A, B and C. It is proposed that only the B clade fibrillar collagens preserved their characteristic modular structure from sponge to human. In mammals, the fibrillar collagens involved in the formation of cross-striated fibrils are types I–III, V, and XI. Type II and type XI collagens compose the fibrils

neg: Gnathostoma spinigerum flat spines, which become sparser and single-tipped further toward the end. Behind a bare region that constitutes roughly half of the body length, many small spines can be found on the posterior tip. the four species gnathostomiasis--"G. doloresi", "G. hispidum", "G. nipponicum", and "G. spinigerum" can cause human –these species are differences in these external appearance and third larvae stage which is helpful for identification. As a nematode, "Gnathostoma spinigerum" has cylindrical, a cuticle layer with three main outer layers made of collagen and other compounds. The outer layers are non-cellular and are secreted by the epidermis. The cuticle layer

neg: Human tooth development created in the adjacent area. Throughout the body, cells that form bone are called osteoblasts. In the case of alveolar bone, these osteoblast cells form from the dental follicle. Similar to the formation of primary cementum, collagen fibers are created on the surface nearest the tooth, and they remain there until attaching to periodontal ligaments. Like any other bone in the human body, alveolar bone is modified throughout life. Osteoblasts create bone and osteoclasts destroy it, especially if force is placed on a tooth. As is the case when movement of teeth is attempted through orthodontics using bands, wires, or

neg: Durotaxis of many tissues in the human body. The stiffness of animal tissues varies over several orders of magnitude, for example: Matrices of varying stiffness are commonly engineered for experimental and therapeutic purposes (e.g. collagen matrices for wound healing). Durotactic gradients are simply made by creating 2-dimensional substrates out of polymer (e.g. acrylamide or polydimethylsiloxane) in which the stiffness is controlled by cross-linking density, which in turn is controlled by cross-linker concentration. The polymer must be coated with a material that the cell can adhere to, such as collagen or fibronectin. The gradients themselves are often synthesized as hydrogels using microfluidic

neg: Procollagen-proline dioxygenase favorably with the proline-rich substrate. The active site consists of Fe2+ bound to two histidine residues and one aspartate residue, a characteristic shared by most 2-oxoglutarate-dependent dioxygenases. The 55 kDa β subunit is responsible for the enzyme’s localization to and retention in the endoplasmic reticulum. This subunit is identical to the enzyme known as protein disulfide isomerase. Prolyl hydroxylase catalyzes the formation of hydroxyproline, which is the most abundant post-translational modification in human body. The modification has a significant impact on the stability of collagen, the major connective tissue of the human body. Specifically, hydroxylation increases the melting temperature (T)

neg: Scar the damage, a clot is created; the clot is the beginning process that results in a provisional matrix. In the process, the first layer is a provisional matrix and is not scar. Over time, the wounded body tissue then overexpresses collagen inside the provisional matrix to create a collagen matrix. This collagen overexpression continues and crosslinks the fiber arrangement inside the collagen matrix, making the collagen dense. This densely packed collagen, morphing into an inelastic whitish collagen scar wall, blocks off cell communication and regeneration; as a result, the new tissue generated will have a different texture and quality than

neg: Nataruk Late Pleistocene age." Antoine Zazzo has since carried out radiocarbon dating of the human remains using apatite, although he stresses the ages obtained should be treated with caution "...because the reliability of the reference age, a bone collagen sample dated in the late 60's or very early 70's, i.e.well before the advent of modern purification techniques, and in a site where collagen preservation is very poor, remains questionable." Nevertheless, the combination of the dates obtained by Antoine, and Wendorf's own assessment of the likely age of the remains, are a strong indication that the age of the human remains in

neg: Collagen 4,000 years ago, and Native Americans used it in bows about 1,500 years ago. The oldest glue in the world, carbon-dated as more than 8,000 years old, was found to be collagen—used as a protective lining on rope baskets and embroidered fabrics, and to hold utensils together; also in crisscross decorations on human skulls. Collagen normally converts to gelatin, but survived due to dry conditions. Animal glues are thermoplastic, softening again upon reheating, so they are still used in making musical instruments such as fine violins and guitars, which may have to be reopened for repairs—an application incompatible with tough,

neg: Tumstatin similar to that of endostatin, which is cleaved from collagen XVIII. The two proteins share 14% amino acid identity, making them very similar in structure. It has been proven to inhibit many types of cells, including bovine endothelial cells, HeLa cells, endothelial cells, and Human umbilical vein endothelial cells (HUVEC) cells. The tumstatin fragment is cleaved by matrix metalloproteinase-9 (MMP) at the alpha chain on the collagen strand. Tumstatin interacts with the αvβ3 integrin found in the apoptosis pathway. There are two activation sites on the tumstatin fragment. One is at the N-terminus and is responsible for inhibiting angiogenesis. The

neg: Chondrocalcin Chondrocalcin Chondrocalcin comes from a family of pro-collagen molecules. This protein is found in the bone and is involved in calcium-binding, which occurs in order to harden (or calcify) the cartilage. Another one of its roles is to assemble the triple collagen helix, which is predominately entails the linkage of glycine and proline amino acids and then the twisting of those linkages. Chondrocalcin is important because cartilage calcification of the growth plate is one of the main occurrences in endochondral bone formation. Because of its importance, it is one of the most highly created polypeptides in human cartilage. This calcium-binding

neg: Procollagen-proline dioxygenase of helical collagen by 16 °C, as compared to unhydroxylated collagen, a difference that allows the protein to be stable at body temperature. The enzyme acts specifically on proline contained within the X-Pro-Gly motif – where Pro is proline. Because of this motif-specific behavior, the enzyme also acts on other proteins that contain this same sequence. Such proteins include C1q, elastins, PrP, Argonaute 2, and conotoxins, among others. As prolyl hydroxylase requires ascorbate as a cofactor to function, its absence compromises the enzyme’s activity. The resulting decreased hydroxylation leads to the disease condition known as scurvy. Since stability of collagen

neg: Isotopes of carbon different plants will affect the δC values in the consumer's body tissues. If an animal (or human) eats only C3 plants, their δC values will be from −18.5 to −22.0‰ in their bone collagen and −14.5‰ in the hydroxylapatite of their teeth and bones. In contrast, C4 feeders will have bone collagen with a value of −7.5‰ and hydroxylapatite value of −0.5‰. In actual case studies, millet and maize eaters can easily be distinguished from rice and wheat eaters. Studying how these dietary preferences are distributed geographically through time can illuminate migration paths of people and dispersal paths of different

neg: Bone arrival, active enzymes, such as tartrate resistant acid phosphatase, are secreted against the mineral substrate. The reabsorption of bone by osteoclasts also plays a role in calcium homeostasis. Bones consist of living cells embedded in a mineralized organic matrix. This matrix consists of organic components, mainly type I collagen – "organic" referring to materials produced as a result of the human body – and inorganic components, primarily hydroxyapatite and other salts of calcium and phosphate. Above 30% of the acellular part of bone consists of the organic components, and 70% of salts. The collagen fibers give bone its tensile strength,

neg: Implantation (human embryo) Type-I collagen, Type-II collagen, Type-III collagen, Type-VII collagen and Type-X collagen. The gelatinases exist in two forms; one digesting Type-IV collagen and one digesting gelatin. The embryo differs from the cells of the mother, and would be rejected as a parasite by the immune system of the mother if it didn't secrete immunosuppressive agents. Such agents are Platelet-activating factor, human chorionic gonadotropin, early pregnancy factor, immunosuppressive factor, Prostaglandin E2, Interleukin 1-alpha, Interleukin 6, interferon-alpha, leukemia inhibitory factor and Colony-Stimulating Factor. Factors from the blastocyst also trigger the final formation of decidual cells into their proper form. In contrast, some decidual

neg: Collagen receptor Collagen receptor Collagen receptors are membrane proteins that bind the extracellular matrix protein collagen, the most abundant protein in mammals. They control mainly cell proliferation, migration and adhesion, coagulation cascade activation and they affect ECM structure by regulation of MMP (matrix metalloproteinases). There are at least eight human collagen receptors belonging to four different classes. Integrins function as the major cell receptor for extracellular matrix protein. These an receptors comprise an α and β transmembrane subunit, which are noncovalently bound. Collagen binding is primarily provided by integrins α1β1, α2β1, α10β1 and α11β1. Integrin α1β1 binds to collagen via the MIDAS

neg: Fibril and collagen V are essential for collagen I forming and collagen XI for collagen II forming. Therefore, cellular mechanisms play key role in the protein self-assembly process. Collagen is the major structural protein outside cells in many connective tissues of animals. As the primary component of connective tissue, it has the largest amount among protein in mammals, occupying 25% to 35% of the all protein content in body. The fibrils in collagen are packed in a crimp structure. The stress/strain curve of collagen, such as tendon, can be subdivided into several regions. The region of small strains,"toe"region, corresponds to the

neg: Gelatin Gelatin Gelatin or gelatine (from meaning "stiff" or "frozen") is a translucent, colorless, brittle (when dry), flavorless food ingredient that is derived from collagen obtained from various animal body parts. It is also referred to as hydrolyzed collagen, collagen hydrolysate, gelatine hydrolysate, hydrolyzed gelatine, and collagen peptides. It is commonly used as a gelling agent in food, medications, drug and vitamin capsules, photographic films and papers, and cosmetics. Substances containing gelatin or functioning in a similar way are called "gelatinous". Gelatin is an irreversibly hydrolyzed form of collagen, wherein the hydrolysis results in the reduction of protein fibrils into smaller

neg: Collagen, type II, alpha 1 fibrils that cross-link to one another in the spaces around cells. The cross-linkages result in the formation of very strong mature type II collagen fibers. The COL2A1 gene is located on the long (q) arm of chromosome 12 between positions 13.11 and 13.2, from base pair 46,653,017 to base pair 46,684,527. Collagen, type II, alpha 1 Collagen, type II, alpha 1 (primary osteoarthritis, spondyloepiphyseal dysplasia, congenital), also known as COL2A1, is a human gene that provides instructions for the production of the pro-alpha1(II) chain of type II collagen. This gene encodes the alpha-1 chain of type II collagen, a fibrillar

neg: Collagen, type XXIII, alpha 1 the brain where the shed form is predominant, whereas in the lungs the molecule is generally found as the full-length form. It has been reported that the cell is able to regulate the amounts of collagen XXIII in the membrane-bound form and in the secreted shed form, influencing the production of one form or the other when it is needed. For that reason, the shedding process of collagen XXIII has been described as a selective proteolysis, carried out principally by furin, although there are other enzymes, like serine and cysteine proteases, which are able to shed the molecule too. When

neg: Weissenbacher–Zweymüller syndrome no history of the disorder in the family. The COL11A2 gene is responsible for providing instructions on making one component of the type XI collagen. Type XI collagen is a complex molecule that helps give structure and strength to the connective tissues. Collagen is found in bone. It is also found in cartilage that makes up most of the skeleton during early development. The mutation of COL11A2 in Weissenbacher-Zweymüller syndrome disrupts the assembly of the type XI collagen molecules. The malfunctioning collagen weakens the connective tissue causing impaired bone development. COL11A2 is also associated with autosomal dominant non-syndromic hearing loss

neg: Type IV collagen associated with the extent of renal injury. Type IV collagen Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. These two features cause the collagen to form in a sheet, the form of the basal lamina. Collagen IV is the more common usage, as

neg: Type IV collagen Type IV collagen Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. These two features cause the collagen to form in a sheet, the form of the basal lamina. Collagen IV is the more common usage, as opposed to the older terminology of "type-IV

neg: TMEM106C is in between COL2A1, the human type II collagen gene, and VDR, the human Vitamin D Receptor gene. This protein is found to be an integral part of the endoplasm reticulum membrane. The TMEM106A protein has a molecular weight of 27.9 kdal with a PI of 6.325. It has 250 amino acids, 230 of which are in the domain of unknown function. No signal peptide has been found for this protein but TMEM106C has transmembrane regions which gives evidence for an internal signal peptide. This protein spans the ER membrane 2 times. There is evidence that these transmembrane regions take

neg: Fibrillogenesis is no concrete evidence or agreement on the exact mechanisms of Fibrillogenesis, however, multiple hypotheses based on primary research put forth various mechanisms to consider. Collagen fibrillogenesis occurs in the plasma membrane during embryonic development. Collagen within the body has a denaturation temperature between 32-40 degrees Celsius, the physiological temperature also falls within this range and thereby poses a significant problem. It is therefore a mystery how collagen survives within the tissues in order to yield itself to the formation of collagen fibrils. A postulated solution to the problem of denaturation based on current research, is that newly formed collagen

neg: Porphyromonas gingivalis Porphyromonas gingivalis Porphyromonas gingivalis belongs to the phylum Bacteroidetes and is a nonmotile, Gram-negative, rod-shaped, anaerobic, pathogenic bacterium. It forms black colonies on blood agar. It is found in the oral cavity, where it is implicated in certain forms of periodontal disease, as well as in the upper gastrointestinal tract, the respiratory tract, and the colon. It has also been isolated from women with bacterial vaginosis. Collagen degradation observed in chronic periodontal disease results in part from the collagenase enzymes of this species. It has been shown in an "in vitro" study that "P. gingivalis" can invade human gingival fibroblasts

neg: Collagen, type VI, alpha 3 Collagen, type VI, alpha 3 Collagen alpha-3(VI) chain is a protein that in humans is encoded by the "COL6A3" gene. This protein is an alpha chain of type VI collagen that aids in microfibril formation. As part of type VI collagen, this protein has been implicated in Bethlem myopathy, Ullrich congenital muscular dystrophy (UCMD), and other diseases related to muscle and connective tissue. This gene encodes the alpha 3 chain, one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective tissues. The alpha 3 chain of type VI collagen is much larger

neg: Wound healing wound healing biology is to induce a more perfect reconstruction of the wound area. Scarless wound healing only occurs in mammalian foetal tissues and complete regeneration is limited to lower vertebrates, such as salamanders, and invertebrates. In adult humans, injured tissue are repaired by collagen deposition, collagen remodelling and eventual scar formation, where fetal wound healing is believed to be more of a regenerative process with minimal or no scar formation. Therefore, foetal wound healing can be used to provide an accessible mammalian model of an optimal healing response in adult human tissues. Clues as to how this might be

neg: Type IV collagen collagen". Collagen IV exists in all metazoan phyla. There are six human genes associated with it: The alpha-3 subunit (COL4A3) of collagen IV is thought to be the antigen implicated in Goodpasture's disease, wherein the immune system attacks the basement membranes of the glomeruli and the alveoli upon the antigenic site on the alpha-3 subunit becomes unsequestered due to environmental exposures. Goodpasture's disease presents with nephritic syndrome and hemoptysis. Microscopic evaluation of biopsied renal tissue will reveal linear deposits of Immunoglobulin G by immunofluorescence. This is classically in young adult males. Mutations to the genes coding for collagen IV lead

neg: Spondyloperipheral dysplasia that fills the vitreous humour (the eyeball). Type II collagen is essential for the normal development of bones and other connective tissues (the tissues that form the body's supportive framework). Mutations in the "COL2A1" gene interfere with the assembly of type II collagen molecules. The protein made by the altered "COL2A1" gene cannot be used to make type II collagen, resulting in a reduced amount of this type of collagen in the body. Instead of forming collagen molecules, the abnormal protein builds up in cartilage cells (chondrocytes). These changes disrupt the normal development of bones, leading to the signs and

neg: Amino acid proteins known as alloproteins incorporating non-proteinogenic amino acids. Many important proteinogenic and non-proteinogenic amino acids have biological functions. For example, in the human brain, glutamate (standard glutamic acid) and gamma-amino-butyric acid ("GABA", non-standard gamma-amino acid) are, respectively, the main excitatory and inhibitory neurotransmitters. Hydroxyproline, a major component of the connective tissue collagen, is synthesised from proline. Glycine is a biosynthetic precursor to porphyrins used in red blood cells. Carnitine is used in lipid transport. Nine proteinogenic amino acids are called "essential" for humans because they cannot be produced from other compounds by the human body and so must be taken

neg: Collagenase Collagenase Collagenases are enzymes that break the peptide bonds in collagen. They assist in destroying extracellular structures in the pathogenesis of bacteria such as "Clostridium". They are considered a virulence factor, facilitating the spread of gas gangrene. They normally target the connective tissue in muscle cells and other body organs. Collagen, a key component of the animal extracellular matrix, is made through cleavage of pro-collagen by collagenase once it has been secreted from the cell. This stops large structures from forming inside the cell itself. In addition to being produced by some bacteria, collagenase can be made by the body

neg: Polyol pathway reactions throughout the body, and under normal conditions they are "not" interchangeable. The decreased concentration of these NADPH leads to decreased synthesis of reduced glutathione, nitric oxide, myo-inositol, and taurine. Myo-inositol is particularly required for the normal function of nerves. Sorbitol may also glycate nitrogens on proteins, such as collagen, and the products of these glycations are referred-to as AGEs - advanced glycation endproducts. AGEs are thought to cause disease in the human body, one effect of which is mediated by RAGE (receptor for advanced glycation endproducts) and the ensuing inflammatory responses induced. They are seen in the hemoglobin A1C

neg: Cardiac skeleton with the central fibrous body. This is the strongest part of the fibrous cardiac skeleton. The upper chambers (atria) and lower (ventricles) are electrically divided by the properties of collagen proteins within the rings. The valve rings, central body and skeleton of the heart consisting of collagen are impermeable to electrical propagation. The only channel allowed (barring accessory/rare preexcitation channels) through this collagen barrier is represented by a sinus that opens up to the atrioventricular node and exits to the bundle of His. The muscle origins/insertions of many of the cardiomyocytes are anchored to opposite sides of the valve rings.

neg: Collagen receptor on fibroblasts, endotelial cells and macrophages. Vogel, W.F., 2001. Collagen-receptor signaling in health and disease. European Journal of Dermatology 11, 506-514. White, D.J., Puranen, S., Johnson, M.S., Heino, J., 2004. The collagen receptor subfamily of the integrins. International Journal of Biochemistry & Cell Biology 36, 1405-1410. Collagen receptor Collagen receptors are membrane proteins that bind the extracellular matrix protein collagen, the most abundant protein in mammals. They control mainly cell proliferation, migration and adhesion, coagulation cascade activation and they affect ECM structure by regulation of MMP (matrix metalloproteinases). There are at least eight human collagen receptors belonging to four different

neg: Sea cucumber "bivium". A remarkable feature of these animals is the "catch" collagen that forms their body wall. This can be loosened and tightened at will, and if the animal wants to squeeze through a small gap, it can essentially liquefy its body and pour into the space. To keep itself safe in these crevices and cracks, the sea cucumber will hook up all its collagen fibers to make its body firm again. The most common way to separate the subclasses is by looking at their oral tentacles. Order Apodida have a slender and elongate body lacking tube feet, with up to

neg: Collagen, type XXIII, alpha 1 Collagen, type XXIII, alpha 1 Collagen α-1 (XXIII) chain is a protein encoded by COL23A1 gene, which is located on chromosome 5q35 in humans, and on chromosome 11B1+2 in mice. The location of this gene was discovered by genomic sequence analysis. Collagen XXIII is a type II transmembrane protein and the fourth in the subfamily of non-fibrillar transmembranous collagens. This kind of collagens have a single pass hydrophobic transmembrane domain. The molecule of collagen XXIII can be found either in membrane-bond form or in shed form. Type XXIII collagen is expressed in both adult tissues and developing organs. It can

neg: Larsen syndrome gene that codes for filamin B. These mutations cause an accelerated rate of apoptosis in the epiphyseal growth plates of individuals with the mutation. The defects can cause short stature and other symptoms associated with Larsen syndrome. Genetic analysis has found that a gene linked to Larsen syndrome, "LAR1", is strongly linked to chromosome 3p markers. The locus of this gene is found in a region defined distally by D3S1581 and proximally by D3S1600. This location can be mapped to chromosome region 3p21.1-14.1. Human type VII collagen gene is found within this region in chromosome region 3p21.1. It is reasonable

neg: Collagen, type VI, alpha 2 identified for this gene. Collagen, type VI, alpha 2 Collagen alpha-2(VI) chain is a protein that in humans is encoded by the "COL6A2" gene. This gene encodes one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective tissues. The product of this gene contains several domains similar to von Willebrand Factor type A domains. These domains have been shown to bind extracellular matrix proteins, an interaction that explains the importance of this collagen in organizing matrix components. Mutations in this gene are associated with Bethlem myopathy and Ullrich scleroatonic muscular dystrophy. Three

neg: Collagen, type VI, alpha 2 Collagen, type VI, alpha 2 Collagen alpha-2(VI) chain is a protein that in humans is encoded by the "COL6A2" gene. This gene encodes one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective tissues. The product of this gene contains several domains similar to von Willebrand Factor type A domains. These domains have been shown to bind extracellular matrix proteins, an interaction that explains the importance of this collagen in organizing matrix components. Mutations in this gene are associated with Bethlem myopathy and Ullrich scleroatonic muscular dystrophy. Three transcript variants have been

neg: Larsen syndrome the structure and activity of the cytoskeleton. The gene that influences the emergence of Larsen syndrome is found in chromosome region, 3p21.1-14.1, a region containing human type VII collagen gene. Larsen syndrome has recently been described as a mesenchyme disorder that affects the connective tissue of an individual. Autosomal dominant and recessive forms of the disorder have been reported, although most cases are autosomal dominant. Reports have found that in Western societies, Larsen syndrome can be found in one in every 100,000 births, but this is most likely an underestimate because the disorder is frequently unrecognized or misdiagnosed. Symptoms are

neg: Collagen, type IV, alpha 1 This report of a new mutation in the COL4A1 gene is the first report of a non-syndromic autosomal dominant congenital cataract that highlights an important role for collagen type IV in the physiological and optical properties of the lens. Additionally, in the cardiovascular field, the COL4A1 and COL4A2 regions on chromosome 13q34 are a highly replicated locus for coronary artery disease. In a normal wall of arteries, collagen type IV acts to inhibit smooth muscle cell proliferation. Accordingly, it was demonstrated that protein expression of collagen type IV in human vascular smooth muscle cells is regulated by both SMAD3 protein

neg: Collagen These two amino acids help stabilize the triple helix—Hyp even more so than Pro; a lower concentration of them is required in animals such as fish, whose body temperatures are lower than most warm-blooded animals. Lower proline and hydroxyproline contents are characteristic of cold-water, but not warm-water fish; the latter tend to have similar proline and hydroxyproline contents to mammals. The lower proline and hydroxproline contents of cold-water fish and other poikilotherm animals leads to their collagen having a lower thermal stability than mammalian collagen. This lower thermal stability means that gelatin derived from fish collagen is not suitable for