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The International Red Cross wound classification system is a system whereby certain features of a wound are scored: the size of the skin wound(s); whether there is a cavity, fracture or vital structure injured; the presence or absence of metallic foreign bodies. A numerical value is given to each feature (E, X, C, F, V, and M).
Collagen alpha-1(VIII) chain is a protein that in humans is encoded by the COL8A1 gene. [5] [6] This gene encodes one of the two alpha chains of type VIII collagen. The gene product is a short chain collagen and a major component of the basement membrane of the corneal endothelium. The type VIII collagen fibril can be either a homo- or a ...
Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen". [citation needed] Collagen IV exists in all metazoan phyla, to whom they served as an evolutionary stepping stone to multicellularity. [1] There are six human genes associated with it: [2] COL4A1, COL4A2, COL4A3, COL4A4, COL4A5, COL4A6
Collagen (/ ˈ k ɒ l ə dʒ ə n /) is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, [1] making up 25% to 35% of protein content. Amino acids are bound together to form a triple helix of elongated fibril [2] known as a collagen helix.
1278 12843 Ensembl ENSG00000164692 ENSMUSG00000029661 UniProt P08123 Q01149 RefSeq (mRNA) NM_000089 NM_007743 RefSeq (protein) NP_000080 NP_031769 Location (UCSC) Chr 7: 94.39 – 94.43 Mb Chr 6: 4.5 – 4.54 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Collagen alpha-2(I) chain is a protein that in humans is encoded by the COL1A2 gene. This gene encodes one of the chains for type ...
Type V Collagen is considered a regulatory fibril forming collagen. [5] Collagen V is associated with the COL5A1 gene which is the gene which provides instructions to produce Collagen V. Type V Collagen, like other collagens, is made up of procollagen molecules. Collagen V molecular isoforms are α1(V)α2(V)α3(V), α1(V)3, and α1(V)2 α2(V).
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 one case, however, a particular type of collagen graft led to significant delay of wound closure. [6] Careful study of histology samples revealed that grafts that delayed wound closure induced the synthesis of new dermis de novo at the injury site, instead of forming scar, which is the normal outcome of the spontaneous wound healing response.