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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 ...
Schematic of a CHP strand (labeled with an "X" tag) hybridizing to denatured collagen chains and forming a collagen triple helix. During disease progression, tissue development, or ageing, collagen can be extensively degraded by collagenolytic proteases, causing its triple helix to unfold at the physiological temperature due to reduced thermal stability.
Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinophilic fibers known as collagen fibers, which make up most of the rope-like dense connective tissue in ...
1277 12842 Ensembl ENSG00000108821 ENSMUSG00000001506 UniProt P02452 P11087 RefSeq (mRNA) NM_000088 NM_007742 RefSeq (protein) NP_000079 NP_031768 Location (UCSC) Chr 17: 50.18 – 50.2 Mb Chr 11: 94.83 – 94.84 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse 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 ...
Timing is important to wound healing. Critically, the timing of wound re-epithelialization can decide the outcome of the healing. [11] If the epithelization of tissue over a denuded area is slow, a scar will form over many weeks, or months; [12] [13] If the epithelization of a wounded area is fast, the healing will result in regeneration.
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.
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 ...
To assist clinicians in standardizing the wound assessment and preparation of wound bed for treatment, the TIME framework was developed in 2002 by a group of wound care experts. [1] [2] The TIME acronym stands for Tissue, Infection/Inflammation, Moisture, and Edge – components that, per the TIME recommendation, should be thoroughly assessed ...