Type I collagen
collagen, type I, alpha 1 | |||||||
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Identifiers | |||||||
Symbol | COL1A1 | ||||||
NCBI gene | 1277 | ||||||
HGNC | 2197 | ||||||
OMIM | 120150 | ||||||
RefSeq | NM_000088 | ||||||
UniProt | P02452 | ||||||
Other data | |||||||
Locus | Chr. 17 q21.3-q22 | ||||||
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collagen, type I, alpha 2 | |||||||
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Identifiers | |||||||
Symbol | COL1A2 | ||||||
Alt. symbols | OI4 | ||||||
NCBI gene | 1278 | ||||||
HGNC | 2198 | ||||||
OMIM | 120160 | ||||||
RefSeq | NM_000089 | ||||||
UniProt | P08123 | ||||||
Other data | |||||||
Locus | Chr. 7 q21.3-22.1 | ||||||
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Type I collagen is the most abundant collagen of the human body. It 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.
Formation
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 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.
Clinical significance
See Collagen, type I, alpha 1#Clinical significance
See also
References
- Junqueira's Basic Histology, p106
External links
- Collagen+type+I at the U.S. National Library of Medicine Medical Subject Headings (MeSH)