Type I collagen

Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen.[1] 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.

collagen, type I, alpha 1
Identifiers
SymbolCOL1A1
NCBI gene1277
HGNC2197
OMIM120150
RefSeqNM_000088
UniProtP02452
Other data
LocusChr. 17 q21.3-q22
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StructuresSwiss-model
DomainsInterPro
collagen, type I, alpha 2
Identifiers
SymbolCOL1A2
Alt. symbolsOI4
NCBI gene1278
HGNC2198
OMIM120160
RefSeqNM_000089
UniProtP08123
Other data
LocusChr. 7 q21.3-22.1
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StructuresSwiss-model
DomainsInterPro

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 pro-collagen. These triple-stranded, rope-like pro-collagen 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 fiber.

Clinical significance

See Collagen, type I, alpha 1#Clinical significance

Markers used to measure bone loss are not easily testable. Degradation of type I collagen releases metabolites that can be used to monitor resorption.[2]

See also

References
  1. "Collagen: What it is, Types, Function & Benefits". Cleveland Clinic. Retrieved 2023-09-20.
  2. Ting, Kay R. (2016). "Clinical Utility of C‐Terminal Telopeptide of Type 1 Collagen in Multiple Myeloma". British Journal of Haematology. 173 (1): 82–88. doi:10.1111/bjh.13928. PMID 26787413.

Further reading
  • Mescher AL (2018). Junqueira's basic histology: text and atlas. McGraw-Hill Education. p. 106. ISBN 978-1-260-02618-4.


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