Английская Википедия:Fibromodulin

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Шаблон:Short description Шаблон:Infobox gene Fibromodulin is a protein that in humans is encoded by the FMOD gene.[1][2]

Fibromodulin is a 42kDa protein of a family of small interstitial leucine-rich repeat proteoglycans (SLRPs). It can have up to four N-linked keratan sulfate chains attached to the core protein within the leucine-rich region. It shares significant sequence homology with biglycan and decorin.[3]

Function

Fibromodulin participates in the assembly of the collagen fibers of the extracellular matrix. It binds to the same site on the collagen type I molecule as lumican.[4] It also inhibits fibrillogenesis of collagen type I and collagen type III in vitro.[5][6] It regulates TGF-beta activities by sequestering TGF-beta into the extracellular matrix.[2]

Clinical significance

There is an age-dependent decline in the synthesis of keratan sulfate chains, so non-glycated forms of fibromodulin can accumulate in tissues such as cartilage.[7]

Fibromodulin is found in the epidermis of human skin and is expressed by skin cells (keratinocytes) in culture. Mice with the gene for fibromodulin knocked out (Fmod-/-) have very fragile skin[8] and abnormal tail and Achilles tendons.[9] The collagen fiber bundles in these tendons are fewer and disorganised and there is less endotenon surrounding the tendon tissue. The levels of lumican, a SLRP with one of the same collagen binding sites as fibromodulin, is increased 4 fold in the tail tendons of Fmod-knockout mice.

References

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Further reading

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Шаблон:Proteoglycans


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