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Fibromodulin
from Wikipedia
FMOD
Identifiers
AliasesFMOD, FM, SLRR2E, fibromodulin
External IDsOMIM: 600245; MGI: 1328364; HomoloGene: 1530; GeneCards: FMOD; OMA:FMOD - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002023

NM_021355

RefSeq (protein)

NP_002014

NP_067330

Location (UCSC)Chr 1: 203.34 – 203.35 MbChr 1: 133.96 – 133.98 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Fibromodulin is a protein that in humans is encoded by the FMOD gene.[5][6]

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.[7]

Function

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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.[8] It also inhibits fibrillogenesis of collagen type I and collagen type III in vitro.[9][10] It regulates TGF-beta activities by sequestering TGF-beta into the extracellular matrix.[6]

Clinical significance

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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.[11]

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[12] and abnormal tail and Achilles tendons.[13] 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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