Fibromodulin

Last updated
FMOD
Identifiers
Aliases FMOD , FM, SLRR2E, fibromodulin
External IDs OMIM: 600245 MGI: 1328364 HomoloGene: 1530 GeneCards: FMOD
Orthologs
SpeciesHumanMouse
Entrez

2331

14264

Ensembl

ENSG00000122176

ENSMUSG00000041559

UniProt

Q06828

P50608

RefSeq (mRNA)

NM_002023

NM_021355

RefSeq (protein)

NP_002014

NP_067330

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

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

Contents

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

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

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.

Related Research Articles

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<span class="mw-page-title-main">Proteoglycan</span> Class of compounds

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<span class="mw-page-title-main">Versican</span>

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<span class="mw-page-title-main">Decorin</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Biglycan</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">MMP10</span>

Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene.

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Lumican, also known as LUM, is an extracellular matrix protein that, in humans, is encoded by the LUM gene on chromosome 12.

<span class="mw-page-title-main">FBLN2</span>

Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.

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<span class="mw-page-title-main">B4GALT7</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Opticin</span> Protein-coding gene in the species Homo sapiens

Opticin is a protein that in humans is encoded by the OPTC gene.

<span class="mw-page-title-main">Asporin</span> Protein-coding gene in the species Homo sapiens

Asporin is a protein that in humans is encoded by the ASPN gene.

<span class="mw-page-title-main">ZBTB7B</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Dermatopontin</span> Protein-coding gene in the species Homo sapiens

Dermatopontin also known as tyrosine-rich acidic matrix protein (TRAMP) is a protein that in humans is encoded by the DPT gene. Dermatopontin is a 22-kDa protein of the noncollagenous extracellular matrix (ECM) estimated to comprise 12 mg/kg of wet dermis weight. To date, homologues have been identified in five different mammals and 12 different invertebrates with multiple functions. In vertebrates, the primary function of dermatopontin is a structural component of the ECM, cell adhesion, modulation of TGF-β activity and cellular quiescence). It also has pathological involvement in heart attacks and decreased expression in leiomyoma and fibrosis. In invertebrate, dermatopontin homologue plays a role in hemagglutination, cell-cell aggregation, and expression during parasite infection.

<span class="mw-page-title-main">Integrin alpha 11</span>

Integrin alpha-11 is a protein that, in humans, is encoded by the ITGA11 gene.

<span class="mw-page-title-main">EMID2</span> Mammalian protein found in Homo sapiens

Collagen alpha-1(XXVI) chain is a protein that in humans is encoded by the EMID2 gene.

<span class="mw-page-title-main">Tsukushi (protein)</span>

Tsukushi or tsukushin is an extracellular matrix protein of the small leucine rich proteoglycan (SLRP) family. In humans it is encoded by the TSKU gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000122176 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041559 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Sztrolovics R, Chen XN, Grover J, Roughley PJ, Korenberg JR (Mar 1995). "Localization of the human fibromodulin gene (FMOD) to chromosome 1q32 and completion of the cDNA sequence". Genomics. 23 (3): 715–7. doi:10.1006/geno.1994.1567. PMID   7851907.
  6. 1 2 "Entrez Gene: FMOD fibromodulin".
  7. ↑ Antonsson P, Heinegård D, Oldberg A (1993). "Structure and deduced amino acid sequence of the human fibromodulin gene". Biochim Biophys Acta. 1174 (2): 204–6. doi:10.1016/0167-4781(93)90117-V. PMID   8357838.
  8. ↑ Halper J (2014). "Proteoglycans and diseases of soft tissues". Progress in Heritable Soft Connective Tissue Diseases. Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology. Vol. 802. pp. 49–58. doi:10.1007/978-94-007-7893-1_4. ISBN   978-94-007-7892-4. PMID   24443020.
  9. ↑ Ezura Y, Chakravarti S, Oldberg A, Chervoneva I, Birk DE (2000). "Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons". J. Cell Biol. 151 (4): 779–88. doi:10.1083/jcb.151.4.779. PMC   2169450 . PMID   11076963.
  10. ↑ Kalamajski S, Oldberg A (2007). "Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11". J Biol Chem. 282 (37): 26740–5. doi: 10.1074/jbc.M704026200 . PMID   17623650.
  11. ↑ Roughley PJ, White RJ, Cs-Szabo G, Mort JS (1996). "Changes with age in the structure of fibromodulin in human articular cartilage". Osteoarthritis and Cartilage. 4 (3): 153–61. doi: 10.1016/s1063-4584(96)80011-2 . PMID   8895216.
  12. ↑ Smith MM, Melrose J (2015). "Proteoglycans in normal and healing skin". Adv Wound Care. 4 (3): 152–73. doi:10.1089/wound.2013.0464. PMC   4352701 . PMID   25785238.
  13. ↑ Juneja SC, Veillette C (2013). "Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review". Arthritis. 2013: 1–30. doi: 10.1155/2013/154812 . PMC   3842050 . PMID   24324885.

Further reading


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