Fibromodulin

Last updated
FMOD
Identifiers
Aliases FMOD , FM, SLRR2E, fibromodulin
External IDs OMIM: 600245; MGI: 1328364; HomoloGene: 1530; GeneCards: FMOD; OMA:FMOD - orthologs
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

<span class="mw-page-title-main">Extracellular matrix</span> Network of proteins and molecules outside cells that provides structural support for cells

In biology, the extracellular matrix (ECM), also called intercellular matrix (ICM), is a network consisting of extracellular macromolecules and minerals, such as collagen, enzymes, glycoproteins and hydroxyapatite that provide structural and biochemical support to surrounding cells. Because multicellularity evolved independently in different multicellular lineages, the composition of ECM varies between multicellular structures; however, cell adhesion, cell-to-cell communication and differentiation are common functions of the ECM.

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

Proteoglycans are proteins that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge. The Ser residue is generally in the sequence -Ser-Gly-X-Gly-, although not every protein with this sequence has an attached glycosaminoglycan. The chains are long, linear carbohydrate polymers that are negatively charged under physiological conditions due to the occurrence of sulfate and uronic acid groups. Proteoglycans occur in connective tissue.

<span class="mw-page-title-main">Decorin</span> Protein-coding gene in humans

Decorin is a protein that in humans is encoded by the DCN gene.

<span class="mw-page-title-main">Biglycan</span> Protein-coding gene in humans

Biglycan is a small leucine-rich repeat proteoglycan (SLRP) which is found in a variety of extracellular matrix tissues, including bone, cartilage and tendon. In humans, biglycan is encoded by the BGN gene which is located on the X chromosome.

<span class="mw-page-title-main">Collagen, type XXVII, alpha 1</span> Protein found in humans

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<span class="mw-page-title-main">Syndecan-2</span> Protein-coding gene in the species Homo sapiens

Syndecan-2 is a protein that in humans is encoded by the SDC2 gene.

<span class="mw-page-title-main">Laminin subunit alpha-1</span> Protein-coding gene in the species Homo sapiens

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.

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

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">Collagen, type XIV, alpha 1</span> Protein found in humans

Collagen alpha-1(XIV) chain is a protein that in humans is encoded by the COL14A1 gene. It likely plays a role in collagen binding and cell-cell adhesion.

<span class="mw-page-title-main">MFAP2</span> Protein-coding gene in the species Homo sapiens

Microfibrillar-associated protein 2 is a protein that in humans is encoded by the MFAP2 gene.

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

Prolargin is a protein that in humans is encoded by the PRELP gene.

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

Beta-1,4-galactosyltransferase 7 also known as galactosyltransferase I is an enzyme that in humans is encoded by the B4GALT7 gene. Galactosyltransferase I catalyzes the synthesis of the glycosaminoglycan-protein linkage in proteoglycans. Proteoglycans in turn are structural components of the extracellular matrix that is found between cells in connective tissues.

<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">Matrilin-1</span> Protein-coding gene in the species Homo sapiens

Matrilin 1, cartilage matrix protein, also known as MATN1, is a matrilin protein which in humans is encoded by the MATN1 gene.

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

Zinc finger and BTB domain-containing protein 7B is a protein that in humans is encoded by the ZBTB7B gene. ZFP67 is an early growth response gene that encodes a zinc finger-containing transcription factor that binds to the promoter regions of type I collagen genes and has a role in development.[supplied by OMIM]

<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">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> Protein-coding gene in the species Homo sapiens

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.

Dick Heinegård was a Swedish biochemist. He received his doctorate in 1974 at Lund University and later became a professor of medical and physiological chemistry there. His research concentrated on the biology and pathology of connective tissue. Heinegård was elected in 2002 as a member of the Kungliga Vetenskapsakademin.

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. 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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