Fibromodulin: Difference between revisions

From Wikipedia, the free encyclopedia
Browse history interactively
← Previous edit
Content deleted Content added
VisualWikitext
OAbot (talk | contribs)
Bots
418,853 edits
m Open access bot: doi added to citation with #oabot.
Citation bot (talk | contribs)
Bots
4,918,591 edits
Alter: chapter. Removed parameters. | Use this bot. Report bugs. | #UCB_CommandLine
 
(10 intermediate revisions by 7 users not shown)
Line 1: Line 1:
{{Short description|Protein}}
{{Infobox_gene}}
{{Infobox_gene}}
'''Fibromodulin''' is a [[protein]] that in humans is encoded by the ''FMOD'' [[gene]].<ref name="pmid7851907">{{cite journal | vauthors = Sztrolovics R, Chen XN, Grover J, Roughley PJ, Korenberg JR | title = Localization of the human fibromodulin gene (FMOD) to chromosome 1q32 and completion of the cDNA sequence | journal = Genomics | volume = 23 | issue = 3 | pages = 715–7 |date=Mar 1995 | pmid = 7851907 | pmc = | doi = 10.1006/geno.1994.1567 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FMOD fibromodulin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2331| accessdate = }}</ref>
'''Fibromodulin''' is a [[protein]] that in humans is encoded by the ''FMOD'' [[gene]].<ref name="pmid7851907">{{cite journal | vauthors = Sztrolovics R, Chen XN, Grover J, Roughley PJ, Korenberg JR | title = Localization of the human fibromodulin gene (FMOD) to chromosome 1q32 and completion of the cDNA sequence | journal = Genomics | volume = 23 | issue = 3 | pages = 715–7 |date=Mar 1995 | pmid = 7851907 | doi = 10.1006/geno.1994.1567 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FMOD fibromodulin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2331}}</ref>


Fibromodulin is a 42kDa [[protein]] of a family of small interstitial leucine-rich repeat [[proteoglycan]]s (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]].<ref name="pmid8357838">{{cite journal | vauthors = Antonsson P, Heinegård D, Oldberg A |title = Structure and deduced amino acid sequence of the human fibromodulin gene |journal = Biochim Biophys Acta |volume = 1174 |issue = 2 |pages = 204–6 |year = 1993 |pmid = 8357838 |doi = 10.1016/0167-4781(93)90117-V}}</ref>
Fibromodulin is a 42kDa [[protein]] of a family of small interstitial leucine-rich repeat [[proteoglycan]]s (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]].<ref name="pmid8357838">{{cite journal | vauthors = Antonsson P, Heinegård D, Oldberg A |title = Structure and deduced amino acid sequence of the human fibromodulin gene |journal = Biochim Biophys Acta |volume = 1174 |issue = 2 |pages = 204–6 |year = 1993 |pmid = 8357838 |doi = 10.1016/0167-4781(93)90117-V}}</ref>


== Function ==
== 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]].<ref>{{cite book | vauthors = Halper J | title = Proteoglycans and diseases of soft tissues | journal = Adv. Exp. Med. Biol. | volume = 802 | pages = 49–58 | year = 2014 | pmid = 24443020 | doi = 10.1007/978-94-007-7893-1_4 | series = Advances in Experimental Medicine and Biology | isbn = 978-94-007-7892-4 }}</ref> It also inhibits fibrillogenesis of [[collagen type I]] and collagen type III ''in vitro''.<ref>{{cite journal | vauthors = Ezura Y, Chakravarti S, Oldberg A, Chervoneva I, Birk DE | title = Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons | journal = J. Cell Biol. | volume = 151 | issue = 4 | pages = 779–88 | year = 2000 | pmid = 11076963 | doi = 10.1083/jcb.151.4.779 | pmc=2169450}}</ref><ref name = "pmid17623650">{{cite journal | vauthors = Kalamajski S, Oldberg A | title = Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11. | journal = J Biol Chem | volume = 282 | issue = 37 |pages = 26740–5 |year = 2007 |pmid= 17623650 |doi= 10.1074/jbc.M704026200 | doi-access = free }}</ref> It regulates TGF-beta activities by sequestering TGF-beta into the extracellular matrix.<ref name="entrez"/>
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]].<ref>{{cite book | vauthors = Halper J | chapter = Proteoglycans and Diseases of Soft Tissues | title = Progress in Heritable Soft Connective Tissue Diseases | volume = 802 | pages = 49–58 | year = 2014 | pmid = 24443020 | doi = 10.1007/978-94-007-7893-1_4 | series = Advances in Experimental Medicine and Biology | isbn = 978-94-007-7892-4 }}</ref> It also inhibits fibrillogenesis of [[collagen type I]] and collagen type III ''in vitro''.<ref>{{cite journal | vauthors = Ezura Y, Chakravarti S, Oldberg A, Chervoneva I, Birk DE | title = Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons | journal = J. Cell Biol. | volume = 151 | issue = 4 | pages = 779–88 | year = 2000 | pmid = 11076963 | doi = 10.1083/jcb.151.4.779 | pmc=2169450}}</ref><ref name = "pmid17623650">{{cite journal | vauthors = Kalamajski S, Oldberg A | title = Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11. | journal = J Biol Chem | volume = 282 | issue = 37 |pages = 26740–5 |year = 2007 |pmid= 17623650 |doi= 10.1074/jbc.M704026200 | doi-access = free }}</ref> It regulates TGF-beta activities by sequestering TGF-beta into the extracellular matrix.<ref name="entrez"/>


== Clinical significance ==
== 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]].<ref>{{cite journal | vauthors = Roughley PJ, White RJ, Cs-Szabo G, Mort JS | title = Changes with age in the structure of fibromodulin in human articular cartilage | journal = Osteoarthritis and Cartilage | volume = 4 | issue = 3 | pages = 153–61 | year = 1996 | pmid = 8895216 | doi=10.1016/s1063-4584(96)80011-2}}</ref>
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]].<ref>{{cite journal | vauthors = Roughley PJ, White RJ, Cs-Szabo G, Mort JS | title = Changes with age in the structure of fibromodulin in human articular cartilage | journal = Osteoarthritis and Cartilage | volume = 4 | issue = 3 | pages = 153–61 | year = 1996 | pmid = 8895216 | doi=10.1016/s1063-4584(96)80011-2| doi-access = free }}</ref>


Fibromodulin is found in the [[epidermis]] of human [[skin]] and is expressed by skin cells ([[keratinocyte]]s) in culture. Mice with the gene for fibromodulin knocked out (Fmod-/-) have very fragile [[skin]]<ref>{{cite journal | vauthors = Smith MM, Melrose J | title = Proteoglycans in normal and healing skin | journal = Adv Wound Care | volume = 4 | issue = 3 | pages = 152–73 | year = 2015 | pmid = 25785238 | doi = 10.1089/wound.2013.0464 | pmc=4352701}}</ref> and abnormal tail and [[Achilles tendon]]s.<ref>{{cite journal | vauthors = Juneja SC, Veillette C | title = Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review | journal = Arthritis | volume = 2013 | pages = 1–30 | year = 2013 | pmid = 24324885 | doi = 10.1155/2013/154812 | pmc=3842050}}</ref> 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.
Fibromodulin is found in the [[epidermis]] of human [[skin]] and is expressed by skin cells ([[keratinocyte]]s) in culture. Mice with the gene for fibromodulin knocked out (Fmod-/-) have very fragile [[skin]]<ref>{{cite journal | vauthors = Smith MM, Melrose J | title = Proteoglycans in normal and healing skin | journal = Adv Wound Care | volume = 4 | issue = 3 | pages = 152–73 | year = 2015 | pmid = 25785238 | doi = 10.1089/wound.2013.0464 | pmc=4352701}}</ref> and abnormal tail and [[Achilles tendon]]s.<ref>{{cite journal | vauthors = Juneja SC, Veillette C | title = Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review | journal = Arthritis | volume = 2013 | pages = 1–30 | year = 2013 | pmid = 24324885 | doi = 10.1155/2013/154812 | pmc=3842050| doi-access = free }}</ref> 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 ==
== References ==
Line 19: Line 20:
== Further reading ==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
* {{cite journal | vauthors = Roughley PJ, Lee ER | title = Cartilage proteoglycans: structure and potential functions | journal = Microscopy Research and Technique | volume = 28 | issue = 5 | pages = 385–97 | date = Aug 1994 | pmid = 7919526 | doi = 10.1002/jemt.1070280505 }}
* {{cite journal | vauthors = Roughley PJ, Lee ER | title = Cartilage proteoglycans: structure and potential functions | journal = Microscopy Research and Technique | volume = 28 | issue = 5 | pages = 385–97 | date = Aug 1994 | pmid = 7919526 | doi = 10.1002/jemt.1070280505 | s2cid = 43194492 }}
* {{cite journal | vauthors = Hildebrand A, Romarís M, Rasmussen LM, Heinegård D, Twardzik DR, Border WA, Ruoslahti E | title = Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta | journal = The Biochemical Journal | volume = 302 | issue = 2 | pages = 527–34 | date = Sep 1994 | pmid = 8093006 | pmc = 1137259 | doi = 10.1042/bj3020527}}
* {{cite journal | vauthors = Hildebrand A, Romarís M, Rasmussen LM, Heinegård D, Twardzik DR, Border WA, Ruoslahti E | title = Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta | journal = The Biochemical Journal | volume = 302 | issue = 2 | pages = 527–34 | date = Sep 1994 | pmid = 8093006 | pmc = 1137259 | doi = 10.1042/bj3020527}}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 | doi-access = free }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 | doi-access = free }}
* {{cite journal | vauthors = Westergren-Thorsson G, Norman M, Björnsson S, Endrésen U, Stjernholm Y, Ekman G, Malmström A | title = Differential expressions of mRNA for proteoglycans, collagens and transforming growth factor-beta in the human cervix during pregnancy and involution | journal = Biochimica et Biophysica Acta | volume = 1406 | issue = 2 | pages = 203–13 | date = Mar 1998 | pmid = 9573366 | doi = 10.1016/S0925-4439(98)00005-2 }}
* {{cite journal | vauthors = Westergren-Thorsson G, Norman M, Björnsson S, Endrésen U, Stjernholm Y, Ekman G, Malmström A | title = Differential expressions of mRNA for proteoglycans, collagens and transforming growth factor-beta in the human cervix during pregnancy and involution | journal = Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease | volume = 1406 | issue = 2 | pages = 203–13 | date = Mar 1998 | pmid = 9573366 | doi = 10.1016/S0925-4439(98)00005-2 | doi-access = free }}
* {{cite journal | vauthors = Font B, Eichenberger D, Goldschmidt D, Boutillon MM, Hulmes DJ | title = Structural requirements for fibromodulin binding to collagen and the control of type I collagen fibrillogenesis--critical roles for disulphide bonding and the C-terminal region | journal = European Journal of Biochemistry / FEBS | volume = 254 | issue = 3 | pages = 580–7 | date = Jun 1998 | pmid = 9688269 | doi = 10.1046/j.1432-1327.1998.2540580.x }}
* {{cite journal | vauthors = Font B, Eichenberger D, Goldschmidt D, Boutillon MM, Hulmes DJ | title = Structural requirements for fibromodulin binding to collagen and the control of type I collagen fibrillogenesis--critical roles for disulphide bonding and the C-terminal region | journal = European Journal of Biochemistry | volume = 254 | issue = 3 | pages = 580–7 | date = Jun 1998 | pmid = 9688269 | doi = 10.1046/j.1432-1327.1998.2540580.x | doi-access = free }}
* {{cite journal | vauthors = Schaefer L, Gröne HJ, Raslik I, Robenek H, Ugorcakova J, Budny S, Schaefer RM, Kresse H | title = Small proteoglycans of normal adult human kidney: distinct expression patterns of decorin, biglycan, fibromodulin, and lumican | journal = Kidney International | volume = 58 | issue = 4 | pages = 1557–68 | date = Oct 2000 | pmid = 11012890 | doi = 10.1046/j.1523-1755.2000.00317.x }}
* {{cite journal | vauthors = Schaefer L, Gröne HJ, Raslik I, Robenek H, Ugorcakova J, Budny S, Schaefer RM, Kresse H | title = Small proteoglycans of normal adult human kidney: distinct expression patterns of decorin, biglycan, fibromodulin, and lumican | journal = Kidney International | volume = 58 | issue = 4 | pages = 1557–68 | date = Oct 2000 | pmid = 11012890 | doi = 10.1046/j.1523-1755.2000.00317.x | doi-access = free }}
* {{cite journal | vauthors = Gori F, Schipani E, Demay MB | title = Fibromodulin is expressed by both chondrocytes and osteoblasts during fetal bone development | journal = Journal of Cellular Biochemistry | volume = 82 | issue = 1 | pages = 46–57 | year = 2001 | pmid = 11400162 | doi = 10.1002/jcb.1115 }}
* {{cite journal | vauthors = Gori F, Schipani E, Demay MB | title = Fibromodulin is expressed by both chondrocytes and osteoblasts during fetal bone development | journal = Journal of Cellular Biochemistry | volume = 82 | issue = 1 | pages = 46–57 | year = 2001 | pmid = 11400162 | doi = 10.1002/jcb.1115 | s2cid = 41342892 }}
* {{cite journal | vauthors = Mayr C, Bund D, Schlee M, Moosmann A, Kofler DM, Hallek M, Wendtner CM | title = Fibromodulin as a novel tumor-associated antigen (TAA) in chronic lymphocytic leukemia (CLL), which allows expansion of specific CD8+ autologous T lymphocytes | journal = Blood | volume = 105 | issue = 4 | pages = 1566–73 | date = Feb 2005 | pmid = 15471955 | doi = 10.1182/blood-2004-04-1233 | doi-access = free }}
* {{cite journal | vauthors = Mayr C, Bund D, Schlee M, Moosmann A, Kofler DM, Hallek M, Wendtner CM | title = Fibromodulin as a novel tumor-associated antigen (TAA) in chronic lymphocytic leukemia (CLL), which allows expansion of specific CD8+ autologous T lymphocytes | journal = Blood | volume = 105 | issue = 4 | pages = 1566–73 | date = Feb 2005 | pmid = 15471955 | doi = 10.1182/blood-2004-04-1233 | doi-access = free }}
* {{cite journal | vauthors = Mikaelsson E, Danesh-Manesh AH, Lüppert A, Jeddi-Tehrani M, Rezvany MR, Sharifian RA, Safaie R, Roohi A, Osterborg A, Shokri F, Mellstedt H, Rabbani H | title = Fibromodulin, an extracellular matrix protein: characterization of its unique gene and protein expression in B-cell chronic lymphocytic leukemia and mantle cell lymphoma | journal = Blood | volume = 105 | issue = 12 | pages = 4828–35 | date = Jun 2005 | pmid = 15741214 | doi = 10.1182/blood-2004-10-3941 | doi-access = free }}
* {{cite journal | vauthors = Mikaelsson E, Danesh-Manesh AH, Lüppert A, Jeddi-Tehrani M, Rezvany MR, Sharifian RA, Safaie R, Roohi A, Osterborg A, Shokri F, Mellstedt H, Rabbani H | title = Fibromodulin, an extracellular matrix protein: characterization of its unique gene and protein expression in B-cell chronic lymphocytic leukemia and mantle cell lymphoma | journal = Blood | volume = 105 | issue = 12 | pages = 4828–35 | date = Jun 2005 | pmid = 15741214 | doi = 10.1182/blood-2004-10-3941 | doi-access = free }}
* {{cite journal | vauthors = Sjöberg A, Onnerfjord P, Mörgelin M, Heinegård D, Blom AM | title = The extracellular matrix and inflammation: fibromodulin activates the classical pathway of complement by directly binding C1q | journal = The Journal of Biological Chemistry | volume = 280 | issue = 37 | pages = 32301–8 | date = Sep 2005 | pmid = 16046396 | doi = 10.1074/jbc.M504828200 | doi-access = free }}
* {{cite journal | vauthors = Sjöberg A, Onnerfjord P, Mörgelin M, Heinegård D, Blom AM | title = The extracellular matrix and inflammation: fibromodulin activates the classical pathway of complement by directly binding C1q | journal = The Journal of Biological Chemistry | volume = 280 | issue = 37 | pages = 32301–8 | date = Sep 2005 | pmid = 16046396 | doi = 10.1074/jbc.M504828200 | doi-access = free }}
* {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R }}
* {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R | s2cid = 4427026 }}
* {{cite journal | vauthors = Sjöberg AP, Trouw LA, Clark SJ, Sjölander J, Heinegård D, Sim RB, Day AJ, Blom AM | title = The factor H variant associated with age-related macular degeneration (His-384) and the non-disease-associated form bind differentially to C-reactive protein, fibromodulin, DNA, and necrotic cells | journal = The Journal of Biological Chemistry | volume = 282 | issue = 15 | pages = 10894–900 | date = Apr 2007 | pmid = 17293598 | doi = 10.1074/jbc.M610256200 | doi-access = free }}
* {{cite journal | vauthors = Sjöberg AP, Trouw LA, Clark SJ, Sjölander J, Heinegård D, Sim RB, Day AJ, Blom AM | title = The factor H variant associated with age-related macular degeneration (His-384) and the non-disease-associated form bind differentially to C-reactive protein, fibromodulin, DNA, and necrotic cells | journal = The Journal of Biological Chemistry | volume = 282 | issue = 15 | pages = 10894–900 | date = Apr 2007 | pmid = 17293598 | doi = 10.1074/jbc.M610256200 | doi-access = free }}
* {{cite journal | vauthors = Kalamajski S, Oldberg A | title = Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11 | journal = The Journal of Biological Chemistry | volume = 282 | issue = 37 | pages = 26740–5 | date = Sep 2007 | pmid = 17623650 | doi = 10.1074/jbc.M704026200 | doi-access = free }}
* {{cite journal | vauthors = Kalamajski S, Oldberg A | title = Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11 | journal = The Journal of Biological Chemistry | volume = 282 | issue = 37 | pages = 26740–5 | date = Sep 2007 | pmid = 17623650 | doi = 10.1074/jbc.M704026200 | doi-access = free }}
{{refend}}
{{refend}}

{{Proteoglycans}}


[[Category:Extracellular matrix proteins]]
[[Category:Extracellular matrix proteins]]

Latest revision as of 05:05, 26 August 2023

FMOD
Identifiers
AliasesFMOD, FM, SLRR2E, fibromodulin
External IDsOMIM: 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 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[edit]

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[edit]

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[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000122176 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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[edit]


Stub icon

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

Retrieved from "https://en.wikipedia.org/w/index.php?title=Fibromodulin&oldid=1172292217"