FMOD (gene)

From Wikipedia, the free encyclopedia

Fibromodulin

Identifiers

FMOD; SLRR2E

External IDs

OMIM: 600245 MGI: 1328364 HomoloGene: 1530

Gene ontology
Molecular Function:	• protein binding
Cellular Component:	• proteinaceous extracellular matrix
Biological Process:	• transforming growth factor beta receptor complex assembly

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002023 (mRNA)
NP_002014 (protein)

XM_977969 (mRNA)
XP_983063 (protein)

Location

Chr 1: 201.58 - 201.59 Mb

Chr 1: 135.85 - 135.86 Mb

Pubmed search

[1]

[2]

Fibromodulin, also known as FMOD, is a human gene.^[1]

Fibromodulin is a member of a family of small interstitial proteoglycans, containing a central region composed of leucine-rich repeats with 4 keratan sulfate chains flanked by disulfide-bonded terminal domains. It may participate in the assembly of the extracellular matrix as it interacts with type I and type II collagen fibrils and inhibits fibrillogenesis in vitro. It may also regulate TGF-beta activities by sequestering TGF-beta into the extracellular matrix.^[1]

[edit] References

^ ^a ^b Entrez Gene: FMOD fibromodulin.

[edit] Further reading

Roughley PJ, Lee ER (1994). "Cartilage proteoglycans: structure and potential functions.". Microsc. Res. Tech. 28 (5): 385–97. doi:10.1002/jemt.1070280505. PMID 7919526.
Sztrolovics R, Chen XN, Grover J, et al. (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.
Hildebrand A, Romarís M, Rasmussen LM, et al. (1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta.". Biochem. J. 302 ( Pt 2): 527–34. PMID 8093006.
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. PMID 8357838.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Westergren-Thorsson G, Norman M, Björnsson S, et al. (1998). "Differential expressions of mRNA for proteoglycans, collagens and transforming growth factor-beta in the human cervix during pregnancy and involution.". Biochim. Biophys. Acta 1406 (2): 203–13. PMID 9573366.
Font B, Eichenberger D, Goldschmidt D, et al. (1998). "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.". Eur. J. Biochem. 254 (3): 580–7. PMID 9688269.
Schaefer L, Gröne HJ, Raslik I, et al. (2000). "Small proteoglycans of normal adult human kidney: distinct expression patterns of decorin, biglycan, fibromodulin, and lumican.". Kidney Int. 58 (4): 1557–68. doi:10.1046/j.1523-1755.2000.00317.x. PMID 11012890.
Gori F, Schipani E, Demay MB (2001). "Fibromodulin is expressed by both chondrocytes and osteoblasts during fetal bone development.". J. Cell. Biochem. 82 (1): 46–57. PMID 11400162.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Mayr C, Bund D, Schlee M, et al. (2005). "Fibromodulin as a novel tumor-associated antigen (TAA) in chronic lymphocytic leukemia (CLL), which allows expansion of specific CD8+ autologous T lymphocytes.". Blood 105 (4): 1566–73. doi:10.1182/blood-2004-04-1233. PMID 15471955.
Mikaelsson E, Danesh-Manesh AH, Lüppert A, et al. (2005). "Fibromodulin, an extracellular matrix protein: characterization of its unique gene and protein expression in B-cell chronic lymphocytic leukemia and mantle cell lymphoma.". Blood 105 (12): 4828–35. doi:10.1182/blood-2004-10-3941. PMID 15741214.
Sjöberg A, Onnerfjord P, Mörgelin M, et al. (2005). "The extracellular matrix and inflammation: fibromodulin activates the classical pathway of complement by directly binding C1q.". J. Biol. Chem. 280 (37): 32301–8. doi:10.1074/jbc.M504828200. PMID 16046396.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Sjöberg AP, Trouw LA, Clark SJ, et al. (2007). "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.". J. Biol. Chem. 282 (15): 10894–900. doi:10.1074/jbc.M610256200. PMID 17293598.
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.