FMOD (gene)

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  (Redirected from Fibromodulin)
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Symbols FMOD ; FM; SLRR2E
External IDs OMIM600245 MGI1328364 HomoloGene1530 GeneCards: FMOD Gene
RNA expression pattern
PBB GE FMOD 202709 at tn.png
More reference expression data
Species Human Mouse
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:
203.31 – 203.32 Mb
Chr 1:
134.04 – 134.05 Mb
PubMed search [1] [2]

Fibromodulin is a protein that in humans is encoded by the FMOD gene.[1][2]

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.[2]


  1. ^ 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. 
  2. ^ a b "Entrez Gene: FMOD fibromodulin". 

Further reading[edit]

  • 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. 
  • 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 (2): 527–34. PMC 1137259. 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. doi:10.1016/0167-4781(93)90117-V. PMID 8357838. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. 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. doi:10.1016/S0925-4439(98)00005-2. 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. doi:10.1046/j.1432-1327.1998.2540580.x. 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. doi:10.1002/jcb.1115. 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. PMC 139241. 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.