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Gene Review

MMRN1  -  multimerin 1

Homo sapiens

Synonyms: ECM, EMILIN-4, EMILIN4, Elastin microfibril interface located protein 4, Elastin microfibril interfacer 4, ...
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Disease relevance of MMRN1

  • Recent studies identified multimerin as a specific coagulation factor V binding protein, complexed with platelet, but not plasma, factor V. These findings led us to investigate individuals with inherited factor V deficiencies for possible multimerin abnormalities [1].
  • These data indicate that patients with factor V Quebec have an inherited bleeding disorder distinct from other platelet disorders and associated with multiple abnormalities, including multimerin deficiency, abnormal platelet factor V, thrombospondin, von Willebrand factor, and fibrinogen, and an epinephrine aggregation defect [1].
  • The products of the collagen-alpha 1(I) and -alpha 2(I) genes form the triple helical molecule collagen type I, which constitutes the major ECM protein in tissue fibrosis [2].
  • Degradation of ECM, particularly interstitial collagen, promotes plaque instability, rendering atheroma prone to rupture [3].
  • Transgenic animals exhibiting nephritis as a result of treatment with anti--glomerular basement membrane antiserum showed significantly more persistent expansion of the mesangial ECM than was seen in parental mice [4].

Psychiatry related information on MMRN1

  • Active MMP-2 may degrade A beta or act on ECM components critical in neuronal survival mechanisms and possibly play a role in Alzheimer's disease (AD) neuropathology [5].

High impact information on MMRN1

  • Cadherin mediated cell compaction and cellular rearrangements may be analogous to integrin-mediated cell spreading and motility on the ECM [6].
  • A hierarchy of ECM-mediated signalling regulates tissue-specific gene expression [7].
  • The concept that the cytoskeleton and éxocellular matrix' (ECM) form an interactive scaffold for perception and transduction of positional information is relatively new [8].
  • Cytokines secreted by cells that mediate the innate and adaptive immune responses play a critical role in regulating the synthesis of ECM components by fibroblasts [9].
  • These findings underscore the potential importance of hepatic macrophages in regulating both stellate cell biology and ECM degradation during regression of hepatic fibrosis [10].

Chemical compound and disease context of MMRN1

  • Taken together, our data indicate that PMA induces a rapid and temporary ECM-dependent enhancement of melanoma cell attachment and spreading, and that the response to ECM components appears not to be due to significant shifts in beta 1 integrin expression, but rather to activation of beta 1 integrins [11].
  • Heparanase, a heparan sulfate-specific endo-beta-D-glucuronidase, plays an important role in tumor cell metastasis through the degradation of extracellular matrix heparan sulfate proteoglycans (ECM HSPG) [12].
  • Human colon cancer cell lines LS174T and LiM6 were plated on plastic, on hepatocyte-derived ECM or on stromal ECM and in the presence of the antimetabolite 5-fluorouracil (5-FU). the topoisomerase I inhibitor camptothecin and the topoisomerase II inhibitor etoposide [13].
  • This indicates that resveratrol may influence the two major factors in the ECM remodeling occurring with tumor invasion, suggesting it may have uses as a therapeutic agent for brain tumors [14].
  • Two sugar analogs, 2-acetamido-2-deoxy-1,5-gluconolactone (CD80110) and 2-acetamido-1,5-imino-1,2,5-trideoxy-D-glucitol (CD 86022), were evaluated for their ability to inhibit 1) human ovarian carcinoma beta-NAG isoenzyme activities, 2) degradation of radiolabeled ECM mediated by HOC cells and beta-NAG, and 3) cell growth [15].

Biological context of MMRN1


Anatomical context of MMRN1


Associations of MMRN1 with chemical compounds


Other interactions of MMRN1


Analytical, diagnostic and therapeutic context of MMRN1


  1. An autosomal dominant, qualitative platelet disorder associated with multimerin deficiency, abnormalities in platelet factor V, thrombospondin, von Willebrand factor, and fibrinogen and an epinephrine aggregation defect. Hayward, C.P., Rivard, G.E., Kane, W.H., Drouin, J., Zheng, S., Moore, J.C., Kelton, J.G. Blood (1996) [Pubmed]
  2. Mithramycin selectively inhibits collagen-alpha 1(I) gene expression in human fibroblast. Nehls, M.C., Brenner, D.A., Gruss, H.J., Dierbach, H., Mertelsmann, R., Herrmann, F. J. Clin. Invest. (1993) [Pubmed]
  3. Tissue factor pathway inhibitor-2 is a novel inhibitor of matrix metalloproteinases with implications for atherosclerosis. Herman, M.P., Sukhova, G.K., Kisiel, W., Foster, D., Kehry, M.R., Libby, P., Schönbeck, U. J. Clin. Invest. (2001) [Pubmed]
  4. Overexpression of the serpin megsin induces progressive mesangial cell proliferation and expansion. Miyata, T., Inagi, R., Nangaku, M., Imasawa, T., Sato, M., Izuhara, Y., Suzuki, D., Yoshino, A., Onogi, H., Kimura, M., Sugiyama, S., Kurokawa, K. J. Clin. Invest. (2002) [Pubmed]
  5. Activated isoforms of MMP-2 are induced in U87 human glioma cells in response to beta-amyloid peptide. Deb, S., Zhang, J.W., Gottschall, P.E. J. Neurosci. Res. (1999) [Pubmed]
  6. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Gumbiner, B.M. Cell (1996) [Pubmed]
  7. A hierarchy of ECM-mediated signalling regulates tissue-specific gene expression. Roskelley, C.D., Srebrow, A., Bissell, M.J. Curr. Opin. Cell Biol. (1995) [Pubmed]
  8. The plant cytoskeleton-cell-wall continuum. Wyatt, S.E., Carpita, N.C. Trends Cell Biol. (1993) [Pubmed]
  9. B cells: no longer bystanders in liver fibrosis. Bhogal, R.K., Bona, C.A. J. Clin. Invest. (2005) [Pubmed]
  10. Mac the knife? Macrophages- the double-edged sword of hepatic fibrosis. Friedman, S.L. J. Clin. Invest. (2005) [Pubmed]
  11. Phorbol ester induced rapid attachment and spreading of melanoma cells and the role of extracellular matrix proteins. van Leeuwen, R.L., Dekker, S.K., Arbiser, J.L., Vermeer, B.J., Bruijn, J.A., Byers, H.R. Int. J. Cancer (1994) [Pubmed]
  12. Inhibition of heparanase activity and heparanase-induced angiogenesis by suramin analogues. Marchetti, D., Reiland, J., Erwin, B., Roy, M. Int. J. Cancer (2003) [Pubmed]
  13. Stromal extracellular matrix reduces chemotherapy-induced apoptosis in colon cancer cell lines. Kouniavsky, G., Khaikin, M., Zvibel, I., Zippel, D., Brill, S., Halpern, Z., Papa, M. Clin. Exp. Metastasis (2002) [Pubmed]
  14. Effect of resveratrol on matrix metalloproteinase-2 (MMP-2) and Secreted Protein Acidic and Rich in Cysteine (SPARC) on human cultured glioblastoma cells. Gagliano, N., Moscheni, C., Torri, C., Magnani, I., Bertelli, A.A., Gioia, M. Biomed. Pharmacother. (2005) [Pubmed]
  15. Inhibition of human ovarian carcinoma cell- and hexosaminidase- mediated degradation of extracellular matrix by sugar analogs. Woynarowska, B., Wikiel, H., Sharma, M., Carpenter, N., Fleet, G.W., Bernacki, R.J. Anticancer Res. (1992) [Pubmed]
  16. Analyses of cellular multimerin 1 receptors: in vitro evidence of binding mediated by alphaIIbbeta3 and alphavbeta3. Adam, F., Zheng, S., Joshi, N., Kelton, D.S., Sandhu, A., Suehiro, Y., Jeimy, S.B., Santos, A.V., Massé, J.M., Kelton, J.G., Cramer, E.M., Hayward, C.P. Thromb. Haemost. (2005) [Pubmed]
  17. Multimerin. Hayward, C.P., Kelton, J.G. Curr. Opin. Hematol. (1995) [Pubmed]
  18. Identification of the MMRN1 binding region within the C2 domain of human factor V. Jeimy, S.B., Woram, R.A., Fuller, N., Quinn-Allen, M.A., Nicolaes, G.A., Dahlbäck, B., Kane, W.H., Hayward, C.P. J. Biol. Chem. (2004) [Pubmed]
  19. Platelet glycoprotein Ia* is the processed form of multimerin--isolation and determination of N-terminal sequences of stored and released forms. Polgár, J., Magnenat, E., Wells, T.N., Clemetson, K.J. Thromb. Haemost. (1998) [Pubmed]
  20. Domain-specific activation of neuronal migration and neurite outgrowth-promoting activities of laminin. Calof, A.L., Campanero, M.R., O'Rear, J.J., Yurchenco, P.D., Lander, A.D. Neuron (1994) [Pubmed]
  21. Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration. Baldus, S., Eiserich, J.P., Mani, A., Castro, L., Figueroa, M., Chumley, P., Ma, W., Tousson, A., White, C.R., Bullard, D.C., Brennan, M.L., Lusis, A.J., Moore, K.P., Freeman, B.A. J. Clin. Invest. (2001) [Pubmed]
  22. Phenotypic variation in a large Swedish pedigree due to SNCA duplication and triplication. Fuchs, J., Nilsson, C., Kachergus, J., Munz, M., Larsson, E.M., Schüle, B., Langston, J.W., Middleton, F.A., Ross, O.A., Hulihan, M., Gasser, T., Farrer, M.J. Neurology (2007) [Pubmed]
  23. Studies of multimerin in human endothelial cells. Hayward, C.P., Cramer, E.M., Song, Z., Zheng, S., Fung, R., Massé, J.M., Stead, R.H., Podor, T.J. Blood (1998) [Pubmed]
  24. A recombinant homotrimer, composed of the alpha helical neck region of human surfactant protein D and C1q B chain globular domain, is an inhibitor of the classical complement pathway. Kishore, U., Strong, P., Perdikoulis, M.V., Reid, K.B. J. Immunol. (2001) [Pubmed]
  25. The EMILIN protein family. Colombatti, A., Doliana, R., Bot, S., Canton, A., Mongiat, M., Mungiguerra, G., Paron-Cilli, S., Spessotto, P. Matrix Biol. (2000) [Pubmed]
  26. Multimerin is found in the alpha-granules of resting platelets and is synthesized by a megakaryocytic cell line. Hayward, C.P., Bainton, D.F., Smith, J.W., Horsewood, P., Stead, R.H., Podor, T.J., Warkentin, T.E., Kelton, J.G. J. Clin. Invest. (1993) [Pubmed]
  27. Human platelets contain forms of factor V in disulfide-linkage with multimerin. Hayward, C.P., Fuller, N., Zheng, S., Adam, F., Jeimy, S.B., Horsewood, I., Quinn-Allen, M.A., Kane, W.H. Thromb. Haemost. (2004) [Pubmed]
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