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Gene Review

MFAP2  -  microfibrillar-associated protein 2

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Disease relevance of MFAP2


High impact information on MFAP2

  • MFAP4 has a fibrinogen-like domain and shares a high level of sequence homology to a fragment of a bovine 36 kDa microfibril-associated glycoprotein [3].
  • It is possible that these mutations alter the ability of fibrillin to bind MAGP-1, which may contribute to the severity of the disease [4].
  • Interestingly, no binding was detected to sequences near the N or C terminus where MAGP-1 and MAGP-2, respectively, were shown to interact with fibrillin-1 [4].
  • Using yeast two-hybrid, ligand blotting, and solid phase binding assays, we have shown that microfibril-associated glycoprotein-1 (MAGP-1) interacts with the 8-cysteine motif of fibrillin-2 encoded by exon 24 [4].
  • Binding to this sequence was demonstrated for full-length MAGP-1 as well as for the MAGP-1 matrix-binding domain encoded by exons 7 and 8 [4].

Biological context of MFAP2


Anatomical context of MFAP2


Associations of MFAP2 with chemical compounds


Other interactions of MFAP2


Analytical, diagnostic and therapeutic context of MFAP2


  1. Molecular cloning of the complementary DNA for an additional member of the family of aortic aneurysm antigenic proteins. Hirose, H., Ozsvath, K.J., Xia, S., Tilson, M.D. J. Vasc. Surg. (1997) [Pubmed]
  2. Identification of tranilast-binding protein as 36-kDa microfibril-associated glycoprotein by drug affinity chromatography, and its localization in human skin. Furuichi, H., Yamashita, K., Okada, M., Toyoshima, T., Hata, Y., Suzuki, S., Itano, T., Shishibori, T., Tokumitsu, H., Kobayashi, R. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  3. The gene for a human microfibril-associated glycoprotein is commonly deleted in Smith-Magenis syndrome patients. Zhao, Z., Lee, C.C., Jiralerspong, S., Juyal, R.C., Lu, F., Baldini, A., Greenberg, F., Caskey, C.T., Patel, P.I. Hum. Mol. Genet. (1995) [Pubmed]
  4. Identification of a major microfibril-associated glycoprotein-1-binding domain in fibrillin-2. Werneck, C.C., Trask, B.C., Broekelmann, T.J., Trask, T.M., Ritty, T.M., Segade, F., Mecham, R.P. J. Biol. Chem. (2004) [Pubmed]
  5. Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils. Gibson, M.A., Sandberg, L.B., Grosso, L.E., Cleary, E.G. J. Biol. Chem. (1991) [Pubmed]
  6. Posttranslational modifications of microfibril associated glycoprotein-1 (MAGP-1). Trask, B.C., Broekelmann, T., Ritty, T.M., Trask, T.M., Tisdale, C., Mecham, R.P. Biochemistry (2001) [Pubmed]
  7. Calvasculin, an encoded protein from mRNA termed pEL-98, 18A2, 42A, or p9Ka, is secreted by smooth muscle cells in culture and exhibits Ca(2+)-dependent binding to 36-kDa microfibril-associated glycoprotein. Watanabe, Y., Usuda, N., Tsugane, S., Kobayashi, R., Hidaka, H. J. Biol. Chem. (1992) [Pubmed]
  8. Microfibril-associated glycoprotein binds to the carboxyl-terminal domain of tropoelastin and is a substrate for transglutaminase. Brown-Augsburger, P., Broekelmann, T., Mecham, L., Mercer, R., Gibson, M.A., Cleary, E.G., Abrams, W.R., Rosenbloom, J., Mecham, R.P. J. Biol. Chem. (1994) [Pubmed]
  9. The protein components of the 12-nanometer microfibrils of elastic and nonelastic tissues. Gibson, M.A., Kumaratilake, J.S., Cleary, E.G. J. Biol. Chem. (1989) [Pubmed]
  10. The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin. Trask, B.C., Trask, T.M., Broekelmann, T., Mecham, R.P. Mol. Biol. Cell (2000) [Pubmed]
  11. Microfibril-associated glycoprotein-2 (MAGP-2) is specifically associated with fibrillin-containing microfibrils but exhibits more restricted patterns of tissue localization and developmental expression than its structural relative MAGP-1. Gibson, M.A., Finnis, M.L., Kumaratilake, J.S., Cleary, E.G. J. Histochem. Cytochem. (1998) [Pubmed]
  12. Purification of fibrillin-containing microfibrils and collagen VI microfibrils by density gradient centrifugation. Kielty, C.M., Hanssen, E., Shuttleworth, C.A. Anal. Biochem. (1998) [Pubmed]
  13. The pattern of fibrillin deposition correlates with microfibril-associated glycoprotein 1 (MAGP-1) expression in cultured blood and lymphatic endothelial cells. Weber, E., Rossi, A., Solito, R., Aglianò, M., Sacchi, G., Gerli, R. Lymphology. (2004) [Pubmed]
  14. Isolation and characterization of a 36-kDa microfibril-associated glycoprotein by the newly synthesized isoquinolinesulfonamide affinity chromatography. Kobayashi, R., Mizutani, A., Hidaka, H. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  15. Microfibril-associated glycoprotein-1 (MAGP-1) is specifically located on the beads of the beaded-filament structure for fibrillin-containing microfibrils as visualized by the rotary shadowing technique. Henderson, M., Polewski, R., Fanning, J.C., Gibson, M.A. J. Histochem. Cytochem. (1996) [Pubmed]
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