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Gene Review

MFAP2  -  microfibrillar-associated protein 2

Homo sapiens

Synonyms: MAGP, MAGP-1, MAGP1, MFAP-2, Microfibril-associated glycoprotein 1, ...
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Disease relevance of MFAP2


High impact information on MFAP2


Biological context of MFAP2

  • Characterization of the human gene for microfibril-associated glycoprotein (MFAP2), assignment to chromosome 1p36.1-p35, and linkage to D1S170 [7].
  • Fragments of tropoelastin corresponding to the N-terminal, C-terminal, and central regions of the molecule were used to characterize the MAGP-1 binding site [8].
  • Like the bovine and murine loci, the human gene has eight coding exons, but it contains two alternatively used 5' untranslated exons, whereas only one untranslated exon was described in the bovine and murine Magp genes [7].
  • In contrast, approximately 10-fold more MAGP-1 was required to support comparable levels of cell adhesion [9].
  • Reduction and alkylation of disulfide bonds in MAGP-1 did not destroy its type VI collagen-binding properties, indicating that the binding site was likely to be in the cysteine-free, N-terminal domain of MAGP-1 [10].

Anatomical context of MFAP2


Associations of MFAP2 with chemical compounds

  • MAGP-2 lacks the proline-, glutamine-, and tyrosine-rich sequences and a hydrophobic carboxyl terminus, characteristic of MAGP-1 [13].
  • MAGP-1 mRNA levels in cultured keratinocytes during Ca(++)-induced differentiation were enhanced eightfold with a concomitant increase in involucrin (a marker of terminal differentiation) mRNA levels [12].
  • Comparison with the previously characterized human MAGP-1 gene showed that structural similarity was largely confined to the exact size, sequence, and junction alignment of the two penultimate exons which encode the first six of the seven cysteine residues that are precisely spaced in both proteins [14].
  • MAGP was extractable from tissue homogenates using NaCl, urea, or guanidine hydrochloride solutions, only if a strong reducing agent was present [15].
  • MAGP is an acidic glycoprotein with a distinctive amino acid composition, being exceptionally rich in glutamic acid, rich in cystine, and low in glycine [15].

Physical interactions of MFAP2

  • Refolding of the purified protein produced a soluble form of MAGP-1 that displayed saturable binding to tropoelastin [8].
  • MAGP-1 bound to a region at the N terminus of fibrillin-1 in a calcium-dependent manner [8].

Regulatory relationships of MFAP2

  • Decorin and biglycan were found not to inhibit the interaction of pepsin-treated type VI collagen with MAGP-1, indicating that its binding site on the collagen is not close to that for the proteoglycans [10].

Other interactions of MFAP2

  • In addition, no evidence of an interaction was observed between MAGP-1 and a tropoelastin construct consisting of domains 17-27 that brackets the kallikrein cleavage site, suggesting a complex mechanism of interaction between the two molecules [8].
  • Binding of MAGP-1 was also tested with overlapping recombinant fibrillin-1 fragments [8].
  • MAGP and fibrillin were also substrates for transglutaminase, which may provide an important mechanism for stabilizing microfibrillar structure [16].
  • Conditions have been defined that permit precise localization within the extracellular matrix of antibodies to MAGP and to elastin, singly and together [17].
  • The exon structure of the human MAGP-2 gene. Similarity with the MAGP-1 gene is confined to two exons encoding a cysteine-rich region [14].

Analytical, diagnostic and therapeutic context of MFAP2


  1. Expression of 36-kDa microfibril-associated glycoprotein (MAGP-36) in human keratinocytes and its localization in skin. Hirano, E., Fujimoto, N., Tajima, S., Akiyama, M., Ishibashi, A., Kobayashi, R., Okamoto, K. J. Dermatol. Sci. (2002) [Pubmed]
  2. Expression of PNA-binding sites on specific glycoproteins by human melanoma cells is associated with a high metastatic potential. Zebda, N., Bailly, M., Brown, S., Doré, J.F., Berthier-Vergnes, O. J. Cell. Biochem. (1994) [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. Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation. Miyamoto, A., Lau, R., Hein, P.W., Shipley, J.M., Weinmaster, G. J. Biol. Chem. (2006) [Pubmed]
  5. MAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrils. Hanssen, E., Hew, F.H., Moore, E., Gibson, M.A. J. Biol. Chem. (2004) [Pubmed]
  6. Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1. Reinboth, B., Hanssen, E., Cleary, E.G., Gibson, M.A. J. Biol. Chem. (2002) [Pubmed]
  7. Characterization of the human gene for microfibril-associated glycoprotein (MFAP2), assignment to chromosome 1p36.1-p35, and linkage to D1S170. Faraco, J., Bashir, M., Rosenbloom, J., Francke, U. Genomics (1995) [Pubmed]
  8. Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1. Jensen, S.A., Reinhardt, D.P., Gibson, M.A., Weiss, A.S. J. Biol. Chem. (2001) [Pubmed]
  9. Microfibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via alphaVbeta3 integrin. Gibson, M.A., Leavesley, D.I., Ashman, L.K. J. Biol. Chem. (1999) [Pubmed]
  10. Microfibril-associated glycoprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the alpha3(VI) chain of type VI collagen. Finnis, M.L., Gibson, M.A. J. Biol. Chem. (1997) [Pubmed]
  11. Ultrastructural immunocytochemical analysis of elastin in the human lamina cribrosa. Changes in elastic fibers in primary open-angle glaucoma. Hernandez, M.R. Invest. Ophthalmol. Vis. Sci. (1992) [Pubmed]
  12. Expression of microfibril-associated glycoprotein-1 (MAGP-1) in human epidermal keratinocytes. Fujimoto, N., Tajima, S., Ishibashi, A. Arch. Dermatol. Res. (2000) [Pubmed]
  13. Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25). Gibson, M.A., Hatzinikolas, G., Kumaratilake, J.S., Sandberg, L.B., Nicholl, J.K., Sutherland, G.R., Cleary, E.G. J. Biol. Chem. (1996) [Pubmed]
  14. The exon structure of the human MAGP-2 gene. Similarity with the MAGP-1 gene is confined to two exons encoding a cysteine-rich region. Hatzinikolas, G., Gibson, M.A. J. Biol. Chem. (1998) [Pubmed]
  15. The major antigen of elastin-associated microfibrils is a 31-kDa glycoprotein. Gibson, M.A., Hughes, J.L., Fanning, J.C., Cleary, E.G. J. Biol. Chem. (1986) [Pubmed]
  16. Elastic fibre assembly: macromolecular interactions. Mecham, R.P., Broekelmann, T., Davis, E.C., Gibson, M.A., Brown-Augsburger, P. Ciba Found. Symp. (1995) [Pubmed]
  17. Post-embedding methods for immunolocalization of elastin and related components in tissues. White, J.F., Hughes, J.L., Kumaratilake, J.S., Fanning, J.C., Gibson, M.A., Krishnan, R., Cleary, E.G. J. Histochem. Cytochem. (1988) [Pubmed]
  18. Ultrastructural distribution of 36-kD microfibril-associated glycoprotein (MAGP-36) in human and bovine tissues. Toyoshima, T., Yamashita, K., Furuichi, H., Shishibori, T., Itano, T., Kobayashi, R. J. Histochem. Cytochem. (1999) [Pubmed]
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