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Gene Review

MFAP5  -  microfibrillar associated protein 5

Homo sapiens

Synonyms: AAT9, MAGP-2, MAGP2, MFAP-5, MP25, ...
 
 
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Disease relevance of MFAP5

  • These results provide evidence that the expression of terminal galactose (beta 1-3)N-acetyl galactosamine structure, positioned on MAGP1 and MAGP2 glycoproteins, is associated with the metastatic potential of human melanoma cells [1].
 

High impact information on MFAP5

 

Biological context of MFAP5

 

Anatomical context of MFAP5

 

Associations of MFAP5 with chemical compounds

 

Physical interactions of MFAP5

  • Moreover, we demonstrate that the C-terminal domain of MAGP-2 is required for binding and activation of Notch1 [3].
 

Other interactions of MFAP5

  • 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 [5].
  • Analysis by immunofluorescent staining showed that MAGP-2 overexpression dramatically increased elastic fibers levels, independently of extracellular levels of soluble tropoelastin, indicating that MAGP-2 stimulates elastic fiber assembly [2].

References

  1. 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]
  2. Microfibril-associated MAGP-2 Stimulates Elastic Fiber Assembly. Lemaire, R., Bayle, J., Mecham, R.P., Lafyatis, R. J. Biol. Chem. (2007) [Pubmed]
  3. 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]
  4. 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]
  5. 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]
 
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