Disease relevance of Mfap5

• Increased expression of type I collagen induced by microfibril-associated glycoprotein 2: novel mechanistic insights into the molecular basis of dermal fibrosis in scleroderma [1].
• Our findings suggest the possibility that MAGP-2-related abnormal collagen assembly, combined with mechanical forces, is involved in the progression of emphysema in the Tsk mice [2].

High impact information on Mfap5

• Our findings suggest that in addition to its role in microfibrils, MAGP-2 may also affect cellular differentiation through modulating the Notch signaling pathway either by binding to cell surface DSL ligands or by facilitating release and/or stabilization of a soluble extracellular form of Jagged1 [3].
• MAGP-2 induced type I collagen even under conditions in which no MAGP-2 matrix was detectable, and did not require the presence of the RGD motif of MAGP-2 in its integrin-binding site [1].
• METHODS: Fibroblast cultures conditionally overexpressing MAGP-2 were developed [1].
• CONCLUSION: This study shows that MAGP-2 stabilizes type I procollagen, identifying an important function of MAGP-2 in extracellular matrix homeostasis [1].
• Moreover, MEF cells expressing tsk-Fbn1 showed increased MAGP-2 matrix [4].

Biological context of Mfap5

• Sequence analysis of additional cDNA clones suggests that the two mRNA forms of MAGP-2 in the mouse arise from alternative polyadenylation site usage [5].
• A 1.4-kb EST clone encoding mouse microfibril-associated glycoprotein-2 (MAGP-2), identified by its similarity with the reported human cDNA, was used to screen a mouse 129 genomic bacterial artificial chromosome (BAC) library [5].

Anatomical context of Mfap5

• Fibrotic SSc skin also showed higher levels of MAGP-2 in the dermis than nonfibrotic SSc skin and normal skin [4].
• Immunoprecipitation of MAGP-2 from transfected COS-7 cells resulted in the coprecipitation of fibrillin [6].
• Northern analysis demonstrates abundant expression of MAGP-2 mRNA in skeletal muscle, lung, and heart [5].

Associations of Mfap5 with chemical compounds

• Deletion analysis of the MAGP-2 bait demonstrated that binding occurred in a core region containing 48% identity and 7 conserved cysteine residues with MAGP-1 [6].

Other interactions of Mfap5

• Identification of a matrix-binding domain in MAGP1 and MAGP2 and intracellular localization of alternative splice forms [7].

Analytical, diagnostic and therapeutic context of Mfap5

• The skin of TSK mice and SSc patients was analyzed by immunohistochemistry for MAGP-2 expression [4].
• Cells were analyzed by Western blotting, Northern blotting, pulse-chase analysis, and immunofluorescence to assess the effect of MAGP-2 on type I collagen [1].

References