Disease relevance of Mfap2

• We assessed the mechanical and nonlinear properties of the respiratory system, the alveolar structure, and the levels of microfibril-associated glycoproteins (MAGP) 1 and 2 in Tsk mice with developmental emphysema; in Pa mice, which are thought to develop adult onset emphysema; and their background, the C57BL/6 mice, at an age of 7 wk [1].

High impact information on Mfap2

• The related microfibrillar protein MAGP-1 was also found to interact with DSL ligands but, unlike MAGP-2, was unable to facilitate the shedding of Jagged1 [2].
• Elastic fibers are composed of the protein elastin and a network of 10-12-nm microfibrils, which are composed of several glycoproteins, including fibrillin-1, fibrillin-2, and MAGP1/2 (microfibril-associated glycoproteins-1 and -2) [2].
• Identification of a matrix-binding domain in MAGP1 and MAGP2 and intracellular localization of alternative splice forms [3].
• 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 [4].
• Two naturally occurring MAGP1 splice variants, MAGP1B (human-specific) and MAGP1D (found in mice), localized intracellularly when expressed as chimeric proteins with green fluorescent protein in rat lung fibroblasts [3].

Biological context of Mfap2

• Mapping of transcriptionally active regions in the 5' flanking sequence identified a region, located between nucleotides -339 and -109 as the Mfap2 basal promoter [5].
• Analysis of this clone indicated that Magp is fragmented into 9 exons, with the initiator Met codon located in exon 2 [6].

Anatomical context of Mfap2

• The basal transcriptional regulation of Mfap2 in muscle cells is discussed [5].
• Consistent with this idea, the Magp transcript appeared to be the widespread product of mesenchymal/connective tissue cells throughout mouse development [6].

Physical interactions of Mfap2

• In ligand blot assays, MAGP1 bound to fibronectin, fibrinogen, and von Willebrand factor, but von Willebrand factor was the only protein of the 3 that bound to MAGP1 in surface plasmon resonance studies [7].

Other interactions of Mfap2

• Furthermore, the absence of immunoreactivity with anti-MAGP on the fibrillin-containing endothelial cell connecting filaments raises the possibility that microfibrils may consist of a family of related filaments rather than a single structural entity [8].
• In contrast, the adjacent 'elastin-associated microfibrils' showed a very strong immunoreaction with anti-MP340 and a moderate reaction with anti-MAGP [8].
• The Mfap2 gene encodes the microfibril-associated glycoprotein-1 (MAGP1), an extracellular matrix protein of microfibrillar structures [5].

References