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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 18 Mar 2014.

Microfibrillar associated protein 5

MAGP-2, Microfibril-associated glycoprotein-2
This gene encodes a 25-kD microfibril-associated glycoprotein which is rich in serine and threonine residues. It lacks a hydrophobic carboxyl terminus and proline-, glutamine-, and tyrosine-rich regions, which are characteristics of a related 31-kDa microfibril-associated glycoprotein (MFAP2). The close similarity between these two proteins is confined to a central region of 60 aa where precise alignment of 7 cysteine residues occurs. The structural differences suggest that this encoded protein has some functions that are distinct from those of MFAP2. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MAGP, fibrillin-1, CD45, elastin, HAD
Papers on MAGP-2
Microfibril-associated glycoprotein 2 (MAGP2) loss of function has pleiotropic effects in vivo.
New
Mecham et al., In J Biol Chem, Nov 2013
Using mice with a targeted inactivation of Mfap5, the gene for MAGP2 protein, we demonstrate that MAGPs have shared as well as unique functions in vivo.
Identification of a functional proprotein convertase cleavage site in microfibril-associated glycoprotein 2.
New
Miyamoto et al., Fullerton, United States. In Matrix Biol, Apr 2013
Microfibril-associated glycoprotein 2 (MAGP2) is a secreted protein associated with multiple cellular activities including the organization of elastic fibers in the extracellular matrix (ECM), angiogenesis, as well as regulating Notch and integrin signaling.
NLF2 gene expression in the endometrium of patients with implantation failure after IVF treatment.
GeneRIF
Menevse et al., Ankara, Turkey. In Gene, 2012
Decreased MFAP5 gene expression in the endometrium of patients with implantation failure after in vitro ertilization treatment
Identification of the chondrocyte lineage using microfibril-associated glycoprotein-2, a novel marker that distinguishes chondrocytes from synovial cells.
GeneRIF
Duguay et al., Cambridge, United States. In Tissue Eng Part C Methods, 2010
The MAGP2-based assay provided superior performance for the purpose of cell culture identification compared to assays using standard reference genes.
A novel fibrotic disorder associated with increased dermal fibroblast proliferation and downregulation of genes of the microfibrillar network.
Hinek et al., Honolulu, United States. In Br J Dermatol, 2010
The lack of mutations within the MAGP2 gene also excluded an MAGP2-associated disorder.
A prognostic gene signature in advanced ovarian cancer reveals a microfibril-associated protein (MAGP2) as a promoter of tumor cell survival and angiogenesis.
Banyard et al., Boston, United States. In Cell Adh Migr, 2010
Within this signature, the authors identified MAGP2, also known as microfibrillar associated protein 5 (MFAP5), as a highly significant indicator of survival and chemosensitivity.
A gene signature predictive for outcome in advanced ovarian cancer identifies a survival factor: microfibril-associated glycoprotein 2.
Impact
GeneRIF
Birrer et al., Houston, United States. In Cancer Cell, 2010
Independent evaluation confirmed the association of a prognostic gene microfibril-associated glycoprotein 2 (MAGP2) with poor prognosis in advanced ovarian cancer
Functional evolution of the microfibril-associated glycoproteins.
Segade, Philadelphia, United States. In Gene, 2009
Two MAGPs, designated MAGP1 and MAGP2, are encoded in the mammalian genome.
Microfibril-associate glycoprotein-2 (MAGP-2) promotes angiogenic cell sprouting by blocking notch signaling in endothelial cells.
GeneRIF
Schiemann et al., Terre Haute, United States. In Microvasc Res, 2008
MAGP-2 promotes angiogenic cell spouting in vitro by antagonizing Notch signaling pathways in endothelial cells.
Microfibril-associated MAGP-2 stimulates elastic fiber assembly.
GeneRIF
Lafyatis et al., Boston, United States. In J Biol Chem, 2007
microfibril-associated MAGP-2 may stimulate elastic fiber macroassembly by targeting the release of elastin globules from the cell membrane onto developing elastic fibers
Early emphysema in the tight skin and pallid mice: roles of microfibril-associated glycoproteins, collagen, and mechanical forces.
Suki et al., Boston, United States. In Am J Respir Cell Mol Biol, 2006
However, the level of MAGP-2, which is associated with both fibrillin-1 and collagen, was higher in the Tsk than in the Pa mice, which also had more MAGP-2 than the C57BL/6.
Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation.
GeneRIF
Weinmaster et al., Los Angeles, United States. In J Biol Chem, 2006
microfibrillar proteins MAGP-1 and MAGP-2 can function outside of their role in elastic fibers to activate a cellular signaling pathway
Increased expression of type I collagen induced by microfibril-associated glycoprotein 2: novel mechanistic insights into the molecular basis of dermal fibrosis in scleroderma.
Lafyatis et al., Boston, United States. In Arthritis Rheum, 2005
Previous studies have suggested that fibrillin 1 mediates skin fibrosis via its interface with associated microfibrillar proteins and type I collagen; in particular, microfibril-associated glycoprotein 2 (MAGP-2), an extracellular matrix protein that binds to fibrillins and the alphavbeta3 integrin, is increased in TSK mouse and human scleroderma skin.
The extracellular matrix protein MAGP-2 interacts with Jagged1 and induces its shedding from the cell surface.
Shipley et al., Saint Louis, United States. In J Biol Chem, 2005
Although fibrillins and MAGPs covalently associate, we find that the DSL (Delta/Serrate/LAG2) protein Jagged1, an activating ligand for Notch receptor signaling, also interacts with MAGP-2 in both yeast two-hybrid and coimmunoprecipitation studies.
MAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrils.
GeneRIF
Gibson et al., Adelaide, Australia. In J Biol Chem, 2004
results show MAGP-2 is covalently and periodically located along the fibrillin-containing microfibrils of the developing nuchal ligament, suggesting that it is an integral component of most if not all of the microfibrils in this elastic fiber-rich tissue
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