Microfibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via αVβ3 integrin

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dc.contributor.authorGibson, M.
dc.contributor.authorLeavesley, D.
dc.contributor.authorAshman, L.
dc.date.issued1999
dc.description.abstractMicrofibril-associated glycoprotein (MAGP)-1 and MAGP-2 are small structurally related glycoproteins that are specifically associated with fibrillin-containing microfibrils. MAGP-2, unlike MAGP-1, contains an RGD motif with potential for integrin binding. To determine if the RGD sequence is active, a series of cell binding assays was performed. MAGP-2 was shown to promote the attachment and spreading of bovine nuchal ligament fibroblasts when coated onto plastic wells in molar quantities similar to those of fibronectin. In contrast, approximately 10-fold more MAGP-1 was required to support comparable levels of cell adhesion. The fibroblast binding to MAGP-2 was completely inhibited if the peptide GRGDSP or the MAGP-2-specific peptide GVSGQRGDDVTTVTSET was added to the reaction medium at a 10 microM final concentration. The control peptide GRGESP had no effect on the interaction. These findings indicate that the cell interaction with MAGP-2 is an RGD-mediated event. A monoclonal antibody to human alphaVbeta3 integrin (LM609) almost completely blocked cell attachment to MAGP-2 when added to the medium at 0.5 microgram/ml, whereas two monoclonal antibodies specific for the human beta1 integrin subunit, 4B4 (blocking) and QE2.E5 (activating), had no effect even at 10 microgram/ml. Fetal bovine aortic smooth muscle cells, ear cartilage chondrocytes, and arterial endothelial cells and human skin fibroblasts and osteoblasts were also observed to adhere strongly to MAGP-2. In addition, each cell type was able to spread on MAGP-2 substrate, with the exception of the endothelial cells, which remained spherical after 2 h of incubation. The binding of each cell type was blocked when the anti-alphaVbeta3 integrin antibody was included in the assay, indicating that alphaVbeta3 integrin is the major receptor for MAGP-2 on several cell types. Thus, MAGP-2 may mediate interactions between fibrillin-containing microfibrils and cell surfaces during the development of a variety of tissues.
dc.identifier.citationJournal of Biological Chemistry, 1999; 274(19):13060-13065
dc.identifier.doi10.1074/jbc.274.19.13060
dc.identifier.issn0021-9258
dc.identifier.issn1083-351X
dc.identifier.urihttp://hdl.handle.net/2440/5664
dc.language.isoen
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.source.urihttps://doi.org/10.1074/jbc.274.19.13060
dc.subjectCell Line
dc.subjectAnimals
dc.subjectCattle
dc.subjectHumans
dc.subjectOligopeptides
dc.subjectContractile Proteins
dc.subjectReceptors, Vitronectin
dc.subjectExtracellular Matrix Proteins
dc.subjectAntibodies, Monoclonal
dc.subjectCell Adhesion
dc.subjectCell Movement
dc.subjectAmino Acid Sequence
dc.subjectProtein Binding
dc.subjectMolecular Sequence Data
dc.subjectAdult
dc.subjectRNA Splicing Factors
dc.titleMicrofibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via αVβ3 integrin
dc.title.alternativeMicrofibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via alphaVbeta3 integrin
dc.typeJournal article
pubs.publication-statusPublished

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