Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/5664
Citations
Scopus Web of Science® Altmetric
?
?
Full metadata record
DC FieldValueLanguage
dc.contributor.authorGibson, M.-
dc.contributor.authorLeavesley, D.-
dc.contributor.authorAshman, L.-
dc.date.issued1999-
dc.identifier.citationJournal of Biological Chemistry, 1999; 274(19):13060-13065-
dc.identifier.issn0021-9258-
dc.identifier.issn1083-351X-
dc.identifier.urihttp://hdl.handle.net/2440/5664-
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.language.isoen-
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC-
dc.source.urihttp://dx.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-
dc.identifier.doi10.1074/jbc.274.19.13060-
pubs.publication-statusPublished-
Appears in Collections:Aurora harvest
Pathology publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.