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J Biol Chem, Vol. 274, Issue 19, 13060-13065, May 7, 1999

Microfibril-associated Glycoprotein-2 Specifically Interacts with a Range of Bovine and Human Cell Types via _V3 Integrin

Mark A. Gibson, David I. Leavesley^¶, and Leonie K. Ashman

From the  Department of Pathology, University of Adelaide, Adelaide, South Australia 5005 and the ^¶ Renal Unit, Royal Adelaide Hospital and the  Hanson Centre for Cancer Research, Institute of Medical and Veterinary Science, Adelaide, South Australia 5000, Australia

Microfibril-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, ~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 µM 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 _V3 integrin (LM609) almost completely blocked cell attachment to MAGP-2 when added to the medium at 0.5 µg/ml, whereas two monoclonal antibodies specific for the human ₁ integrin subunit, 4B4 (blocking) and QE2.E5 (activating), had no effect even at 10 µg/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-_V3 integrin antibody was included in the assay, indicating that _V3 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.

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