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J. Biol. Chem., Vol. 263, Issue 36, 19433-19436, 12, 1988
A Oldberg, A Franzen, D Heinegard, M Pierschbacher and E Ruoslahti
Bone sialoprotein (BSP) is an extracellular matrix glycoprotein associated
with the mineral bone matrix. The amino acid sequence of BSP contains an
Arg-Gly-Asp (RGD) sequence which confers to the protein cell binding
properties (Oldberg, A., Franzen, A., and Heinegard, D. (1988) J. Biol.
Chem. 263, 19430-19432). When BSP was used as an affinity matrix to isolate
a cell surface receptor from rat osteosarcoma cells, a protein composed of
polypeptides similar in size to those of a previously characterized
vitronectin receptor was obtained. This putative BSP receptor, like the
vitronectin receptor, bound also to an affinity matrix made of an
RGD-containing heptapeptide. Moreover, similar patterns of inhibition of
cell attachment to BSP and vitronectin was obtained with variant RGD-
containing peptides, with BSP and with vitronectin. Finally, an anti-
vitronectin receptor antiserum immunoprecipitated a receptor identical in
size to the receptor bound to a BSP affinity matrix. These results show
that BSP is recognized by an RGD-directed receptor and that both
vitronectin and BSP can bind to this receptor.
Identification of a bone sialoprotein receptor in osteosarcoma cells
Department of Physiological Chemistry, University of Lund, Sweden.
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