[HTML][HTML] The integrin α9β1 binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin
Y Yokosaki, N Matsuura, T Sasaki, I Murakami… - Journal of Biological …, 1999 - ASBMB
The integrin α 9 β 1 mediates cell adhesion to tenascin-C and VCAM-1 by binding to
sequences distinct from the common integrin-recognition sequence, arginine-glycine-
aspartic acid (RGD). A thrombin-cleaved NH 2-terminal fragment of osteopontin containing
the RGD sequence has recently been shown to also be a ligand for α 9 β 1. In this report, we
used site-directed mutagenesis and synthetic peptides to identify the α 9 β 1 recognition
sequence in osteopontin. α 9-transfected SW480, Chinese hamster ovary, and L-cells …
sequences distinct from the common integrin-recognition sequence, arginine-glycine-
aspartic acid (RGD). A thrombin-cleaved NH 2-terminal fragment of osteopontin containing
the RGD sequence has recently been shown to also be a ligand for α 9 β 1. In this report, we
used site-directed mutagenesis and synthetic peptides to identify the α 9 β 1 recognition
sequence in osteopontin. α 9-transfected SW480, Chinese hamster ovary, and L-cells …