TY - JOUR
T1 - Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells
AU - Cheresh, David A.
AU - Berliner, Shlomo A.
AU - Vicente, Vicente
AU - Ruggeri, Zaverio M.
N1 - Funding Information:
This work was supported by National Institutes of Health grants CA45726 (D. A C.) and HL31950 and HL37522 (2. M. IR.). We wish to thank Regina Derango, Diane Sander, and James R. Rloberts for their expert technical assistance. We also thank Drs. R. A. Reisfeld, J. W. Smith, and D. Vestal for critical review and Ms. Lynne Kottel for preparation of this manuscript. This is manuscript number 5908-IMM-CVB from the Research Institute of Scripps Clinic.
PY - 1989/9/8
Y1 - 1989/9/8
N2 - Endothelial cells and activated platelets express integrin-type receptors responsible for adhesion to fibrinogen. We have located distinct integrin-directed endothelial cell and platelet attachment sites on immobilized fibrinogen using a combination of synthetic peptides, fibrinogen fragments, and specific anti-peptide monoclonal antibodies. Endothelial cells exclusively recognize an Arg-Gly-Asp-containing site near the C-terminus of the α chain (α residues 572-574) but fail to recognize the Arg-Gly-Asp sequence in the N-terminal region of the same chain (α residues 95-97). In contrast, platelets do not require either Arg-Gly-Asp sequence for binding to intact fibrinogen and are capable of recognizing, in addition to the α 572-574 sequence, a site at the C-terminus of the γ chain (γ residues 400-411). These data suggest a molecular mechanism whereby platelets and endothelial cells interact with distinct sites on the fibrinogen molecule during hemostasis and wound healing.
AB - Endothelial cells and activated platelets express integrin-type receptors responsible for adhesion to fibrinogen. We have located distinct integrin-directed endothelial cell and platelet attachment sites on immobilized fibrinogen using a combination of synthetic peptides, fibrinogen fragments, and specific anti-peptide monoclonal antibodies. Endothelial cells exclusively recognize an Arg-Gly-Asp-containing site near the C-terminus of the α chain (α residues 572-574) but fail to recognize the Arg-Gly-Asp sequence in the N-terminal region of the same chain (α residues 95-97). In contrast, platelets do not require either Arg-Gly-Asp sequence for binding to intact fibrinogen and are capable of recognizing, in addition to the α 572-574 sequence, a site at the C-terminus of the γ chain (γ residues 400-411). These data suggest a molecular mechanism whereby platelets and endothelial cells interact with distinct sites on the fibrinogen molecule during hemostasis and wound healing.
UR - http://www.scopus.com/inward/record.url?scp=0024428206&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(89)90946-X
DO - 10.1016/0092-8674(89)90946-X
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C2 - 2673537
AN - SCOPUS:0024428206
VL - 58
SP - 945
EP - 953
JO - Cell
JF - Cell
SN - 0092-8674
IS - 5
ER -