TY - JOUR
T1 - Analysis of platelet adhesion with a radioactive chemical crosslinking reagent
T2 - Interaction of thrombospondin with fibronectin and collagen
AU - Lahav, Judith
AU - Schwartz, Martin Alexander
AU - Hynes, Richard O.
N1 - Funding Information:
This research was supported by grants from the U.S. Public Health Service and from the National Institutes of Health (to R. 0. H. and Michael Gimbrone). J. L. is grateful for the support of Dr. Gimbrone during the final phase of this work. R. 0. H. was the recipient of a Research Career Development Award from the U.S. Public Health Service and the National Cancer Institute. We are grateful to Dr. John Lawler (St. Elizabeth’s Hospital, Boston) for gifts of thrombospondin and antithrombospondin antiserum. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
PY - 1982/11
Y1 - 1982/11
N2 - We have analyzed the interactions of platelets and platelet-secreted proteins with proteins bound to glass substrata. Using a newly developed radioactive crosslinking reagent, N-succinimidyl-3-[(2-nitro-4-azidophenyl)-2-aminoethyldithio] propionate, we observed crosslinking between thrombospondin released from the platelets and surface-bound fibronectin or collagen. The crosslinking was selective and specific, since thrombospondin showed little crosslinking to substratum-bound bovine serum albumin or ovalbumin, even though it bound to these surfaces. Furthermore, although albumin and fibrinogen released by platelets bound to fibronectincoated substrata as well as did thrombospondin, these two proteins crosslinked at much lower levels than seen for thrombospondin. Interaction between fibronectin and thrombospondin was confirmed by affinity chromatography. These results suggest that thrombospondin and fibronectin may interact during platelet-substratum adhesion or during platelet-platelet aggregation, or both.
AB - We have analyzed the interactions of platelets and platelet-secreted proteins with proteins bound to glass substrata. Using a newly developed radioactive crosslinking reagent, N-succinimidyl-3-[(2-nitro-4-azidophenyl)-2-aminoethyldithio] propionate, we observed crosslinking between thrombospondin released from the platelets and surface-bound fibronectin or collagen. The crosslinking was selective and specific, since thrombospondin showed little crosslinking to substratum-bound bovine serum albumin or ovalbumin, even though it bound to these surfaces. Furthermore, although albumin and fibrinogen released by platelets bound to fibronectincoated substrata as well as did thrombospondin, these two proteins crosslinked at much lower levels than seen for thrombospondin. Interaction between fibronectin and thrombospondin was confirmed by affinity chromatography. These results suggest that thrombospondin and fibronectin may interact during platelet-substratum adhesion or during platelet-platelet aggregation, or both.
UR - http://www.scopus.com/inward/record.url?scp=0020366972&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(82)90425-1
DO - 10.1016/0092-8674(82)90425-1
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AN - SCOPUS:0020366972
SN - 0092-8674
VL - 31
SP - 253
EP - 262
JO - Cell
JF - Cell
IS - 1
ER -