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001-es BibID:	BIBFORM004658
Első szerző:	Burgess, Janette K.
Cím:	Physical proximity and functional association of glycoprotein 1balpha and protein-disulfide isomerase on the platelet plasma membrane / Burgess, J. K., Hotchkiss, K. A., Suter, C., Dudman, N. P., Szollosi, J., Chesterman, C. N., Chong, B. H., Hogg, P. J.
Dátum:	2000
Megjegyzések:	Platelet function is influenced by the platelet thiol-disulfide balance. Platelet activation resulted in 440% increase in surface protein thiol groups. Two proteins that presented free thiol(s) on the activated platelet surface were protein-disulfide isomerase (PDI) and glycoprotein 1balpha (GP1balpha). PDI contains two active site dithiols/disulfides. The active sites of 26% of the PDI on resting platelets was in the dithiol form, compared with 81% in the dithiol form on activated platelets. Similarly, GP1balpha presented one or more free thiols on the activated platelet surface but not on resting platelets. Anti-PDI antibodies increased the dissociation constant for binding of vWF to platelets by approximately 50% and PDI and GP1balpha were sufficiently close on the platelet surface to allow fluorescence resonance energy transfer between chromophores attached to PDI and GP1balpha. Incubation of resting platelets with anti-PDI antibodies followed by activation with thrombin enhanced labeling and binding of monoclonal antibodies to the N-terminal region of GP1balpha on the activated platelet surface. These observations indicated that platelet activation triggered reduction of the active site disulfides of PDI and a conformational change in GP1balpha that resulted in exposure of a free thiol(s).
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Antibodies blood Blood Platelets Cell Membrane chemistry Disulfides Energy Transfer enzymology Fluorescence Glycoproteins Human immunology Membrane Glycoproteins metabolism Molecular Weight pathology Platelet Activation Platelet Aggregation Platelet Membrane Glycoproteins Protein Disulfide-Isomerase Proteins Research Sulfhydryl Compounds Support, Non-U.S.Gov't Thrombin von Willebrand Factor
Megjelenés:	The Journal of Biological Chemistry. - 275 : 13 (2000), p. 9758-9766. -
További szerzők:	Hotchkiss, Kylie A. Suter, Catherine Dudman, Nicholas P. B. Szöllősi János (1953-) (biofizikus) Chesterman, Colin N. Chong, Beng H. Hogg, Philip J.
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