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J Biol Chem, Vol. 275, Issue 13, 9758-9766, March 31, 2000
From the 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 1b
Physical Proximity and Functional Association of Glycoprotein
1b
and Protein-disulfide Isomerase on the Platelet Plasma
Membrane*
§,§,
,,, and
Centre for Thrombosis and Vascular Research,
School of Pathology, University of New South Wales and the Department
of Haematology, Prince of Wales Hospital, Sydney NSW 2052, Australia,
the ¶ Department of Molecular and Cellular Oncology, St.
Vincent's Hospital, Garvan Institute of Medical Research, Darlinghurst
NSW 2010, Australia, the Department of Cardiovascular Medicine,
Prince Henry Hospital, Little Bay NSW 2036, Australia, and the
** Department of Biophysics and Cell Biology, Medical University School
of Debrecen, Debrecen 4012, Hungary
(GP1b). 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, GP1b 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 ~50% and PDI and GP1b
were sufficiently close on the platelet surface to allow fluorescence
resonance energy transfer between chromophores attached to PDI and
GP1b. 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 GP1b 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 GP1b that resulted in exposure of a free thiol(s).
*
This work was supported by grants from the National Health
and Medical Research Council of Australia, the National Heart
Foundation of Australia, and an Infrastructure Grant from the New South
Wales Health Department.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Centre for
Thrombosis and Vascular Research, School of Pathology, University of New South Wales, Sydney NSW, 2052 Australia. Tel.: 61-2-9385-1004; Fax:
61-2-9385-1389; E-mail: p.hogg@unsw.edu.au.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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