Donate Help Contact The AHA Sign In Home
American Heart Association
Arteriosclerosis, Thrombosis, and Vascular Biology
Search: search_blue_button Advanced Search
« Previous Article | Table of Contents | Next Article »
Arteriosclerosis, Thrombosis, and Vascular Biology. 1991;11:882-891

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wencel-Drake, J. D.
Right arrow Articles by Kunicki, T. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wencel-Drake, J. D.
Right arrow Articles by Kunicki, T. J.

Arteriosclerosis and Thrombosis, Vol 11, 882-891, Copyright © 1991 by American Heart Association

ARTICLES

Activation of calpain I and hydrolysis of calpain substrates (actin- binding protein, glycoprotein Ib, and talin) are not a function of thrombin-induced platelet aggregation

JD Wencel-Drake, JR Okita, DS Annis and TJ Kunicki
Department of Medical Laboratory Sciences, University of Illinois, Chicago 60612.

Calcium-activated neutral proteinase (calpain) has been shown to cleave proteins involved in the maintenance of cell structure. In human platelets, substrates of calpain include glycoprotein Ib (GPIb), actin- binding protein (ABP), and talin. GPIb-ABP complexes can be isolated in detergent extracts and are thought to represent membrane-cytoskeleton attachment sites. It has been hypothesized that the hydrolysis of GPIb- ABP by calpain is regulated by the extent of binding of this proteinase to the plasma membrane-cytoskeleton interface with platelet activation. Recently, another calpain substrate (talin) has been shown to redistribute from the cytoplasm to the plasma membrane-cytoskeleton interface as the result of thrombin stimulation. To investigate the intracellular distribution of calpain I, we employed the monoclonal antibody B27D8, specific for the heavy chain (catalytic subunit) of calpain I. Indirect immunofluorescent staining of resting human platelets revealed undetectable surface antigen. Permeabilization with Triton X-100, however, revealed a diffuse intracellular antigen consistent with a cytosolic distribution. To determine whether this antigen distribution reflected the proenzyme or the activated form of calpain I and to assess the degree of hydrolysis of ABP, GPIb, and talin, we employed B27D8 and murine monoclonal antibodies against ABP (1B3 and 3D1), GPIb (LJIb10), and rabbit polyclonal antibodies against talin (A2 and B11) in a quantitative immunotransblot assay. Examination of resting platelets revealed that calpain I existed as the 85-kd proenzyme form and that ABP, GPIb, and talin existed in their native intact forms. When platelets were aggregated with thrombin, autoproteolysis of calpain I occurred within the 30 seconds required to completely solubilize platelet aggregates in sodium dodecyl sulfate- containing buffer and not as a direct result of thrombin-induced activation.(ABSTRACT TRUNCATED AT 250 WORDS)


This article has been cited by other articles:


Home page
 BloodHome page
A. Oda, H. Miki, I. Wada, H. Yamaguchi, D. Yamazaki, S. Suetsugu, M. Nakajima, A. Nakayama, K. Okawa, H. Miyazaki, et al.
WAVE/Scars in platelets
Blood, April 15, 2005; 105(8): 3141 - 3148.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
A. Oda, H. Wakao, and H. Fujita
Calpain is a signal transducer and activator of transcription (STAT) 3 and STAT5 protease
Blood, March 1, 2002; 99(5): 1850 - 1852.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
A. Oda, H. D. Ochs, B. J. Druker, K. Ozaki, C. Watanabe, M. Handa, Y. Miyakawa, and Y. Ikeda
Collagen Induces Tyrosine Phosphorylation of Wiskott-Aldrich Syndrome Protein in Human Platelets
Blood, September 15, 1998; 92(6): 1852 - 1858.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Huang, N. N. Tandon, N. J. Greco, Y. Ni, T. Wang, and X. Zhan
Proteolysis of Platelet Cortactin by Calpain
J. Biol. Chem., August 1, 1997; 272(31): 19248 - 19252.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
Y. Miyakawa, A. Oda, B. J. Druker, K. Ozaki, M. Handa, H. Ohashi, and Y. Ikeda
Thrombopoietin and Thrombin Induce Tyrosine Phosphorylation of Vav in Human Blood Platelets
Blood, April 15, 1997; 89(8): 2789 - 2798.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
C. P.M. Hayward, E. M. Cramer, W. H. Kane, S. Zheng, M. Bouchard, J.-M. Masse, and G. E. Rivard
Studies of a Second Family With the Quebec Platelet Disorder: Evidence That the Degradation of the alpha -Granule Membrane and Its Soluble Contents Are Not Secondary to a Defect in Targeting Proteins to alpha -Granules
Blood, February 15, 1997; 89(4): 1243 - 1253.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
M. Bertagnolli, S. Locke, M. Hensler, P. Bray, and M. Beckerle
Talin distribution and phosphorylation in thrombin-activated platelets
J. Cell Sci., January 12, 1993; 106(4): 1189 - 1199.
[Abstract] [PDF]


ATVB Home | Subscriptions | Archives | Feedback | Authors | Help | AHA Journals Home | Search
Copyright © 1991 American Heart Association, Inc. All rights reserved. Unauthorized use prohibited.