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. 1993;13:1567-1571

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
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 McNicol, A.
Right arrow Articles by Gerrard, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McNicol, A.
Right arrow Articles by Gerrard, J. M.

Arteriosclerosis and Thrombosis, Vol 13, 1567-1571, Copyright © 1993 by American Heart Association

ARTICLES

Phospholipase C activity in platelets from Bernard-Soulier syndrome patients

A McNicol, J Drouin, KJ Clemetson and JM Gerrard
Manitoba Institute of Cell Biology, Winnipeg, Canada.

The levels of glycoprotein (GP) Ib and GPV and phospholipase C activity were measured in platelets from three Bernard-Soulier syndrome patients. The patients' platelets had 46%, 46%, and 24% of control levels of GPIb alpha and 43%, trace, and 13% of control levels of GPV as determined by immunoblot analysis. Stimulation by thrombin, trypsin, the thromboxane analogue U46619, and the combination of U46619 and trypsin caused the formation of [32P]phosphatidic acid, an index of phospholipase C activity, in [32P]orthophosphate-prelabeled platelets. With all agonists, however, the formation of [32P]phosphatidic acid was markedly reduced in Bernard-Soulier syndrome platelets compared with control platelets. These data indicated a postreceptor defect in phospholipase C activation in Bernard-Soulier syndrome platelets and confirmed earlier observations of potential proteolytic and nonproteolytic mechanisms of platelet activation.


This article has been cited by other articles:


Home page
 BloodHome page
J. A. Lopez, R. K. Andrews, V. Afshar-Kharghan, and M. C. Berndt
Bernard-Soulier Syndrome
Blood, June 15, 1998; 91(12): 4397 - 4418.
[Full Text] [PDF]

Home page
 J. Pharmacol. Exp. Ther.Home page
A. McNicol and C. A. Robson
Thrombin Receptor-Activating Peptide Releases Arachidonic Acid from Human Platelets: A Comparison with Thrombin and Trypsin
J. Pharmacol. Exp. Ther., May 1, 1997; 281(2): 861 - 867.
[Abstract] [Full Text]

Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
A. McNicol, M. Sutherland, R. Zou, and J. Drouin
Defective Thrombin-Induced Calcium Changes and Aggregation of Bernard-Soulier Platelets Are Not Associated With Deficient Moderate-Affinity Receptors
Arterioscler Thromb Vasc Biol, May 1, 1996; 16(5): 628 - 632.
[Abstract] [Full Text]


ATVB Home | Subscriptions | Archives | Feedback | Authors | Help | AHA Journals Home | Search
Copyright © 1993 American Heart Association, Inc. All rights reserved. Unauthorized use prohibited.