This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nealen, M. L. Articles by Bray, P. F. Search for Related Content PubMed PubMed Citation Articles by Nealen, M. L. Articles by Bray, P. F. Related Collections Pathophysiology Platelets

(Circulation Research. 2001;88:438.)
© 2001 American Heart Association, Inc.

Molecular Medicine

Human Platelets Contain a Glycosylated Estrogen Receptor ß

Michele L. Nealen, K. Vinod Vijayan, Everlie Bolton, Paul F. Bray

From the Department of Medicine (M.L.N., K.V.V., E.B., P.F.B.) and the Program in Cellular and Molecular Medicine (M.L.N.), Johns Hopkins University School of Medicine, Baltimore, Md.

Correspondence to Paul F. Bray, MD, Baylor College of Medicine, Thrombosis Research Section, Department of Medicine, One Baylor Plaza, BCM 286, Room N1319, Houston, TX 77030. E-mail pbray{at}bcm.tmc.edu

Abstract—Platelets play an important role in the coronary thrombus formation that leads to myocardial ischemia and infarction. Gender differences in the development of coronary heart disease and its outcomes are partly regulated by estrogen and its receptors, but the roles of the latter in thrombogenicity are less well-defined. We previously demonstrated the presence of estrogen receptor (ER) ß in cells of the megakaryocytic lineage. In this study, we characterize human platelet ERß and its expression using biochemical and molecular biological techniques. Western immunoblotting showed that platelet ERß migrated with an apparent molecular mass 3.7 kDa larger than ERß in a variety of cell lines (including those of prostate and breast origin). A rigorous investigation of platelet ERß mRNA by reverse transcriptase–polymerase chain reaction revealed normal transcripts and a single alternately spliced mRNA. However, this variant form was smaller, lacking exon 2, and could not account for the larger protein size seen in platelets. Treatment of ERß with N-glycosidase F, which removes core carbohydrate residues, caused a more rapid migration through polyacrylamide gels but had no effect on ERß from human cell lines. We conclude that the larger form of ERß in human platelets is not attributable to alternate mRNA splicing but primarily to tissue-specific glycosylation.

Key Words: platelet • estrogen receptor • glycosylation

This article has been cited by other articles:

				K. Aschbacher, R. von Kanel, P. J. Mills, S. Hong, S. K. Roepke, B. T. Mausbach, T. L. Patterson, M. G. Ziegler, J. E. Dimsdale, S. Ancoli-Israel, et al. Combination of Caregiving Stress and Hormone Replacement Therapy is Associated With Prolonged Platelet Activation to Acute Stress Among Postmenopausal Women Psychosom Med, November 1, 2007; 69(9): 910 - 917. [Abstract] [Full Text] [PDF]

				O. Vitseva, D. A. Flockhart, Y. Jin, S. Varghese, and J. E. Freedman The Effects of Tamoxifen and Its Metabolites on Platelet Function and Release of Reactive Oxygen Intermediates J. Pharmacol. Exp. Ther., March 1, 2005; 312(3): 1144 - 1150. [Abstract] [Full Text] [PDF]

				J. Q. Chen, M. Delannoy, C. Cooke, and J. D. Yager Mitochondrial localization of ER{alpha} and ER{beta} in human MCF7 cells Am J Physiol Endocrinol Metab, June 1, 2004; 286(6): E1011 - E1022. [Abstract] [Full Text] [PDF]

				M. Maccarrone, M. Bari, N. Battista, and A. Finazzi-Agro Estrogen stimulates arachidonoylethanolamide release from human endothelial cells and platelet activation Blood, December 1, 2002; 100(12): 4040 - 4048. [Abstract] [Full Text] [PDF]