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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 Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Andrews, D. A. Articles by Low, P. S. Search for Related Content PubMed PubMed Citation Articles by Andrews, D. A. Articles by Low, P. S. Related Collections Red Cells Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 November 2002, Vol. 100, No. 9, pp. 3392-3399 RED CELLS Phorbol ester stimulates a protein kinase C-mediated agatoxin-TK-sensitive calcium permeability pathway in human red blood cells Dina A. Andrews, Lu Yang, and Philip S. Low From the Departments of Veterinary Pathobiology and Chemistry, Purdue University, West Lafayette, IN. Calcium entry into mature erythrocytes (red blood cells; RBCs) is associated with multiple changes in cell properties. At low intracellular Ca2+, efflux of potassium and water predominates, leading to changes in erythrocyte rheology. At higher Ca2+ content, activation of kinases and phosphatases, rupture of membrane-to-skeleton bridges, stimulation of a phospholipid scramblase and phospholipase C, and induction of transglutaminase-mediated protein cross-linking are also observed. Because the physiologic relevance of these latter responses depends partially on whether Ca2+ entry involves a regulated channel or nonspecific leak, we explored mechanisms that initiate controlled Ca2+ influx. Protein kinase C (PKC) was considered a prime candidate for the pathway regulator, and phorbol-12 myristate-13 acetate (PMA), a stimulator of PKC, was examined for its influence on erythrocyte Ca2+. PMA was found to stimulate a rapid, dose-dependent influx of calcium, as demonstrated by the increased fluorescence of an entrapped Ca2+-sensitive dye, Fluo-3/AM. The PMA-induced entry was inhibited by staurosporine and the PKC-selective inhibitor chelerythrine chloride, but was activated by the phosphatase inhibitors okadaic acid and calyculin A. The PMA-promoted calcium influx was also inhibited by -agatoxin-TK, a calcium channel blocker specific for Cav2.1 channels. To confirm that a Cav2.1-like calcium channel exists in the mature erythrocyte membrane, RBC membrane preparations were immunoblotted with antiserum against the 1A subunit of the channel. A polypeptide of the expected molecular weight (190 kDa) was visualized. These studies indicate that an -agatoxin-TK-sensitive, Cav2.1-like calcium permeability pathway is present in the RBC membrane and that it may function under the control of kinases and phosphatases. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C.-A. Chen, L. J. Druhan, S. Varadharaj, Y.-R. Chen, and J. L. Zweier Phosphorylation of Endothelial Nitric-oxide Synthase Regulates Superoxide Generation from the Enzyme J. Biol. Chem., October 3, 2008; 283(40): 27038 - 27047. [Abstract] [Full Text] [PDF] M. Foller, R. S. Kasinathan, S. Koka, S. M. Huber, B. Schuler, J. Vogel, M. Gassmann, and F. Lang Enhanced susceptibility to suicidal death of erythrocytes from transgenic mice overexpressing erythropoietin Am J Physiol Regulatory Integrative Comp Physiol, September 1, 2007; 293(3): R1127 - R1134. [Abstract] [Full Text] [PDF] A. Akel, C. A. Wagner, J. 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	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020