{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T01:28:36Z","timestamp":1790731716545,"version":"4.1.0"},"reference-count":75,"publisher":"American Society of Hematology","issue":"9","content-domain":{"domain":["ashpublications.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2002,11,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>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 \u03c9-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 \u03b11A subunit of the channel. A polypeptide of the expected molecular weight (190 kDa) was visualized. These studies indicate that an \u03c9-agatoxin-TK\u2013sensitive, Cav2.1-like calcium permeability pathway is present in the RBC membrane and that it may function under the control of kinases and phosphatases.<\/jats:p>","DOI":"10.1182\/blood.v100.9.3392","type":"journal-article","created":{"date-parts":[[2002,10,16]],"date-time":"2002-10-16T23:03:08Z","timestamp":1034809388000},"page":"3392-3399","update-policy":"https:\/\/doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":96,"title":["Phorbol ester stimulates a protein kinase C\u2013mediated agatoxin-TK\u2013sensitive calcium permeability pathway in human red blood cells"],"prefix":"10.1182","volume":"100","author":[{"given":"Dina A.","family":"Andrews","sequence":"first","affiliation":[{"name":"From the Departments of Veterinary Pathobiology and Chemistry, Purdue University, West Lafayette, 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