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Parathyroid hormone uses both adenylate cyclase and protein kinase C to regulate acid production in osteoclasts
Author(s) -
May Lisa G.,
Gay Carol V.
Publication year - 1997
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19970615)65:4<565::aid-jcb11>3.0.co;2-b
Subject(s) - parathyroid hormone , protein kinase c , medicine , adenylate kinase , endocrinology , chemistry , cyclase , adenosine , stimulation , protein kinase a , biochemistry , biology , calcium , phosphorylation , enzyme
Osteoclasts, isolated from the endosteum of 2.5‐ to 3‐week‐old chickens, were treated with acridine orange, a hydrogen ion concentration‐sensitive fluorescent dye, in order to monitor changes in acid production. The adenylate cyclase inhibitor, alloxan, blocked parathyroid hormone (PTH)‐stimulated acid production. Dibutyryl cyclic adenosine monophosphate, a membrane‐permeant form of cyclic adenosine monophosphate, mimicked the PTH effect. Bisindolylmaleimide, a specific inhibitor of protein kinase C (PKC), blocked the initial stimulation (15, 30, and 60 min) of acid production by PTH but had no effect on long‐term stimulation (120 min). Confocal microscopy of osteoclasts stained with fluorescein‐conjugated bisindolylmaleimide revealed a shift in location of PKC from the cytoplasm to the plasma membrane region after treatment with parathyroid hormone. The results of these studies support the hypothesis that PTH regulation of acid production in osteoclasts involves both adenylate cyclase and PKC as effectors. J. Cell. Biochem. 65:565–573. © 1997 Wiley‐Liss Inc.