Am J Physiol Cell Physiol Watch the video to learn how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 281: C514-C523, 2001;
0363-6143/01 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (8)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Korchak, H. M.
Right arrow Articles by Kilpatrick, L. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Korchak, H. M.
Right arrow Articles by Kilpatrick, L. E.
Vol. 281, Issue 2, C514-C523, August 2001

Negative regulation of ligand-initiated Ca2+ uptake by PKC-beta II in differentiated HL60 cells

Helen M. Korchak1, Barbara E. Corkey2, Gordon C. Yaney2, and Laurie E. Kilpatrick1

1 Departments of Pediatrics and Biochemistry/Biophysics, University of Pennsylvania School of Medicine, The Joseph Stokes Jr. Research Institute of the Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104; and 2 Obesity Research Unit, Department of Medicine, Boston University School of Medicine, Boston, Massachusetts 02118

In phagocytic cells, fMet-Leu-Phe triggers phosphoinositide remodeling, activation of protein kinase C (PKC), release of intracellular Ca2+ and uptake of extracellular Ca2+. Uptake of extracellular Ca2+ can be triggered by store-operated Ca2+ channels (SOCC) and via a receptor-operated nonselective cation channel(s). In neutrophilic HL60 cells, the PKC activator phorbol myristate acetate (PMA) activates multiple PKC isotypes, PKC-alpha , PKC-beta , and PKC-delta , and inhibits ligand-initiated mobilization of intracellular Ca2+ and uptake of extracellular Ca2+. Therefore PKC is a negative regulator at several points in Ca2+ mobilization. In contrast, selective depletion of PKC-beta in HL60 cells by an antisense strategy enhanced fMet-Leu-Phe-initiated Ca2+ uptake but not mobilization of intracellular Ca2+. Thapsigargin-induced Ca2+ uptake through SOCC was not affected by PKC-beta II depletion. Thus PKC-beta II is a selective negative regulator of Ca2+ uptake but not release of intracellular Ca2+ stores. PKC-beta II inhibits a receptor-operated cation or Ca2+ channel, thus inhibiting ligand-initiated Ca2+ uptake.

calcium mobilization; protein kinase C isotypes; inositol 1,4,5-trisphosphate; signal transduction


This article has been cited by other articles:


Home page
 BloodHome page
C. M. Hammond, D. White, J. Tomic, Y. Shi, and D. E. Spaner
Extracellular calcium sensing promotes human B-cell activation and function
Blood, December 1, 2007; 110(12): 3985 - 3995.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. K. Berdiev, J. Xia, B. Jovov, J. M. Markert, T. B. Mapstone, G. Y. Gillespie, C. M. Fuller, J. K. Bubien, and D. J. Benos
Protein Kinase C Isoform Antagonism Controls BNaC2 (ASIC1) Function
J. Biol. Chem., November 22, 2002; 277(48): 45734 - 45740.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online