Advertisement
J. Lipid Res.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Facchinetti, M. M.
Right arrow Articles by de Boland, A. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Facchinetti, M. M.
Right arrow Articles by de Boland, A. R.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

The Journal of Lipid Research, Vol. 39, 197-204, January 1998
Copyright © 1998 by Lipid Research, Inc.


Original Article

Calcitriol transmembrane signalling: regulation of rat muscle phospholipase D activity

Maria Marta Facchinettia, Ricardo Bolanda, and Ana R. de Bolanda
a Departamento de Biologia, Bioquimica y Farmacia, Universidad Nacional del Sur, 8000 Bahia Blanca, Argentina

Correspondence to: Ana R. de Boland.

In rat skeletal muscle, calcitriol, the hormonal form of vitamin D3, rapidly stimulates the biphasic formation of diacylglycerol (DAG), the second phase being independent of phosphoinositide hydrolysis driven by phospholipase C. In this work we showed that the effect of calcitriol on the second phase of DAG formation was totally inhibited in the absence of extracellular Ca2+ and by the Ca2+-channel blockers nifedipine and verapamil, whereas the Ca2+ ionophore A23184, similar to calcitriol, increased DAG formation by 100%. GTP{gamma}S, which activates G protein-mediated signals, mimicked the effects of the hormone while GDP ßS, an inhibitor of G proteins, suppressed calcitriol-induced DAG formation. To elucidate the metabolic pathway of the late phase of DAG production, we examined the contribution of phospholipase D (PLD), which acts on phosphatidylcholine (PC) generating phosphatidic acid that is converted to DAG by a phosphatidate phosphohydrolase. In [3H]arachidonate-labeled muscle, calcitriol increased [3H]phosphatidylethanol (PEt) formation in the presence of ethanol, a reaction specific for PLD. The effects of the hormone were time- and dose-dependent with maximum PEt levels achieved at 10-9 M. The phorbol ester TPA also stimulated PEt formation. The combination of calcitriol and TPA was more effective than either compound alone. In rat muscle, calcitriol increased PKC activity in a time-dependent fashion. Bisindolymaleimide, a selective inhibitor of the enzyme, completely suppressed TPA-induced PEt and attenuated the effects of the hormone.

These results provide the first evidence concerning calcitriol stimulation of the hydrolysis of PC in a mammalian tissue through a phospholipase D catalyzed mechanism involving Ca2+, protein kinase C, and G proteins.—Facchinetti, M. M., R. Boland, and A. R. de Boland. Calcitriol transmembrane signalling: regulation of rat muscle phospholipase D activity. J. Lipid Res. 1998. 39: 197–204.

Supplementary key words: rat skeletal muscle, calcitriol, diacylglycerol, phospholipase D, phosphatidylethanol, protein kinase C, G proteins


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
T. A. Hornberger, W. K. Chu, Y. W. Mak, J. W. Hsiung, S. A. Huang, and S. Chien
The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle
PNAS, March 21, 2006; 103(12): 4741 - 4746.
[Abstract] [Full Text] [PDF]


Home page
Physiol. Rev.Home page
R. M. LOSEL, E. FALKENSTEIN, M. FEURING, A. SCHULTZ, H.-C. TILLMANN, K. ROSSOL-HASEROTH, and M. WEHLING
Nongenomic Steroid Action: Controversies, Questions, and Answers
Physiol Rev, July 1, 2003; 83(3): 965 - 1016.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Z. Schwartz, V. L. Sylvia, D. Larsson, I. Nemere, D. Casasola, D. D. Dean, and B. D. Boyan
1alpha ,25(OH)2D3 Regulates Chondrocyte Matrix Vesicle Protein Kinase C (PKC) Directly via G-protein-dependent Mechanisms and Indirectly via Incorporation of PKC during Matrix Vesicle Biogenesis
J. Biol. Chem., March 29, 2002; 277(14): 11828 - 11837.
[Abstract] [Full Text] [PDF]


Home page
Pharmacol. Rev.Home page
E. Falkenstein, H.-C. Tillmann, M. Christ, M. Feuring, and M. Wehling
Multiple Actions of Steroid Hormones---A Focus on Rapid, Nongenomic Effects
Pharmacol. Rev., December 1, 2000; 52(4): 513 - 556.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
A. Gomez-Munoz, J. S. Martens, and U. P. Steinbrecher
Stimulation of Phospholipase D Activity by Oxidized LDL in Mouse Peritoneal Macrophages
Arterioscler. Thromb. Vasc. Biol., January 1, 2000; 20(1): 135 - 143.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Gastrointest. Liver Physiol.Home page
S. Khare, M. Bissonnette, B. Scaglione-Sewell, R. K. Wali, M. D. Sitrin, and T. A. Brasitus
1,25-Dihydroxyvitamin D3 and TPA activate phospholipase D in Caco-2 cells: role of PKC-alpha
Am J Physiol Gastrointest Liver Physiol, April 1, 1999; 276(4): G993 - G1004.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement