Advertisement
JBC

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 Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 Peters, C. A.
Right arrow Articles by Hunzicker-Dunn, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Peters, C. A.
Right arrow Articles by Hunzicker-Dunn, M.
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?

J Biol Chem, Vol. 274, Issue 52, 37499-37505, December 24, 1999

Activation of PKC delta  in the Rat Corpus Luteum during Pregnancy
POTENTIAL ROLE OF PROLACTIN SIGNALING*

Carl A. Peters, Evelyn T. Maizels, and Mary Hunzicker-DunnDagger

From the Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611

Maintenance of pregnancy in the rat requires the corpus luteum. At a time when rat placental lactogens (rPLs) are required to support progesterone production by the corpus luteum and when relaxin expression is initiated, expression of a specific protein kinase C (PKC) isoform, PKC delta , is dramatically increased. We therefore assessed whether prolactin (PRL) receptor activation promotes activation of PKC delta  in a luteinized granulosa cell model. We also assessed the activation status of PKC delta  in corpora lutea obtained when the corpus luteum is exposed to chronically high concentrations of rPLs. The activity of PKC delta  was assessed by two means: an immune complex (IC) assay and Western blotting with a phospho-epitope-specific antibody that detects PKC delta  phosphorylated on serine 662. PKC delta  activation in the IC kinase assay was determined by the ability of immunoprecipitated PKC delta  to phosphorylate the PKC delta -preferential substrate small heat shock protein (HSP-27). Treatment of luteinized rat granulosa cells with phorbol myristate acetate, a known activator of PKC, promoted a 7-fold increase in HSP-27 phosphorylation by PKC delta . Similarly, immunoreactivity with the phospho-epitope-specific PKC delta  antibody was increased in extracts prepared from luteinized granulosa cells treated with phorbol myristate acetate or following in vitro activation of recombinant PKC delta . Using these assays, we assessed whether PRL receptor agonists were capable of activating PKC delta  in luteinized granulosa cells. PRL receptor agonists induced translocation PKC delta  from the cytosolic to the Triton-soluble membrane fraction and increased PKC delta  activity assessed by both IC kinase assay and Western blotting with phospho-epitope-specific PKC delta  antibody. Analysis of PKC delta  activity in corpora lutea obtained during pregnancy by both the IC kinase assay and Western blotting with the phospho-epitope-specific PKC delta  antibody revealed that PKC delta  activity was increased throughout the second half of pregnancy. These results demonstrate that PRL receptor activation promotes the acute activation of PKC delta  in luteinized rat granulosa cells. At a time when the rat is exposed to chronically high concentrations of rPLs, PKC delta  is increasingly expressed and active.

* This work was supported by National Institutes of Health Grant P01 HD 21921 (to M. H.-D.) and the Training Program in Reproductive Biology (T32 HD 07068).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Cell and Molecular Biology, Northwestern University Medical School, 303 E. Chicago Ave., Chicago, IL 60611. Tel: 312-503-8940; Fax: 312-503-0566; E-mail: mhd@nwu.edu.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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
 Endocr Relat CancerHome page
F. Doll, J. Pfeilschifter, and A. Huwiler
Prolactin upregulates sphingosine kinase-1 expression and activity in the human breast cancer cell line MCF7 and triggers enhanced proliferation and migration
Endocr. Relat. Cancer, June 1, 2007; 14(2): 325 - 335.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
L. T. Budnik and A. K. Mukhopadhyay
Lysophosphatidic Acid-Induced Nuclear Localization of Protein Kinase C {delta} in Bovine Theca Cells Stimulated with Luteinizing Hormone
Biol Reprod, September 1, 2002; 67(3): 935 - 944.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
L. M. Salvador, E. Maizels, D. B. Hales, E. Miyamoto, H. Yamamoto, and M. Hunzicker-Dunn
Acute Signaling by the LH Receptor Is Independent of Protein Kinase C Activation
Endocrinology, August 1, 2002; 143(8): 2986 - 2994.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
J. Frasor, U. Barkai, L. Zhong, A. T. Fazleabas, and G. Gibori
PRL-Induced ER{alpha} Gene Expression Is Mediated by Janus Kinase 2 (Jak2) While Signal Transducer and Activator of Transcription 5b (Stat5b) Phosphorylation Involves Jak2 and a Second Tyrosine Kinase
Mol. Endocrinol., November 1, 2001; 15(11): 1941 - 1952.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
J. J. Peluso, A. Pappalardo, and G. Fernandez
Basic Fibroblast Growth Factor Maintains Calcium Homeostasis and Granulosa Cell Viability by Stimulating Calcium Efflux via a PKC{delta}-Dependent Pathway
Endocrinology, October 1, 2001; 142(10): 4203 - 4211.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
L. T. Budnik and A. K. Mukhopadhyay
Lysophosphatidic Acid Antagonizes the Morphoregulatory Effects of the Luteinizing Hormone on Luteal Cells: Possible Role of Small Rho-G-Proteins
Biol Reprod, July 1, 2001; 65(1): 180 - 187.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
E. T. Maizels, A. Mukherjee, G. Sithanandam, C. A. Peters, J. Cottom, K. E. Mayo, and M. Hunzicker-Dunn
Developmental Regulation of Mitogen-Activated Protein Kinase-Activated Kinases-2 and -3 (MAPKAPK-2/-3) in Vivo during Corpus Luteum Formation in the Rat
Mol. Endocrinol., May 1, 2001; 15(5): 716 - 733.
[Abstract] [Full Text]

Home page
 Mol. Endocrinol.Home page
C. A. Peters, E. T. Maizels, M. C. Robertson, R. P.C. Shiu, M. S. Soloff, and M. Hunzicker-Dunn
Induction of Relaxin Messenger RNA Expression in Response to Prolactin Receptor Activation Requires Protein Kinase C {delta} Signaling
Mol. Endocrinol., April 1, 2000; 14(4): 576 - 590.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
F. Gaubert, F. Escaffit, C. Bertrand, M. Korc, L. Pradayrol, F. Clemente, and A. Estival
Expression of the High Molecular Weight Fibroblast Growth Factor-2 Isoform of 210 Amino Acids Is Associated with Modulation of Protein Kinases C delta and epsilon and ERK Activation
J. Biol. Chem., January 5, 2001; 276(2): 1545 - 1554.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement