HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hansen Ree, A. Articles by Taskén, K. A. Search for Related Content PubMed PubMed Citation Articles by Hansen Ree, A. Articles by Taskén, K. A. Agricola Articles by Hansen Ree, A. Articles by Taskén, K. A.

Calcium/Phospholipid-Dependent Protein Kinases in Rat Sertoli Cells: Regulation of Androgen Receptor Messenger Ribonucleic Acid¹

^a Institute of Medical Biochemistry, ^b Department of Tumor Biology, ^c Norwegian Radium Hospital, and Neurochemical Laboratory, University of Oslo, 0317 Oslo, Norway

The possibility that Sertoli cell responses to testosterone are modulated by the calcium/phospholipid-dependent protein kinase (protein kinase C; PKC) was examined in rat Sertoli cells in culture. Both soluble and particulate cell fractions showed low constitutive phosphotransferase activity. Incubation with the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA; 10^-7 M) was associated with a transient induction in both cell fractions of calcium/phosphatidylserine-dependent PKC activity, which was elevated from 15 min to 1 h. Consistent with this, mRNAs for the calcium/phospholipid-dependent isomeric forms of PKC (, ß, and ) were detected. The expression levels of mRNAs for PKC and PKCß were also up-regulated (2.5- to 3-fold) by TPA (10^-7 M), but these effects were much slower (peaking after 12 h) than those on phosphotransferase activity. In the presence of TPA (10^-7 M), expression of androgen receptor (AR) mRNA showed a transient time-dependent down-regulation (~70%), in which the nadir was reached after 6 h and baseline expression was again obtained after 12 h. The regulatory effect of PKC activation on AR mRNA was confirmed by the absence of response to a biologically inactive phorbol ester. A concentration-dependent decrease (half-maximal effect at ~10^-8 M TPA) of AR mRNA was also observed. These data suggest that Sertoli cell responses to testosterone may be inhibited by a transiently active PKC with a wide intracellular distribution.

¹ This work was supported by the Norwegian Research Council and the Norwegian Cancer Society. A.H.R. is research fellow of the Norwegian Cancer Society, and K.A.T. is research fellow of the Norwegian Research Council.

² Correspondence: Anne Hansen Ree, Department of Tumor Biology, Norwegian Radium Hospital, Montebello, 0310 Oslo, Norway. FAX: 47 2252 2421; ahree{at}radium.uio.no

³ Current address: Winnie Eskild, Department of Biochemistry, University of Oslo, Oslo, Norway.

This article has been cited by other articles:

				T. Saether, T. N. Tran, H. Rootwelt, B. O. Christophersen, and T. B. Haugen Expression and Regulation of {Delta}5-Desaturase, {Delta}6-Desaturase, Stearoyl-Coenzyme A (CoA) Desaturase 1, and Stearoyl-CoA Desaturase 2 in Rat Testis Biol Reprod, July 1, 2003; 69(1): 117 - 124. [Abstract] [Full Text] [PDF]

				K. W. Braun, M.-N. Vo, and K. H. Kim Positive Regulation of Retinoic Acid Receptor Alpha by Protein Kinase C and Mitogen-Activated Protein Kinase in Sertoli Cells Biol Reprod, July 1, 2002; 67(1): 29 - 37. [Abstract] [Full Text] [PDF]

				J. k. Chen and L. L. Heckert Dmrt1 Expression Is Regulated by Follicle-Stimulating Hormone and Phorbol Esters in Postnatal Sertoli Cells Endocrinology, March 1, 2001; 142(3): 1167 - 1178. [Abstract] [Full Text] [PDF]