Prolactin signalling in porcine theca cells: the involvement of protein kinases and phosphatases
R. Ciereszko A C , M. Opałka A , B. Kamińska A , T. Górska B and L. Dusza A
+ Author Affiliations
- Author Affiliations
A Department of Animal Physiology, University of Warmia and Mazury in Olsztyn, Poland.
B Department of Animal Physiology and Biochemistry, August Cieskowski University of Agriculture, Poznań, Poland.
C To whom correspondence should be addressed. email: reniac@uwm.edu.pl
Reproduction, Fertility and Development 15(1) 27-35 https://doi.org/10.1071/RD02049
Submitted: 4 January 2002 Accepted: 16 December 2002 Published: 16 December 2002
Abstract
The hypothesis that protein kinase C (PKC) and tyrosine kinases, as well as serine–threonine and tyrosine phosphatases, are involved in prolactin (PRL) signalling in theca cells harvested from porcine follicles was tested. Theca cells were incubated with PRL for 24 h to stimulate progesterone (P4) production. In addition, treatments included inhibitors of PKC and tyrosine kinases, as well as serine–threonine phosphatase inhibitor and tyrosine phosphatase inhibitor. Prolactin significantly stimulated P4 production by theca cells and all inhibitors suppressed the PRL-stimulated P4 production. After incubation with PRL for 2, 5, 10 or 20 min, theca cells were homogenized and cytosolic and membrane fractions were obtained. This was followed by determination of PKC activity in partially purified subcellular fractions by measuring the transfer of 32P from [γ−32P] adenosine triphosphatase (ATP) to histone III-S. In unstimulated porcine theca cells the major proportion of PKC activity was present in the cytosol. Incubation of cells with PRL resulted in a rapid, time-dependent increase in the amount of PKC activity in the membrane fraction. Protein kinase C activity in the membrane fraction was maximal after 10 min of cells’ exposure to PRL. Protein kinase C activation was assessed also by measuring the specific association of 3H-phorbol dibutyrate (3H-PDBu) with theca cells after treatment with PRL. Prolactin significantly increased 3H-PDBu-specific binding in theca cells. In contrast to PKC, total inositol phosphate accumulation was not affected by PRL in the current study. In summary, PRL stimulated P4 production by porcine theca cells derived from large follicles. The results of the study were consistent with the hypothesis that PKC is one of the intracellular mediators of PRL action in porcine theca cells. Protein kinase C activation does not appear to occur through the action of phosphatidylinositol-dependent phospholipase C. Moreover, the involvement of tyrosine kinases, as well as tyrosine and serine–threonine phosphatases, in PRL signalling in the examined cells is suggested.
Extra keywords: phospholipase C
Acknowledgments
We thank Beata Szwarc for her excellent technical assistance. This work was supported by grants 5P06D 048 14 and 0206 0205 from the State Committee for Scientific Research (KBN) in Poland.
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