Lysophosphatidic acid-induced nuclear localization of protein kinase C delta in bovine theca cells stimulated with luteinizing hormone.
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Lysophosphatidic acid-induced nuclear localization of protein kinase C delta in bovine theca cells stimulated with luteinizing hormone. / Budnik, Lygia Therese; Mukhopadhyay, Amal K.
In: BIOL REPROD, Vol. 67, No. 3, 3, 2002, p. 935-944.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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T1 - Lysophosphatidic acid-induced nuclear localization of protein kinase C delta in bovine theca cells stimulated with luteinizing hormone.
AU - Budnik, Lygia Therese
AU - Mukhopadhyay, Amal K
PY - 2002
Y1 - 2002
N2 - The amounts of lysophospholipase D (LPLD) and the ovarian protein kinase C delta (PKCdelta) increase during the course of pregnancy. Because LPLD is involved in the production of the bioactive phospholipid lysophosphatidic acid (LPA), we examined whether stimulation with LPA would influence PKCdelta in the ovary. We used immunoblotting and immunohistochemical methods to show that stimulation of bovine theca cells with LPA leads to an unexpected redistribution of PKCdelta from the cytosol to the perinuclear area and that in the presence of LH, LPA induces a complete nuclear translocation of PKCdelta. These effects of LPA are dose dependent, can be mimicked by phorbol ester, and are inhibited by a PKCdelta inhibitor, rottlerin. Concomitantly, under the same experimental conditions both LPA and the phorbol ester PMA (4beta-phorbol-12-myristate-13-acetate) augment LH-stimulated progesterone accumulation in this cell system. This functional effect of LPA and PMA is abolished in cells pretreated with rottlerin. It is unclear whether the nuclear localization of PKCdelta indicates a specific function of the enzyme in the bovine ovary. Because PKCdelta supports a luteotropic function in rodent models, a similar role in the bovine ovary is also likely.
AB - The amounts of lysophospholipase D (LPLD) and the ovarian protein kinase C delta (PKCdelta) increase during the course of pregnancy. Because LPLD is involved in the production of the bioactive phospholipid lysophosphatidic acid (LPA), we examined whether stimulation with LPA would influence PKCdelta in the ovary. We used immunoblotting and immunohistochemical methods to show that stimulation of bovine theca cells with LPA leads to an unexpected redistribution of PKCdelta from the cytosol to the perinuclear area and that in the presence of LH, LPA induces a complete nuclear translocation of PKCdelta. These effects of LPA are dose dependent, can be mimicked by phorbol ester, and are inhibited by a PKCdelta inhibitor, rottlerin. Concomitantly, under the same experimental conditions both LPA and the phorbol ester PMA (4beta-phorbol-12-myristate-13-acetate) augment LH-stimulated progesterone accumulation in this cell system. This functional effect of LPA and PMA is abolished in cells pretreated with rottlerin. It is unclear whether the nuclear localization of PKCdelta indicates a specific function of the enzyme in the bovine ovary. Because PKCdelta supports a luteotropic function in rodent models, a similar role in the bovine ovary is also likely.
M3 - SCORING: Zeitschriftenaufsatz
VL - 67
SP - 935
EP - 944
JO - BIOL REPROD
JF - BIOL REPROD
SN - 0006-3363
IS - 3
M1 - 3
ER -