Abstract
The calcium- and lipid-dependent protein kinase (protein kinase C) is an intracellular messenger for the phospholipase C/polyphosphoinositide pathway. This pathway has been shown to be an important transduction system in hormone action (1) and plays a role in many other cell activities (2–4). It has been proposed that the hormonal control of ovarian function utilizes the phospholipase C/protein kinase C transduction pathway (5). We recently reported that an endogenous inhibitor of protein kinase C was present in the rat ovary on day 7 of pseudopregnancy (6). The presence of an endogenous inhibitor of protein kinase C presents a potential mechanism for regulation of the enzyme in addition to the well-characterized diacylglycerol, phospholipid, and calcium activators. These studies were undertaken to determine whether the activity of the endogenous inhibitor of protein kinase C varied throughout pseudopregnancy in the rat ovary.
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