Phosphoinositide-specific phospholipase C (PLC) plays a major role in transmembrane signaling by catalyzing the hydrolysis
of phosphatidylinositol 4,5-bisphosphate (PIP2) and thereby generating the second messenger molecules inositol
1,4,5-trisphosphate (IP3) and diacylglycerol. Several distinct PLC enzymes have been identified in a variety of mammalian
tissues.
General function
Enzyme, Hydrolase
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Cellular localization
Cytoplasmic, Nuclear
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Ovarian function
Oogenesis
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Avazeri N, et al 2000 reported the cytoplasmic and nuclear phospholipase C-beta 1 relocation and its role
in resumption of meiosis in the mouse oocyte.
They used
specific monoclonal antibodies to monitor the in vitro dynamics of the
subcellular distribution of the enzyme from the release of the oocyte from the
follicle until breakdown of the germinal vesicle (GVBD) by Western blotting,
electron microscope immunohistochemistry, and confocal microscope
immunofluorescence. PLC-beta1 became relocated to the oocyte cortex and the
nucleoplasm during the G2/M transition, mainly in the hour preceding GVBD. The
enzyme was a 150-kDa protein, corresponding to PLC-beta 1a. Its synthesis in
the cytoplasm increased during this period, and it accumulated in the
nucleoplasm. GVBD was dramatically inhibited by the microinjection of
anti-PLC-beta1 monoclonal antibody into the germinal vesicle (GV) only when
this accumulation was at its maximum.
Expression regulated by
Comment
Ovarian localization
Oocyte, Luteal cells
Comment
Boiti et al 2000 reported that nitric oxide synthase activity and progesterone release by isolated corpora lutea of
rabbits in the early and mid-luteal phases of pseudopregnancy are modulated differently
by prostaglandin E-2 and prostaglandin F-2alpha via adenylate cyclase and
phospholipase C.