Phorbol ester receptors in mammalian brain: characterization, localization and target size
نویسندگان
چکیده
منابع مشابه
Heterogeneous localization of protein kinase C in rat brain: autoradiographic analysis of phorbol ester receptor binding.
Protein kinase C is a calcium- and phospholipid-stimulated enzyme present in high concentration in the brain. Phorbol esters are potent tumor promoters that bind to specific receptors with high affinity. Several lines of evidence indicate that the phorbol ester receptor is identical to protein kinase C. To determine the distribution of protein kinase C, we have localized phorbol ester receptors...
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A specific surface receptor for urokinase plasminogen activator (uPA) recognizes the amino-terminal growth factor-like sequence of uPA, a region independent from and not required for the catalytic activity of this enzyme. The properties of the uPA receptor (uPAR) and the localization and distribution of uPA in tumor cells and tissues suggest that the uPA/uPAR interaction may be important in reg...
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In recent years, there have been great advances in our understanding of the pharmacology and biology of the receptors for the phorbol ester tumor promoters and the second messenger diacylglycerol (DAG). The traditional view of protein kinase C (PKC) as the sole receptor for the phorbol esters has been challenged with the discovery of proteins unrelated to PKC that bind phorbol esters with high ...
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Endocytosis is an essential process for cell function. There are at least two types of endocytosis: receptor-mediated endocytosis and fluid-phase endocytosis. Endosomal vesicles derived from both types of endocytosis fuse with a common endosomal sorting compartment and appear to share common components. Interestingly, factors that affect endosome fusion regulate the kinetics and extent of endoc...
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Phorbol esters inhibited the uptake of a fluorescent glucose analogue in goose but not in human erythrocytes. Specific phorbol-12,13-dibutyrate (PDB) binding sites were identified in both goose and human erythrocytes. In the absence of Ca2+ and phospholipid, PDB binding in whole cell lysates was similar to that in intact cells, but addition of Ca2+ (0.5 mM) and phosphatidyl serine (96 microgram...
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1987
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)58220-8