Hyperoxia, unlike phorbol ester, induces glutathione peroxidase through a protein kinase C-independent mechanism
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منابع مشابه
Characterization of calcium-independent forms of protein kinase C-beta in phorbol ester-treated rabbit platelets.
The subcellular distribution, size, and activation state of protein kinase C (PKC) were studied after short term exposure of rabbit platelets to a saturating dose of 12-O-tetradecanoylphorbol 13-acetate (TPA). Cytosolic and Nonidet P-40-solubilized particulate extracts prepared from TPA-treated platelets were subjected to analytical column chromatography on Mono Q, hydroxylapatite, and Superose...
متن کاملc-fos promoter insensitivity to phorbol ester and possible role of protein kinase C in androgen-independent cancer cells.
In exploring the biological basis of androgen-independent prostate cancer, we observed serum-independent growth of androgen-independent cells. We then discovered that in androgen-independent but not androgen-dependent cells, the serum-responsive gene c-fos is insensitive to phorbol esters, which regulate c-fos through the same mechanisms as serum. Transient expression of protein kinase C, throu...
متن کاملProtein kinase C heterogeneity in GH4C1 rat pituitary cells. Characterization of a Ca2(+)-independent phorbol ester receptor.
Clonal GH4C1 rat pituitary cells are heterogeneous with respect to phorbol dibutyrate receptors (PDBu-R) and protein kinase C (PKC) content. GH cell PDBu-Rs can be separated into two categories based on Ca2(+)-modulation of receptor affinity. Approximately 70% of the cytosolic PDBu-Rs demonstrate Ca2(+)-sensitive receptor affinity and redistribute from the soluble to the particulate fraction in...
متن کاملThe effects of phorbol ester on mouse blastomeres: a role for protein kinase C in compaction?
The effects of phorbol myristate acetate (PMA) and other activators of protein kinase C on the cytoskeletal organization of mouse oocytes and early embryos have been examined. The effects observed depended on the developmental stage on exposure to PMA. PMA had little effect on the cytoskeletal or microvillous organization of unfertilized oocytes. Interphase cells from embryos prior to compactio...
متن کاملPhorbol Esters and Related Analogs Regulate the Subcellular Localization of b2-Chimaerin, a Non-protein Kinase C Phorbol Ester Receptor*
The novel phorbol ester receptor b2-chimaerin is a Rac-GAP protein possessing a single copy of the C1 domain, a 50-amino acid motif initially identified in protein kinase C (PKC) isozymes that is involved in phorbol ester and diacylglycerol binding. We have previously shown that, like PKCs, b2-chimaerin binds phorbol esters with high affinity in a phospholipid-dependent manner (Caloca, M. J., F...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1997
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3260117