Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Wayne B. Anderson"'
Publikováno v:
Biochemical and Biophysical Research Communications. 261:779-783
Glutathione transferase zeta (GSTZ) catalyzes the biotransformation of α-haloalkanoic acids. Treatment of rats or humans with dichloroacetic acid prolongs its elimination half-life, and preliminary studies in this laboratory show that fluorine-lacki
Publikováno v:
Archives of Biochemistry and Biophysics. 363:121-128
In fibroblasts, the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) stimulates phospholipase D (PLD)-mediated hydrolysis of both phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn) by PKC-alpha-mediated nonphosph
Publikováno v:
Archives of Biochemistry and Biophysics. 363:246-258
Since tumor promoter benzoyl peroxide (BPO) mimics phorbol esters in some aspects, its effects on protein kinase C (PKC) were previously studied. However, in those studies due to the presence of thiol agents in the PKC preparations, the sensitive rea
Publikováno v:
Biochemical and Biophysical Research Communications. 223:98-103
Subcellular redistribution (translocation) was initiated by treatment of NIH 3T3 cells overexpressing different epitope-tagged fragments of PKC epsilon with PMA, and was analyzed by immunocytochemistry. The PMA-induced translocation of holo PKC epsil
Publikováno v:
Biochemical and Biophysical Research Communications. 220:125-130
Monomethylethanolamine (1 mM) and dimethylethanolamine (1 mM) stimulated DNA synthesis 10- and 15-fold, respectively, in NIH 3T3 fibroblasts. In addition, simultaneous treatments with insulin (500 nM) and methylated ethanolamine analogues (1 mM or le
Publikováno v:
Analytical Biochemistry. 206:24-35
In the conventional approach protein kinase activity and phorbol ester binding associated with protein kinase C (PKC) are measured by initially incubating samples in either test tubes or multiwell plates, followed by filtration of the terminated reac
Publikováno v:
Archives of Biochemistry and Biophysics. 285:382-387
The oxidant mitogen/tumor promoter, periodate, was used to selectively modify either the regulatory domain or the catalytic domain of protein kinase C (PKC) to induce oxidative activation or inactivation of PKC, respectively. Periodate, at micromolar
Publikováno v:
Biochemical and biophysical research communications. 311(4)
We have previously demonstrated that a 33kDa C-terminal fragment of c-Raf-1 underwent a mobility shift in response to hydrogen peroxide (H(2)O(2)) and phorbol myristate acetate (PMA), respectively. In this study, we have demonstrated that H(2)O(2) in
Publikováno v:
Archives of biochemistry and biophysics. 397(2)
Phorbol 12-myristate-13-acetate (PMA), a potent tumor promoter and activator of most protein kinase C (PKC) isotypes, was found to significantly inhibit the growth of low population density (1-5% confluency) NIH 3T3 cells. Higher cell population dens
Publikováno v:
Biochemical and biophysical research communications. 214(2)
Experiments were carried out to determine Raf-1 protein kinase domain fragments which exhibit a characteristic electrophoretic mobility shift noted with Raf-1 protein kinase in response to serum and phorbol ester (PMA) treatment of serum-deprived NIH