SmPKC1, a new protein kinase C identified in the platyhelminth parasite Schistosoma mansoni

2006 ◽  
Vol 345 (3) ◽  
pp. 1138-1148 ◽  
Author(s):  
Diana Bahia ◽  
Lívia Avelar ◽  
Renato A. Mortara ◽  
Naji Khayath ◽  
Yutao Yan ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Schistosoma Mansoni ◽  
Kinase C ◽  
Platyhelminth Parasite ◽  
New Protein

Schistosoma mansoni: Possible involvement of protein kinase C in linoleic acid-induced proteolytic enzyme release from cercariae

1991 ◽  
Vol 72 (3) ◽  
pp. 311-320 ◽  
Author(s):  
Kenichiro Matsumura ◽  
Yoshinori Mitsui ◽  
Katsuyuki Sato ◽  
Makoto Sakamoto ◽  
Yoshiki Aoki
Keyword(s):  
Protein Kinase C ◽  
Linoleic Acid ◽  
Protein Kinase ◽  
Schistosoma Mansoni ◽  
Proteolytic Enzyme ◽  
Enzyme Release ◽  
Kinase C

Endoxifen: A New, Protein Kinase C inhibitor to treat acute and mixed mania associated with bipolar I disorder

2020 ◽  
Author(s):  
Ateeq Ahmad ◽  
Saifuddin Sheikh ◽  
Mujtaba Ali Khan ◽  
Alok Chaturvedi ◽  
Piyush Patel ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Bipolar I Disorder ◽  
Kinase C ◽  
Protein Kinase C Inhibitor ◽  
New Protein

Developmental Expression of Protein Kinase C Activity in Schistosoma Mansoni

1992 ◽  
Vol 46 (3) ◽  
pp. 358-365 ◽  
Author(s):  
Peter M. Wiest ◽  
G. Richard Olds ◽  
Wayne D. Bowen ◽  
Daniel C. Burnham
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Schistosoma Mansoni ◽  
Developmental Expression ◽  
Kinase C ◽  
Protein Kinase C Activity

Induction of 24-hydroxylase cytochrome P450 mRNA by 1,25-dihydroxyvitamin D and phorbol esters in normal rat kidney (NRK-52E) cells

1997 ◽  
Vol 153 (2) ◽  
pp. 199-205 ◽  
Author(s):  
H J Armbrecht ◽  
M L Chen ◽  
T L Hodam ◽  
M A Boltz
Keyword(s):  
Protein Synthesis ◽  
Cytochrome P450 ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Target Cells ◽  
Mrna Levels ◽  
Dihydroxyvitamin D ◽  
1,25 Dihydroxyvitamin D ◽  
Kinase C ◽  
New Protein

Abstract The biologically active form of vitamin D, 1,25-dihydroxyvitamin D (1,25(OH)2D), acts on intestinal, renal, and bone cells to regulate skeletal and mineral metabolism. 1,25(OH)2D also induces 24-hydroxylase activity in these target cells. The 24-hydroxylase hydroxylates 1,25(OH)2D to 1,24,25-trihydroxyvitamin D and 25(OH)D to 24,25-dihydroxyvitamin D. The production of 1,24,25-trihydroxyvitamin D is thought to be the first step in the inactivation of 1,25(OH)2D by its target tissues. Previous studies have characterized the induction of the 24-hydroxylase by 1,25(OH)2D in clonal cell lines from intestine and bone. The purpose of these studies was to characterize the induction of the 24-hydroxylase by 1,25(OH)2D in the kidney, using the clonal rat renal cell line NRK-52E. 1,25(OH)2D (10−7 m) increased the mRNA levels for the cytochrome P450 component of the 24-hydroxylase (P450cc24) by sevenfold after 36 h in NRK-52E cells. 1,25(OH)2D increased P450cc24 mRNA levels in a dose-dependent manner with an EC50 of 10−8 m. In parallel experiments, 1,25(OH)2D significantly increased 24-hydroxylase enzyme activity after 48–72 h. The increase in P450cc24 mRNA induced by 1,25(OH)2D required on-going transcription and translation and was inhibited by H-7, a protein kinase C inhibitor. Tetradecanoyl phorbol acetate markedly increased the magnitude of the tissue responsiveness to 1,25(OH)2D by a protein kinase C-dependent pathway. These studies demonstrate that 1,25(OH)2D increases P450cc24 mRNA levels in NRK-52E cells by a mechanism requiring new protein synthesis and involving protein kinase C. This is in contrast to the action of 1,25(OH)2D in intestinal cells, which does not require new protein synthesis, and in osteoblastic cells, which does not involve protein kinase C. Journal of Endocrinology (1997) 153, 199–205

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