scholarly journals Prostaglandin E2 modulates proximal tubule Na+-ATPase activity: Cooperative effect between protein kinase A and protein kinase C

2011 ◽  
Vol 507 (2) ◽  
pp. 281-286 ◽  
Author(s):  
J.D. Líbano-Soares ◽  
S.S. Landgraf ◽  
E. Gomes-Quintana ◽  
A.G. Lopes ◽  
C. Caruso-Neves
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Prostaglandin E2 ◽  
Proximal Tubule ◽  
Protein Kinase A ◽  
Cooperative Effect ◽  
Kinase C ◽  
Kinase A

Phosphorylation of NADPH oxidase activator 1 (NOXA1) on serine 282 by MAP kinases and on serine 172 by protein kinase C and protein kinase A prevents NOX1 hyperactivation

2010 ◽  
Vol 24 (6) ◽  
pp. 2077-2092 ◽  
Author(s):  
Yolande Kroviarski ◽  
Maya Debbabi ◽  
Rafik Bachoual ◽  
Axel Pe´rianin ◽  
Marie‐Anne Gougerot‐Pocidalo ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nadph Oxidase ◽  
Protein Kinase A ◽  
Map Kinases ◽  
Kinase C ◽  
Kinase A

scholarly journals Pituitary adenylate cyclase activating polypeptide as a novel hypophysiotropic factor in fish

2000 ◽  
Vol 78 (3) ◽  
pp. 329-343 ◽  
Author(s):  
Anderson OL Wong ◽  
Wen Sheng Li ◽  
Eric KY Lee ◽  
Mei Yee Leung ◽  
Lai Yin Tse ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Adenylate Cyclase ◽  
Protein Kinase A ◽  
Anterior Pituitary ◽  
Kinase C ◽  
Pituitary Adenylate Cyclase ◽  
Pacap Receptors ◽  
Kinase A

Pituitary adenylate cyclase activating polypeptide (PACAP) is a novel member of the secretin-glucagon peptide family. In mammals, this peptide has been located in a wide range of tissues and is involved in a variety of biological functions. In lower vertebrates, especially fish, increasing evidence suggests that PACAP may function as a hypophysiotropic factor regulating pituitary hormone secretion. PACAP has been identified in the brain-pituitary axis of representative fish species. The molecular structure of fish PACAP is highly homologous to mammalian PACAP. The prepro-PACAP in fish, however, is distinct from that of mammals as it also contains the sequence of fish GHRH. In teleosts, the anterior pituitary is under direct innervation of the hypothalamus and PACAP nerve fibers have been identified in the pars distalis. Using the goldfish as a fish model, mRNA transcripts of PACAP receptors, namely the PAC1 and VPAC1 receptors, have been identified in the pituitary as well as in various brain areas. Consistent with the pituitary expression of PACAP receptors, PACAP analogs are effective in stimulating growth hormone (GH) and gonadotropin (GTH)-II secretion in the goldfish both in vivo and in vitro. The GH-releasing action of PACAP is mediated via pituitary PAC1 receptors coupled to the adenylate cyclase-cAMP-protein kinase A and phospholipase C-IP3-protein kinase C pathways. Subsequent stimulation of Ca2+ entry through voltage-sensitive Ca2+ channels followed by activation of Ca2+-calmodulin protein kinase II is likely the downstream mechanism mediating PACAP-stimulated GH release in goldfish. Although the PACAP receptor subtype(s) and the associated post-receptor signaling events responsible for PACAP-stimulated GTH-II release have not been characterized in goldfish, these findings support the hypothesis that PACAP is produced in the hypothalamus and delivered to the anterior pituitary to regulate GH and GTH-II release in fish.Key words: PACAP, VIP, PAC1 receptor, VPAC1 receptor, VPAC2 receptor, growth hormone, gonadotropin-II, cAMP, protein kinase A, protein kinase C, calcium, pituitary cells, goldfish, and teleost.

scholarly journals Phosphorylation of low molecular mass cytosolic proteins by protein kinase C and protein kinase A in the rabbit exocrine pancreas

1989 ◽  
Vol 185 (2) ◽  
pp. 461-468 ◽  
Author(s):  
Antoine G. H. EDERVEEN ◽  
Jos V. M. LEEST ◽  
Sjenet E. EMST-DE VRIES ◽  
Jan Joep H. H. M. PONT
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Molecular Mass ◽  
Protein Kinase A ◽  
Exocrine Pancreas ◽  
Cytosolic Proteins ◽  
Kinase C ◽  
Kinase A

Activators of protein kinase A and of protein kinase C inhibit MDCK cell myo-inositol and betaine uptake.

1995 ◽  
Vol 6 (6) ◽  
pp. 1559-1564
Author(s):  
A S Preston ◽  
A Yamauchi ◽  
H M Kwon ◽  
J S Handler
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Translational Regulation ◽  
Mdck Cells ◽  
Relative Effect ◽  
Amino Acid Sequences ◽  
Prolonged Incubation ◽  
Kinase C ◽  
Kinase A

Amino acid sequences of the myo-inositol and betaine cotransporters that are induced in MDCK cells by hypertonicity include consensus sequences for phosphorylation by protein kinase A and by protein kinase C. To test for the effect of activation of protein kinases A and C on the activity of those cotransporters, MDCK cells were exposed to activators of each kinase and the activity of both cotransporters was assayed. Incubation with 8-bromoadenosine 3':5'-cyclic monophosphate (8Br-cAMP) or 3-isobutyl-1-methylxanthine (IBMX), activators of protein kinase A, and incubation with an active phorbol ester or with an active diacylglycerol, activators of protein kinase C, inhibited the activity of both cotransporters by about 30%. The relative effect of the activation of protein kinase A and of protein kinase C was similar in hypertonic and isotonic cells. The effects of activators of protein kinase A and of protein kinase C were not additive. The two cotransporters behaved differently when protein kinase C activity was down-regulated by prolonged incubation with a higher concentration of phorbol 12-myristate 13-acetate. There was a doubling of activity of the myo-inositol cotransporter and no change in the activity of the betaine cotransporter in hypertonic and isotonic cells. Although the mechanisms of the effects of activation of the two kinases remain to be established, it is clear that the kinases can mediate post-translational regulation of the uptake of compatible osmolytes.

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