scholarly journals A KCNQ1 mutation contributes to the concealed type 1 long QT phenotype by limiting the Kv7.1 channel conformational changes associated with protein kinase A phosphorylation

Heart Rhythm ◽  
2014 ◽  
Vol 11 (3) ◽  
pp. 459-468 ◽  
Author(s):  
Daniel C. Bartos ◽  
John R. Giudicessi ◽  
David J. Tester ◽  
Michael J. Ackerman ◽  
Seiko Ohno ◽  
...  
1995 ◽  
Vol 306 (1) ◽  
pp. 147-151 ◽  
Author(s):  
R Lecocq ◽  
F Lamy ◽  
C Erneux ◽  
J E Dumont

A method is presented for the rapid purification of dog thyroid calcyphosine, a protein previously identified as a major substrate for cyclic AMP-dependent protein kinase in dog thyroid slices stimulated by thyrotropin [Lecocq, Lamy and Dumont (1979) Eur. J. Biochem. 102, 147-152]. The protein was previously identified as a spot on two-dimensional gels and is now purified in its native form by a procedure involving three chromatographic steps. Homogeneous calcyphosine identified by SDS/PAGE, immunoblotting and peptide sequencing can be obtained within 7 h. As for calmodulin, Ca(2+)-dependent conformational changes can be shown by Ca(2+)-dependent hydrophobic interaction chromatography using phenyl-Sepharose. Unlike calmodulin, calcyphosine is a substrate for protein kinase A.


2016 ◽  
Vol 32 (2) ◽  
pp. 333-346 ◽  
Author(s):  
Catherine Le Stunff ◽  
Francoise Tilotta ◽  
Jérémy Sadoine ◽  
Dominique Le Denmat ◽  
Claire Briet ◽  
...  

1996 ◽  
Vol 270 (1) ◽  
pp. G103-G112 ◽  
Author(s):  
T. Urushidani ◽  
T. Nagao

The effects of pkadaic acid (OKA) and calyculin A (CLA), inhibitors of protein phosphatases type 1 (PrPase1) and type 2A (PrPase2A), an acid secretion were examined in rabbit isolated gastric gland, CLA, but not OKA, strongly stimulated acid secretion by itself without affecting glandular adenosine 3',5'-cyclic monophosphate (cAMP) contents. CLA-induced secretion was suggested to be mainly due to the increase in the phosphorylation of protein kinase A substrates via the inhibition of PrPase1 in the parietal cell, since 1) CLA-induced secretion was not inhibited by cimetidine or atropine, 2) a protein kinase A inhibitor inhibited the secretion, whereas a protein kinase C inhibitor did not, 3) CLA augmented dibutyryl cAMP-induced secretion in some cases, and 4) OKA, which is 100 times more selective to PrPase2A than to PrPase1, was not a secretagogue. Unexpectedly, CLA did not augment the secretion by histamine, possibly because the inhibitor augmented the phosphorylation-mediating negative feedback pathway as well. Both CLA and OKA markedly increased phosphorylation of ezrin, a putative protein kinase A substrate, in the course of secretory activation.


2010 ◽  
Vol 31 (4) ◽  
pp. 369-379 ◽  
Author(s):  
Anélia Horvath ◽  
Jérôme Bertherat ◽  
Lionel Groussin ◽  
Marine Guillaud-Bataille ◽  
Kitman Tsang ◽  
...  

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