Aquaporin-1 channel function is positively regulated by protein kinase C. (Q48792407)

15 February 2018

title

Aquaporin-1 channel function is positively regulated by protein kinase C. (English)

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15 February 2018

11

Hugo Katus

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author name string

Wei Zhang

1

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15 February 2018

Edgar Zitron

2

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Meike Hömme

3

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Lars Kihm

4

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Christian Morath

5

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Daniel Scherer

6

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Stephan Hegge

7

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Dierk Thomas

8

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Claus P Schmitt

9

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Martin Zeier

10

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Christoph Karle

12

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Vedat Schwenger

13

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language of work or name

English

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publication date

23 May 2007

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Journal of Biological Chemistry

published in

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volume

282

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issue

29

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page(s)

20933-20940

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Aquaporin water channels--from atomic structure to clinical medicine

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Human cardiac inwardly-rectifying K+ channel Kir(2.1b) is inhibited by direct protein kinase C-dependent regulation in human isolated cardiomyocytes and in an expression system

21 January 2018

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High glucose-induced human umbilical vein endothelial cell hyperpermeability is dependent on protein kinase C activation and independent of the Ca2+-nitric oxide signalling pathway

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Regulation of skin microvasculature angiogenesis, cell migration, and permeability by a specific inhibitor of PKCalpha

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Inhibition of protein kinase Calpha prevents endothelial cell migration and vascular tube formation in vitro and myocardial neovascularization in vivo

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Human cardiac inwardly rectifying current IKir2.2 is upregulated by activation of protein kinase A.

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Single amino acids in the carboxyl terminal domain of aquaporin-1 contribute to cGMP-dependent ion channel activation

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Mechanism of Gating and Ion Conductivity of a Possible Tetrameric Pore in Aquaporin-1

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Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry.

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Delayed K+ clearance associated with aquaporin-4 mislocalization: phenotypic defects in brains of alpha-syntrophin-null mice

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21 January 2018

Identifiers

DOI

10.1074/JBC.M703858200

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15 February 2018

PubMed ID

17522053

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15 February 2018