Bile acids stimulate PKCalpha autophosphorylation and activation: role in the attenuation of prostaglandin E1-induced cAMP production in human dermal fibroblasts (Q28241149)

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scientific article (publication date: August 2006)

Language	Label	Description	Also known as
English	Bile acids stimulate PKCalpha autophosphorylation and activation: role in the attenuation of prostaglandin E1-induced cAMP production in human dermal fibroblasts	scientific article (publication date: August 2006)

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scholarly article

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Bile acids stimulate PKCalpha autophosphorylation and activation: role in the attenuation of prostaglandin E1-induced cAMP production in human dermal fibroblasts (English)

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author name string

Man Le

1

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Lada Krilov

2

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Jianping Meng

3

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Kelli Chapin-Kennedy

4

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Susan Ceryak

5

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Bernard Bouscarel

6

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language of work or name

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publication date

August 2006

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American Journal of Physiology - Gastrointestinal and Liver Physiology

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291

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2

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G275-87

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Hepatic uptake of bile acids in man. Fasting and postprandial concentrations of individual bile acids in portal venous and systemic blood serum

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Hepatotoxic bile acids increase cytosolic Ca++ activity of isolated rat hepatocytes

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cPKC-dependent sequestration of membrane-recycling components in a subset of recycling endosomes

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Bile acids as endogenous vasodilators?

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Signal transduction and hepatocellular bile acid transport: cross talk between bile acids and second messengers

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The role of protein kinase C in the inactivation of hepatic glycogen synthase by calcium-mobilizing agonists

1 reference

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Threonine-497 is a critical site for permissive activation of protein kinase C alpha

1 reference

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Extrahepatic deposition and cytotoxicity of lithocholic acid: studies in two hamster models of hepatic failure and in cultured human fibroblasts.

1 reference

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Bile acids mobilise internal Ca2+ independently of external Ca2+ in rat hepatocytes

1 reference

https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

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Protein kinase C--a question of specificity

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https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

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The regulation of protein kinase C by chenodeoxycholate, deoxycholate and several structurally related bile acids.

1 reference

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Bile acids, non-phorbol-ester-type tumor promoters, stimulate the phosphorylation of protein kinase C substrates in human platelets and colon cell line HT29

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Protein kinase C isoenzymes: divergence in signal transduction?

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Instability of the G-protein beta5 subunit in detergent

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Ca2+-dependent protein kinase C isoforms induce cholestasis in rat liver

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

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Deoxycholic acid activates protein kinase C and phospholipase C via increased Ca2+ entry at plasma membrane.

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https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

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Protein kinase C phosphorylated at a conserved threonine is retained in the cytoplasm.

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https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

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Protein kinase C: structure, function, and regulation

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Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions

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Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm

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Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C

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Protein kinase C--a family affair

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A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis

1 reference

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Contributions to maxima in protein kinase C activation

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https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

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Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes.

1 reference

https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

21 January 2018

Diurnal changes in serum unconjugated bile acids in normal man.

1 reference

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Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element

1 reference

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Distinctive activation mechanisms and functions for protein kinase Cdelta

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Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Calpha in response to diacylglycerol

1 reference

https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

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The bile acid analog fusidic acid can replace phosphatidylserine in the activation of protein kinase C by 12-O-tetradecanoylphorbol 13-acetate in vitro

1 reference

https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

21 January 2018

Down-regulation of protein kinase C is due to an increased rate of degradation

1 reference

https://api.crossref.org/works/10.1152%2FAJPGI.00346.2005

21 January 2018

The role of protein kinase C in cell surface signal transduction and tumour promotion

1 reference

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Bile Acids on the Skin of Patients with Pruritic Hepatobiliary Disease

1 reference

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21 January 2018

Identifiers

10.1152/AJPGI.00346.2005

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