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Studies with protein kinase C inhibitors presently available cannot elucidate the role of protein kinase C in the activation of NADPH oxidase

Seifert, Roland and Schächtele, C. (1988) Studies with protein kinase C inhibitors presently available cannot elucidate the role of protein kinase C in the activation of NADPH oxidase. Biochemical and biophysical research communications 152 (2), pp. 585-592.

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Abstract

The effects of various protein kinase C (PKC) inhibitors on NADPH oxidase (NO) activation by the phorbol ester PMA and by the chemotactic peptide FMLP were studied. H-7 reduced the effects of both stimuli in human neutrophils (HN) and HL-60 cells by 13-63%. Polymyxin B did not inhibit NO activation by PMA and FMLP in HN and reduced the effects of both stimuli in HL-60 cells by 27-55%. Retinal and ...

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Item Type:Article
Date:1988
Institutions:Chemistry and Pharmacy > Institute of Pharmacy > Pharmacology and Toxicology (Prof. Schlossmann formerly Prof. Seifert)
Identification Number:
ValueType
2835037PubMed ID
Classification:
NotationType
1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineMESH
Cytochalasin B/pharmacologyMESH
Enzyme Activation/drug effectsMESH
FemaleMESH
HumansMESH
Isoquinolines/pharmacologyMESH
MaleMESH
N-Formylmethionine Leucyl-Phenylalanine/pharmacologyMESH
NADH, NADPH Oxidoreductases/metabolismMESH
Neutrophils/enzymologyMESH
Piperazines/pharmacologyMESH
Protein Kinase C/physiologyMESH
Superoxides/metabolismMESH
Tetradecanoylphorbol Acetate/pharmacologyMESH
Tumor Cells, CulturedMESH
Subjects:600 Technology > 610 Medical sciences Medicine
600 Technology > 615 Pharmacy
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Unknown
Owner: Universitätsbibliothek Regensburg
Deposited On:26 Jan 2012 08:33
Last Modified:13 Mar 2014 18:29
Item ID:23268
Owner Only: item control page

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