Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells.

Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells. Research Abstract Details 

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Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells. Abstract Text:

R Nozawa,H Kato,T Yokota,

NADPH oxidase was induced in HL-60 human promyelocytic leukemia cells when these cells were treated with 10(-7) M 1,25-dihydroxyvitamin D3 (VD3) for 4 days. The treated cells were disrupted by sonication, and the postnuclear fraction was separated into 48,000 X g supernatant (cytosol) and precipitate (membrane) fractions. Membrane-bound NADPH oxidase was activated in vitro with SDS and cytosol. However, the cytosol from untreated HL-60 cells could not activate NADPH oxidase. The cytosolic activity was induced 2 days after VD3 treatment and fully expressed on day 4. The activity was heat-sensitive and destroyed by trypsin. The possibility that the cytosolic activation factor is a protein kinase C (PKC) was then tested. Ca2+- and phospholipid-dependent PKC activity was low in the cytosol of untreated HL-60 cells but increased in the cytosols of VD3-treated cells 4 and 11 times, respectively, 2 days and 4 days after treatment. H-7 [1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride], inhibited PKC activity in a dose-dependent manner at 1-100 microM. Cytosolic activity of NADPH oxidase was not inhibited at all at those concentrations. Furthermore, PKC activity was lost when Ca2+ was omitted from the assay mixture, but NADPH oxidase was activated in the presence of EGTA. These results indicated that the cytosolic factor is not a PKC, and that NADPH oxidase in this cell-free system is activated by a mechanism that does not involve PKC.

Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells. Publishing Authors By Initials

R Nozawa,H Kato,T Yokota,

For similar enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: protein kinase c research abstracts see: enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: protein kinase c research

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Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 103

Page Numbers: 43-7

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 1988

Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells. Keywords Mesh Terms:

KEYWORDS: Protein Kinase C

MESH TERMS: antagonists & inhibitors

Chemical & Substance for Abstract: Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells. Information

Substance Name: Protein Kinase C

Registry Number: EC 2.7.11.13

Grant and Affiliation Information for Induction of cytosolic activation factor for NADPH oxidase in differentiated HL-60 leukemia cells.

AFFILIATION: Department of Bacteriology, Juntendo University School of Medicine, Tokyo.

Country: JAPAN

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MEDLINETA: J Biochem

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