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Titolo:
IN-VITRO ACTIVATION OF A 60-70 KDA HISTONE H4 PROTEIN-KINASE FROM NEUTROPHILS BY LIMITED PROTEOLYSIS
Autore:
LIU RC; LEAVIS P; BADWEY JA;
Indirizzi:
BOSTON BIOMED RES INST,20 STANIFORD ST BOSTON MA 02114 BOSTON BIOMED RES INST BOSTON MA 02114 HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOLEC PHARMACOL BOSTON MA 02115
Titolo Testata:
Biochimica et biophysica acta. Protein structure and molecular enzymology
fascicolo: 1, volume: 1295, anno: 1996,
pagine: 89 - 95
SICI:
0167-4838(1996)1295:1<89:IAOA6K>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
FMET-LEU-PHE; SIGNAL-TRANSDUCTION; RESPIRATORY BURST; SYNERGISTIC STIMULATION; SUPEROXIDE PRODUCTION; CHEMOTACTIC FACTORS; PHOSPHORYLATION; SUBSTRATE; CALCIUM; CELLS;
Keywords:
NEUTROPHIL; SIGNAL TRANSDUCTION; PROTEIN KINASE; ACTIVATION, IN VITRO; HISTONE H4 PROTEIN KINASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
R.C. Liu et al., "IN-VITRO ACTIVATION OF A 60-70 KDA HISTONE H4 PROTEIN-KINASE FROM NEUTROPHILS BY LIMITED PROTEOLYSIS", Biochimica et biophysica acta. Protein structure and molecular enzymology, 1295(1), 1996, pp. 89-95

Abstract

Neutrophils stimulated with the chemotactic peptide fMet-Leu-Phe (fMLP) are known to exhibit a rapid and transient activation of a histone H4 kinase that may function in a stimulatory pathway downstream of phosphatidylinositol 3-kinase. The activity of this histone kinase in unstimulated neutrophils and cells treated with 1.0 mu M fMLP for 10 sec was 8.8 +/- 5 and 43 +/- 2 pmol P/min per 10(7) cells, respectively. In this paper, we report that unstimulated neutrophils contain a latentH4 kinase in the 100 000 X g soluble fraction that can be markedly activated by treatment with trypsin. The values for the untreated and trypsin treated enzyme were 5.5 +/- 1.0 and 63.6 +/- 18 pmol P/min per 10(7) cell-equivalents, respectively. This kinase was insensitive to a selective antagonist of protein kinase C (i.e., 50 mu M 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7)) but completely blocked by 100 nM staurosporine. Only a single peak of activity was observed for thisenzyme when the 100 000 x g supernatant fraction was fractionated on either an exclusion (KW-803) or an anion exchange column (DEAE), or during isoelectric focusing. The molecular weight of the latent kinase was 64 +/- 6 kDa and the isoelectric point was 7.6 +/- 0.1. During all fractionation procedures, the H4 kinase co-chromatographed with a trypsin-activated kinase that catalyzed the phosphorylation of a peptide which corresponds to residues 297-331 of the 47 kDa subunit of the NADPH-oxidase complex (p47-phox), The properties of the trypsin-activated H4 kinase from unstimulated neutrophils are very similar to those reported for this enzyme from fMLP-stimulated cells.

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Documento generato il 21/01/21 alle ore 04:03:00