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Titolo:
Presence of a phospholipase D (PLD) distinct from PLD1 or PLD2 in human neutrophils: immunobiochemical characterization and initial purification
Autore:
Horn, JM; Lehman, JA; Alter, G; Horwitz, J; Gomez-Cambronero, J;
Indirizzi:
Wright State Univ, Dept Physiol & Biophys, Sch Med, Dayton, OH 45435 USA Wright State Univ Dayton OH USA 45435 phys, Sch Med, Dayton, OH 45435 USA Wright State Univ, Sch Med, Dept Anat, Dayton, OH 45435 USA Wright State Univ Dayton OH USA 45435 ed, Dept Anat, Dayton, OH 45435 USA Wright State Univ, Sch Med, Dept Biochem & Mol Biol, Dayton, OH 45435 USA Wright State Univ Dayton OH USA 45435 em & Mol Biol, Dayton, OH 45435 USA Allegheny Univ Hlth Sci, MCP Hahnemann Sch Med, Philadelphia, PA 19129 USAAllegheny Univ Hlth Sci Philadelphia PA USA 19129 ladelphia, PA 19129 USA
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
fascicolo: 1, volume: 1530, anno: 2001,
pagine: 97 - 110
SICI:
1388-1981(20010115)1530:1<97:POAPD(>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADP-RIBOSYLATION FACTOR; PHOSPHATIDIC-ACID PRODUCTION; GTP-BINDING PROTEIN; CELL-FREE SYSTEM; RAT-BRAIN; NADPH OXIDASE; STIMULATED NEUTROPHILS; SUPEROXIDE GENERATION; ISCHEMIA-REPERFUSION; SIGNAL-TRANSDUCTION;
Keywords:
phospholipase D; enzyme characterization; neutrophil; signal transduction; phosphotyrosine;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Gomez-Cambronero, J Wright State Univ, Dept Physiol & Biophys, Sch Med, Dayton, OH 45435 USA Wright State Univ Dayton OH USA 45435 n, OH 45435 USA
Citazione:
J.M. Horn et al., "Presence of a phospholipase D (PLD) distinct from PLD1 or PLD2 in human neutrophils: immunobiochemical characterization and initial purification", BBA-MOL C B, 1530(1), 2001, pp. 97-110

Abstract

Utilizing the transphosphatidylation reaction catalyzed by phospholipase D(PLD) in the presence of a primary alcohol and the short-chain phospholipid PC8, we have characterized the enzyme from human neutrophils. A pH optimum of 7.8-8.0 was determined. PIP2, EDTA/EGTA, and ATP were found to enhancebasal PLD activity in vitro. Inhibitory elements were: oleate, Triton X-100, n-octyl-beta -glucopyranoside, divalent cations, GTP gammaS and H2O2. The apparent K-m for the butanol substrate was 0.1 mM and the V-max was 6.0 nmol mg(-1) h(-1). Immunochemical analysis by anti-pan PLD antibodies revealed a neutrophil PLD of similar to 90 kDa and other bands recognized minimally by anti-PLD1 or anti-PLD2 antibodies. The 90-kDa protein is tyrosine-phosphorylated upon cell stimulation with GM-CSF and formyl-Met-Leu-Phe. Protein partial purification using column liquid chromatography was performed after cell subfractionation. Based on the enzyme's regulatory and inhibitory factors, and its molecular weight, these data indicate an enzyme isoform that might be different from die mammalian PLD1/2 forms described earlier. The present results lay the foundation for further purification of this granulocyte PLD isoform. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 25/01/20 alle ore 09:31:05