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Titolo:
Phospholipase D (PLD) is present in Leishmania donovani and its activity increases in response to acute osmotic stress
Autore:
Blum, JJ; Lehman, JA; Horn, JM; Gomez-Cambronero, J;
Indirizzi:
Wright State Univ, Sch Med, Dept Physiol & Biophys, Dayton, OH 45435 USA Wright State Univ Dayton OH USA 45435 iol & Biophys, Dayton, OH 45435 USA Duke Univ, Med Ctr, Dept Cell Biol, Durham, NC 27710 USA Duke Univ DurhamNC USA 27710 d Ctr, Dept Cell Biol, Durham, NC 27710 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
Titolo Testata:
JOURNAL OF EUKARYOTIC MICROBIOLOGY
fascicolo: 1, volume: 48, anno: 2001,
pagine: 102 - 110
SICI:
1066-5234(200101/02)48:1<102:PD(IPI>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADP-RIBOSYLATION FACTOR; GTP-BINDING PROTEIN; PHOSPHATIDIC-ACID; MAJOR PROMASTIGOTES; NADPH OXIDASE; SURFACE LIPOPHOSPHOGLYCAN; ENDOPLASMIC-RETICULUM; HUMAN NEUTROPHILS; GENE FAMILY; ACTIVATION;
Keywords:
cell volume changes; cytoskeleton; immune complex enzyme assay; Leishmania; phospholipase D; PLD;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Gomez-Cambronero, J Wright State Univ, Sch Med, Dept Physiol & Biophys, Dayton, OH 45435 USA Wright State Univ Dayton OH USA 45435 n, OH 45435 USA
Citazione:
J.J. Blum et al., "Phospholipase D (PLD) is present in Leishmania donovani and its activity increases in response to acute osmotic stress", J EUKAR MIC, 48(1), 2001, pp. 102-110

Abstract

We report here that the signaling molecule phospholipase D (PLD) is present in the parasitic protozoan Leishmania donovani. In vitro enzymatic activity is dependent on Ca2+ and Mg2+ ions. its basal activity is stimulated by phosphatidyl-inositol-4,5-bisphosphate (PIP2), and its pH optima are pH 8.0and pH 6.0. PLD activity increases 3-fold about 5 min after an abrupt decrease in osmolality from 317 mOsm (isosmotic) to 155 mOsm and increases 1.5-fold in response to an abrupt increase in osmolality to 617 mOsM. Cells grown for > 24 h under the anisosmotic conditions showed only marginal changesin activity compared to the controls grown under isosmotic conditions. indicating an adaptation to long-term exposure to hypo- or hyper-osmolarity. Immunologically, two isoforms, PLD1 and PLD2, are present. An analysis of invitro PLD activity in anti-PLD immunocomplexes revealed that either hypotonic (cell swelling) or hypertonic stress (cell shrinking) causes an increase in PLD1 activation but a reduction in PLD2 activity. The interplay between these two isoforms results in a predominance for PLD1 in the observed increase when measuring total PLD activity. Finally, the increase in enzymaticactivity in acute hyposmotic shock is accompanied by tyrosyl phosphorylation of the PLD1 isoform, suggesting a role for protein tyrosine kinase in the control of PLD activity in response to osmotic stress.

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Documento generato il 19/09/20 alle ore 21:56:54