نتایج جستجو برای: phospholipase d (pld)

تعداد نتایج: 596477  

دنینگ, دیوید, رابسون, جفری, کاظمی, عبدالحسن,

Background and Objective: Secretory extracellular Phospholipases are generally involved in hydrolysis of extracellular phospholipids and thus providing nutritive source of carbon, nitrogen, and phosphate. However, intracellular phospholipases perform metabolic functions and adjust biologic activities. Synthesis of phospholipases in different pathogenic microorganisms and their mode of action in...

Journal: :iranian journal of microbiology 0
ad noodeh department of life sciences, faculty of science and technology, anglia ruskin university, cambridge, uk. n singh department of life sciences, faculty of science and technology, anglia ruskin university, cambridge, uk. gd robson department of immunology and microbiology, faculty of life sciences, university of manchester, manchester, uk.

background and objectives: phospholipases are a group of enzymes that breakdown phospholipid molecules producing second products. these second products play a diverse role in the cell such as signal transduction and digestion in humans. in this study, the effect of phospholipids on the expression of pld genes of a. fumigatus was investigated. the pld genes of this fungus were also investigated ...

Journal: :Japanese Journal of Pharmacology 1997

Journal: :Journal of Biological Chemistry 1997

Journal: :The Biochemical journal 1992
B Geny S Cockcroft

Stimulation of phospholipase D (PLD) by cell surface receptors has been observed in many cell types. We have investigated the mechanism of activation of this enzyme in undifferentiated HL60 cells. GTP analogues and Ca2+ (buffered in the nanomolar to micromolar range) were introduced into HL60 cells in the presence of the permeabilizing agent, streptolysin O. We report that guanosine 5'-[gamma-t...

Journal: :The Biochemical journal 1992
I J Uings N T Thompson R W Randall G D Spacey R W Bonser A T Hudson L G Garland

The tyrosine kinase inhibitors ST271, ST638 and erbstatin inhibited phospholipase D (PLD) activity in human neutrophils stimulated by fMet-Leu-Phe, platelet-activating factor and leukotriene B4. These compounds did not inhibit phorbol ester-stimulated PLD, indicating that they do not inhibit PLD per se, but probably act at a site between the receptor and the phospholipase. In contrast, the prot...

Journal: :The Biochemical journal 1996
K M Ella J W Dolan C Qi K E Meier

A gene encoding phospholipase D (PLD) in Saccharomyces cerevisiae was identified. The 195 kDa product of PLD1 has 24% overall sequence identity with a plant PLD. Expression of yeast PLD activity was eliminated by one-step gene disruption. Yeast haploids lacking PLD activity were deficient in growth on non-fermentable carbon sources. Diploids lacking expression of PLD1 were unable to sporulate.

Journal: :Anesthesia and analgesia 2002
Jinen Chen Shuji Dohi Zhiming Tan Yoshiko Banno Yoshinori Nozawa

UNLABELLED Bradykinin induces activation of phospholipase D (PLD) via B(2) receptors in neuronal cells. To demonstrate molecular mechanism(s) of local anesthetics, we examined whether and how local anesthetics affect bradykinin-induced PLD activation in PC12 cells. Using [(3)H]Palmitic acid-labeled PC12 cells stimulated with bradykinin, formation of [(3)H]phosphatidylbutanol was measured as a v...

Journal: :Journal of lipid research 2002
Encarnación Pérez-Andrés María Fernández-Rodriguez Mónica González Ana Zubiaga Ainara Vallejo Itxaso García Carlos Matute Stéphanie Pochet Jean Paul Dehaye Miguel Trueba Aida Marino Antonio Gómez-Muñoz

Exogenous ATP stimulated phospholipase D (PLD), but not sphingomyelinase in rat submandibular gland (SMG) acini. PLD activation was dependent upon extracellular Ca(2+) and did not involve intracellular Ca(2+) mobilization or phosphoinositide-specific phospholipase C activation. ATP-stimulated PLD was attenuated by inhibition or downregulation of protein kinase C (PKC). PLD activation was fully ...

Journal: :The Biochemical journal 1991
M Liscovitch V Chalifa M Danin Y Eli

The effects of aminoglycoside antibiotics on phospholipase D (PLD) activity were investigated in permeabilized NG108-15 cells and in isolated rat brain membranes. Neomycin inhibited guanosine 5'-[gamma-thio]triphosphate-stimulated PLD activity in digitonin-permeabilized NG108-15 cells in a concentration-dependent manner (50% inhibition at 100 microM). Neomycin similarly inhibited PLD activity p...

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