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Titolo:
Hormonal regulation of phospholipase D activity in Ca2+ transporting cellsof rabbit connecting tubule and cortical collecting duct
Autore:
Bosch, RR; Hoenderop, JGJ; van der Heijden, L; De Pont, JJHHM; Bindels, RJM; Willems, PHGM;
Indirizzi:
Univ Nijmegen, Med Ctr, Dept Biochem 160, NL-6500 HB Nijmegen, NetherlandsUniv Nijmegen Nijmegen Netherlands NL-6500 HB 0 HB Nijmegen, Netherlands Univ Nijmegen, Med Ctr, Dept Cell Physiol, NL-6500 HB Nijmegen, Netherlands Univ Nijmegen Nijmegen Netherlands NL-6500 HB 0 HB Nijmegen, Netherlands
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
fascicolo: 2-3, volume: 1538, anno: 2001,
pagine: 329 - 338
SICI:
0167-4889(20010423)1538:2-3<329:HROPDA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; MUSCARINIC ACETYLCHOLINE-RECEPTORS; ADP-RIBOSYLATION-FACTOR; FRTL-5 THYROID-CELLS; CANINE KIDNEY-CELLS; CALCIUM-TRANSPORT; D ACTIVATION; CYTOSOLIC CA2+; PHORBOL ESTER; STIMULATION;
Keywords:
cortical collecting duct; connecting tubule; Ca2+ reabsorption; vasopressin; ATP; N-6-cyclopentyladenosine; chelerythrine; phorbol ester;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Willems, PHGM Univ Nijmegen, Med Ctr, Dept Biochem 160, POB 9101, NL-6500 HB Nijmegen, Netherlands Univ Nijmegen POB 9101 Nijmegen Netherlands NL-6500 HB ands
Citazione:
R.R. Bosch et al., "Hormonal regulation of phospholipase D activity in Ca2+ transporting cellsof rabbit connecting tubule and cortical collecting duct", BBA-MOL CEL, 1538(2-3), 2001, pp. 329-338

Abstract

Phospholipase D (PLD is distributed widely in mammalian tissues where it is believed to play an important role in the regulation of cell functions and cell fate by a variety of extracellular signals. In this study, we used primary cultures of rabbit connecting tubule (CNT) and cortical collecting duct (CCD) cells, sown to confluence on a permeable support, to investigate the possible involvement of PLD in the mechanism of action of hormones thatregulate Ca2+ reabsorption. RT-PCR revealed the presence of transcripts ofPLD1b and PLD2, but not PLD1a, in these cultures. Moreover, the expressionof substantial amounts of PLD1 protein was demonstrated by Western blotting. To measure PLD activity, cells were labelled with [H-3]myristic acid after which the PLD-catalysed formation of radiolabelled phosphatidylethanol ([H-3]PtdEth) was measured in the presence of 1% (v/v) ethanol. Deamino-Cys.D-Arg(8)-vasopressin (dDAVP) and N-6-cyclopentyladenosine (CPA), two potentstimulators of Ca2+ transport across these monolayers, stimulated PLD activity as was indicated by a marked increase in [H-3]PtdEth. Similarly, ATP, a potent inhibitor of dDAVP- and CPA-stimulated Ca2+ transport, increased the formation of [H-3]PtdEth. PLD activity was furthermore increased by 8Br-cAMP and following acute (30 min) stimulation of protein kinase C (PKC) with a phorbol ester (PMA). Chronic PMA treatment (120 hi to downregulate phorbol ester-sensitive PKC isoforms did not affect PLD activation by dDAVP, CPA and 8Br-cAMP, while markedly decreasing the effect of ATP and abolishing the affect of PMA. The PKC inhibitor chelerythrine significantly reduced PLD activation by dDAVP, CPA and 8Br-cAMP, without changing the effect of ATP. The inhibitor only partially reduced the effect of PMA. This study shows that Ca2+ transporting cells of CNT and CCB contain a regulated PLD activity. The physiological relevance of this activity, which is not involved in Ca2+ reabsorption, remains to be established (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 27/09/20 alle ore 06:59:00