Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Protein kinase C-mediated regulation of the renal Na+/dicarboxylate cotransporter, NaDC-1
Autore:
Pajor, AM; Sun, N;
Indirizzi:
Univ Texas, Med Branch, Dept Physiol & Biophys, Galveston, TX 77555 USA Univ Texas Galveston TX USA 77555 siol & Biophys, Galveston, TX 77555 USA
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
fascicolo: 1-2, volume: 1420, anno: 1999,
pagine: 223 - 230
SICI:
0005-2736(19990820)1420:1-2<223:PKCROT>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
BRUSH-BORDER MEMBRANE; SUBCELLULAR REDISTRIBUTION; SEROTONIN TRANSPORTERS; FUNCTIONAL REGULATION; XENOPUS-OOCYTES; RAT-KIDNEY; PHOSPHORYLATION; ACID; CITRATE; INHIBITION;
Keywords:
succinate; citrate; sodium co-transport; phorbol esters; membrane trafficking;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Pajor, AM Univ Texas, Med Branch, Dept Physiol & Biophys, Galveston, TX 77555 USA Univ Texas Galveston TX USA 77555 phys, Galveston, TX 77555 USA
Citazione:
A.M. Pajor e N. Sun, "Protein kinase C-mediated regulation of the renal Na+/dicarboxylate cotransporter, NaDC-1", BBA-BIOMEMB, 1420(1-2), 1999, pp. 223-230

Abstract

The Na+/dicarboxylate cotransporter of the renal proximal tubule, NaDC-1, reabsorbs Krebs cycle intermediates, such as succinate and citrate, from the tubular filtrate. Although long-term regulation of this transporter by chronic metabolic acidosis and K+ deficiency is well documented, there is no information on acute regulation of NaDC-1. In the present study, the transport of succinate in Xenopus oocytes expressing NaDC-1 was inhibited up to 95% by two activators of protein kinase C, phorbol 12-myristate, 13-acetate (PMA) and sn-1,2-dioctanoylglycerol (DOG). Activation of protein kinase A had no effect on NaDC-1 activity. The inhibition of NaDC-1 transport by PMA was dose-dependent, and could be prevented by incubation of the oocytes with staurosporine. Mutations of the two consensus protein kinase C phosphorylation sites in NaDC-1 did not affect inhibition by PMA. The inhibitory effects of PMA were partially prevented by cytochalasin D, which disrupts microfilaments and endocytosis. PMA treatment was also associated with a decrease of approximately 30% in the amount of NaDC-1 protein found on the plasma membrane. We conclude that the inhibition of NaDC-1 transport activity by PMA occurs by a combination of endocytosis and inhibition of transport activity. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 23:57:54