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Titolo:
NHE3 activity and trafficking depend on the state of actin organization inproximal tubule
Autore:
Chalumeau, C; Du Cheyron, D; Defontaine, N; Kellermann, O; Paillard, M; Poggioli, J;
Indirizzi:
INSERM, U356, Inst Federat Rech 58, F-75270 Paris 06, France INSERM Paris France 06 6, Inst Federat Rech 58, F-75270 Paris 06, France Univ Paris 06, Hop Broussais, Assistance Publ, Paris, France Univ Paris 06 Paris France op Broussais, Assistance Publ, Paris, France Inst Pasteur, Lab Differenciat Cellulaire, Paris, France Inst Pasteur Paris France r, Lab Differenciat Cellulaire, Paris, France
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY
fascicolo: 2, volume: 280, anno: 2001,
pagine: F283 - F290
SICI:
0363-6127(200102)280:2<F283:NAATDO>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
NA+-H+ EXCHANGE; METABOLIC-ACIDOSIS; ANGIOTENSIN-II; RAT-KIDNEY; MEMBRANES; VESICLES; CELLS; ACTIVATION; ADAPTATION; TRANSPORT;
Keywords:
kidney; sodium/hydrogen exchanger 3 antiporter; protein trafficking;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Poggioli, J INSERM, U356, Inst Federat Rech 58, 15 Rue Ecole Med, F-75270 Paris 06, France INSERM 15 Rue Ecole Med Paris France 06 5270 Paris 06, France
Citazione:
C. Chalumeau et al., "NHE3 activity and trafficking depend on the state of actin organization inproximal tubule", AM J P-REN, 280(2), 2001, pp. F283-F290

Abstract

The present study was addressed to define the contribution of cytoskeletonelements in the kidney proximal tubule Na+/H+ exchanger 3 (NHE3) activity under basal conditions. We used luminal membrane vesicles (LMV) isolated from suspensions of rat cortical tubules pretreated with either colchicine (Colch) or cytochalasin D (Cyto D). Colch pretreatment of suspensions (200 muM for 60 min) moderately decreased LMV NHE3 activity. Cyto D pretreatment (1 muM for 60 min) elicited an increase in LMV NHE3 transport activity but did not increase Na-glucose cotransport activity. Cyto D pretreatment of suspensions did not change the apparent affinity of NHE3 for internal H+. In contrast, after Cyto D pretreatment of the suspensions, NHE3 protein abundance was increased in LMV and remained unchanged in cortical cell homogenates. The effect of Cyto D on NHE3 was further assessed with cultures of murinecortical cells. The amount of surface biotinylated NHE3 increased on Cyto D treatment, whereas NHE3 protein abundance was unchanged in cell homogenates. In conclusion, under basal conditions NHE3 activity depends on the state of actin organization possibly involved in trafficking processes between luminal membrane and intracellular compartment.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 20:08:18