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Titolo:
ADENOSINE TRIPHOSPHATE-DEPENDENT COPPER TRANSPORT IN HUMAN LIVER
Autore:
DIJKSTRA M; VANDENBERG GJ; WOLTERS H; VELD GI; SLOOFF MJH; HEYMANS GSA; KUIPERS F; VONK RJ;
Indirizzi:
UNIV GRONINGEN HOSP,LAB NUTR & METAB,HANZEPL 1,POSTBUS 30001 NL-9700 RB GRONINGEN NETHERLANDS UNIV GRONINGEN HOSP,GRONINGEN INST DRUG STUDIES,DEPT PEDIAT GRONINGENNETHERLANDS UNIV GRONINGEN HOSP,GRONINGEN INST DRUG STUDIES,DEPT SURG GRONINGEN NETHERLANDS DELFT UNIV TECHNOL,INST INTERFAC REACTOR NL-2629 JB DELFT NETHERLANDS
Titolo Testata:
Journal of hepatology
fascicolo: 1, volume: 25, anno: 1996,
pagine: 37 - 42
SICI:
0168-8278(1996)25:1<37:ATCTIH>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
WILSON DISEASE GENE; PLASMA-MEMBRANE VESICLES; P-TYPE ATPASES; MENKES DISEASE; CANDIDATE GENE; RAT-LIVER; CANALICULAR MEMBRANE; BILE-SALT; ATP; GLUTATHIONE;
Keywords:
BILE CANALICULAR MEMBRANE; COPPER; P-TYPE ATPASE; TRANSPORT KINETICS; VESICLE; WILSON DISEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
M. Dijkstra et al., "ADENOSINE TRIPHOSPHATE-DEPENDENT COPPER TRANSPORT IN HUMAN LIVER", Journal of hepatology, 25(1), 1996, pp. 37-42

Abstract

Background/Aim: The recent cloning and sequencing of the Wilson disease gene indicates that hepatic copper (Cu) transport is mediated by a P-type ATPase. The location of this Cu-transporting protein within thehepatocyte is not known; in view of its proposed function and currentconcepts of hepatic Cu transport, it may reside in intracellular membranes (endoplasmic reticulum (ER), lysosomes) and/or in the bile canalicular membrane, The objective of this study was to establish characteristics and localization of ATP-dependent Cu transport in human liver. Methods: We have investigated Cu transport in vesicles of human liverplasma membranes showing a gradual increase in enrichment of canalicular domain markers: i.e. basolateral liver plasma membranes (blLPM), amixed population of basolateral and canalicular (XLPM) and canalicular liver plasma membranes (cLPM). Results: In the presence of ATP (4 mM) and an ATP-regenerating system, uptake of radiolabeled Cu (Cu-64, 10mu M) into cLPM vesicles and, to a lesser extent, into blLPM and XLPMwas clearly stimulated when compared to control AMP values. Initial uptake rates of ATP-dependent Cu transport were 5.6, 7.8 and 13.7 nmol . min(-1). mg(-1) protein for blLPM, XLPM and cLPM, respectively, and showed no relationship with marker enzyme activity of ER and lysosomes(glucose-6-phosphatase and acid-phosphatase, respectively). Leucine aminopeptidase activity, as a marker for the cLPM, significantly correlated with ATP-dependent uptake rates measured in different membrane preparations: r=0.70 (n=9, p<0.05). Estimated K-m and V-max values of ATP-dependent Cu uptake were 49.5 mu M and 36.9 nmol . min(-1). mg(-1) protein, respectively. Conclusion: This study provides biochemical evidence for the presence of an ATP-dependent Cu transport system in humanliver (cCOP), mainly localized at the canalicular domain of the hepatocytic plasma membrane.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 17/01/21 alle ore 17:20:41