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Molecular alterations of canalicular transport systems in experimental models of cholestasis: possible functional correlations.
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MedLine Citation:
PMID:  9626757     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The discovery of unidirectional, ATP-dependent canalicular transport systems (also termed "export pumps") for bile salts, amphiphilic anionic conjugates, lipophilic cations, and phospholipids has opened new opportunities for understanding biliary physiology and the pathophysiology of cholestasis. In addition, ATP-independent canalicular transport systems for glutathione and bicarbonate contribute to (bile acid-independent) bile formation. Canalicular excretion of bile salts and several non-bile acid organic anions is impaired in various experimental models of cholestasis. Recent cloning of several canalicular transport systems now facilitates studies on their molecular regulation in cholestasis. Although the picture is far from complete, experimental evidence now exists that decreased or even absent expression of canalicular transport proteins may explain impaired transport function resulting in hyperbilirubinemia and cholestasis. With the increasing availability of molecular probes for these transport systems in humans, new information on the molecular regulation of canalicular transport proteins in human cholestatic liver diseases is beginning to emerge and should bring new insights into their pathophysiology and treatment. This article gives an overview on molecular alterations of canalicular transport systems in experimental models of cholestasis and discusses the potential implications of these changes for the pathophysiology of cholestasis.
Authors:
M Trauner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  The Yale journal of biology and medicine     Volume:  70     ISSN:  0044-0086     ISO Abbreviation:  Yale J Biol Med     Publication Date:    1997 Jul-Aug
Date Detail:
Created Date:  1998-09-09     Completed Date:  1998-09-09     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0417414     Medline TA:  Yale J Biol Med     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  365-78     Citation Subset:  IM    
Affiliation:
Department of Internal Medicine, Karl Franzens University School of Medicine, Graz, Austria. michael.trauner@kfunigraz.ac.at
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
Animals
Anion Transport Proteins
Bicarbonates / metabolism
Bile Acids and Salts / metabolism
Bile Canaliculi / physiopathology*
Biological Transport, Active
Carrier Proteins / metabolism
Cholestasis / etiology,  genetics,  physiopathology*
Cholesterol / metabolism
Disease Models, Animal
Glutathione / metabolism
Humans
P-Glycoprotein / metabolism
Phospholipids / metabolism
Grant Support
ID/Acronym/Agency:
DK 34989/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Anion Transport Proteins; 0/Bicarbonates; 0/Bile Acids and Salts; 0/Carrier Proteins; 0/P-Glycoprotein; 0/Phospholipids; 56-65-5/Adenosine Triphosphate; 57-88-5/Cholesterol; 70-18-8/Glutathione
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Full Text
Journal Information
Journal ID (nlm-ta): Yale J Biol Med
Journal ID (pmc): yjbm
ISSN: 0044-0086
ISSN: 1551-4056
Publisher: Yale Journal of Biology and Medicine
Article Information
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Print publication date: Season: Jul?Aug Year: 1997
Volume: 70 Issue: 4
First Page: 365 Last Page: 378
ID: 2589339
PubMed Id: 9626757

Molecular alterations of canalicular transport systems in experimental models of cholestasis: possible functional correlations.
M. Trauner Email: michael.trauner@kfunigraz.ac.at
Department of Internal Medicine, Karl Franzens University School of Medicine, Graz, Austria.



Article Categories:
  • Research Article


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