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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 391, Issue 1

Issues

Hexose-6-phosphate dehydrogenase in the endoplasmic reticulum

Silvia Senesi
  • Department of Pathophysiology, Experimental Medicine and Public Health, University of Siena, I-53100 Siena, Italy
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/ Miklos Csala
  • Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, H-1094 Budapest, Hungary
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/ Paola Marcolongo
  • Department of Pathophysiology, Experimental Medicine and Public Health, University of Siena, I-53100 Siena, Italy
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/ Rosella Fulceri
  • Department of Pathophysiology, Experimental Medicine and Public Health, University of Siena, I-53100 Siena, Italy
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/ Jozsef Mandl
  • Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, H-1094 Budapest, Hungary
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/ Gabor Banhegyi
  • Department of Pathophysiology, Experimental Medicine and Public Health, University of Siena, I-53100 Siena, Italy
  • Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, H-1094 Budapest, Hungary
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/ Angelo Benedetti
  • Department of Pathophysiology, Experimental Medicine and Public Health, University of Siena, I-53100 Siena, Italy
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Published Online: 2009-10-06 | DOI: https://doi.org/10.1515/bc.2009.146

Abstract

Hexose-6-phosphate dehydrogenase (H6PD) is a luminal enzyme of the endoplasmic reticulum that is distinguished from cytosolic glucose-6-phosphate dehydrogenase by several features. H6PD converts glucose-6-phosphate and NADP+ to 6-phosphogluconate and NADPH, thereby catalyzing the first two reactions of the pentose-phosphate pathway. Because the endoplasmic reticulum has a separate pyridine nucleotide pool, H6PD provides NADPH for luminal reductases. One of these enzymes, 11β-hydroxysteroid dehydrogenase type 1 responsible for prereceptorial activation of glucocorticoids, has been the focus of much attention as a probable factor in the pathomechanism of several human diseases including insulin resistance and the metabolic syndrome. This review summarizes recent advances related to the functions of H6PD.

Keywords: apparent cortisone reductase deficiency; glucocorticoids; glucose-6-phosphate; 11β-hydroxysteroid dehydrogenase type 1; NADPH

About the article

Corresponding author


Received: 2009-08-05

Accepted: 2009-09-03

Published Online: 2009-10-06

Published in Print: 2010-01-01


Citation Information: Biological Chemistry, Volume 391, Issue 1, Pages 1–8, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2009.146.

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