Tissue-specific dysregulation of 11β-hydroxysteroid dehydrogenase type 1 and pathogenesis of the metabolic syndrome

2004 ◽  
Vol 27 (10) ◽  
pp. 969-974 ◽  
Author(s):  
P. Putignano ◽  
F. Pecori Giraldi ◽  
F. Cavagnini
2010 ◽  
Vol 391 (1) ◽  
Author(s):  
Silvia Senesi ◽  
Miklos Csala ◽  
Paola Marcolongo ◽  
Rosella Fulceri ◽  
Jozsef Mandl ◽  
...  

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.


10.5772/28641 ◽  
2011 ◽  
Author(s):  
Cidalia D. ◽  
Maria J. ◽  
Isabel Azevedo ◽  
Rosario Monteiro

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