scholarly journals Appropriate Function of 11β-Hydroxysteroid Dehydrogenase Type 1 in the Endoplasmic Reticulum Lumen Is Dependent on Its N-terminal Region Sharing Similar Topological Determinants with 50-kDa Esterase

2004 ◽  
Vol 279 (30) ◽  
pp. 31131-31138 ◽  
Author(s):  
Christoph Frick ◽  
Atanas G. Atanasov ◽  
Peter Arnold ◽  
Juris Ozols ◽  
Alex Odermatt
Keyword(s):  
Endoplasmic Reticulum ◽  
Hydroxysteroid Dehydrogenase ◽  
Terminal Region ◽  
Endoplasmic Reticulum Lumen

Why is 11β-hydroxysteroid dehydrogenase type 1 facing the endoplasmic reticulum lumen?

2006 ◽  
Vol 248 (1-2) ◽  
pp. 15-23 ◽  
Author(s):  
Alex Odermatt ◽  
Atanas G. Atanasov ◽  
Zoltan Balazs ◽  
Roberto A.S. Schweizer ◽  
Lyubomir G. Nashev ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Hydroxysteroid Dehydrogenase ◽  
Endoplasmic Reticulum Lumen

Hexose-6-phosphate dehydrogenase in the endoplasmic reticulum

2010 ◽  
Vol 391 (1) ◽  
Author(s):  
Silvia Senesi ◽  
Miklos Csala ◽  
Paola Marcolongo ◽  
Rosella Fulceri ◽  
Jozsef Mandl ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Metabolic Syndrome ◽  
Endoplasmic Reticulum ◽  
Pentose Phosphate Pathway ◽  
Hydroxysteroid Dehydrogenase ◽  
Pyridine Nucleotide ◽  
Pentose Phosphate ◽  
The Metabolic Syndrome ◽  
Glucose 6 Phosphate Dehydrogenase

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.

scholarly journals The Glucose-6-Phosphate Transporter-Hexose-6-Phosphate Dehydrogenase-11β-Hydroxysteroid Dehydrogenase Type 1 System of the Adipose Tissue

Endocrinology ◽  
2007 ◽  
Vol 148 (5) ◽  
pp. 2487-2495 ◽  
Author(s):  
Paola Marcolongo ◽  
Simona Piccirella ◽  
Silvia Senesi ◽  
Livius Wunderlich ◽  
Isabelle Gerin ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Adipose Tissue ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Hydroxysteroid Dehydrogenase ◽  
Phosphate Transporter ◽  
Nicotinamide Adenine ◽  
Functional Connection ◽  
Pharmacological Targets ◽  
Isolated Adipocytes

11β-Hydroxysteroid dehydrogenase type 1, expressed mainly in the endoplasmic reticulum of adipocytes and hepatocytes, plays an important role in the prereceptorial activation of glucocorticoids. In liver endoplasmic reticulum-derived microsomal vesicles, nicotinamide adenine dinucleotide phosphate reduced supply to the enzyme is guaranteed by a tight functional connection with hexose-6-phosphate dehydrogenase and the glucose-6-phosphate transporter (G6PT). In adipose tissue, the proteins and their activities supporting the action of 11β-hydroxysteroid dehydrogenase type 1 have not been explored yet. Here we report the occurrence of the hexose-6-phosphate dehydrogenase in rat epididymal fat, as detected at the level of mRNA, protein, and activity. In the isolated microsomes, the activity was evident only on the permeabilization of the membrane because of the poor permeability to the cofactor nicotinamide adenine dineucleotide phosphate (NADP+), which is consistent with the intralumenal compartmentation of both the enzyme and a pool of pyridine nucleotides. In fat cells, the access of the substrate, glucose-6-phosphate to the intralumenal hexose-6-phosphate dehydrogenase appeared to be mediated by the liver-type G6PT. In fact, the G6PT expression was revealed at the level of mRNA and protein. Accordingly, the transport of glucose-6-phosphate was demonstrated in microsomal vesicles, and it was inhibited by S3483, a prototypic inhibitor of G6PT. Furthermore, isolated adipocytes produced cortisol on addition of cortisone, and the production was markedly inhibited by S3483. The results show that adipocytes are equipped with a functional G6PT-hexose-6-phosphate dehydrogenase-11β-hydroxysteroid dehydrogenase type 1 system and indicate that all three components are potential pharmacological targets for modulating local glucocorticoid activation.

The role of hepatic 11[b]-hydroxysteroid dehydrogenase type 1 in cholesterol homeostasis

2013 ◽  
pp. 1-1
Author(s):  
Kajal Manwani ◽  
Tak Y Man ◽  
Christopher J Kenyon ◽  
Ruth Andrew ◽  
Karen E Chapman ◽  
...  
Keyword(s):  
Hydroxysteroid Dehydrogenase ◽  
Cholesterol Homeostasis

Macrophage-specific 11b-hydroxysteroid dehydrogenase type 1 deficiency promotes angiogenesis but impairs resolution of K/BxN serum induced arthritis

2013 ◽  
pp. 1-1
Author(s):  
Zhenguang Zhang ◽  
Agnes Coutinho ◽  
Patrick Hadoke ◽  
Donald Salter ◽  
Jonathan Seckl ◽  
...  
Keyword(s):  
Hydroxysteroid Dehydrogenase

Suppression of 11[beta]-hydroxysteroid dehydrogenase type 1 target gene regulation by hypoxia

2016 ◽  
Author(s):  
Bushra Shammout ◽  
Adewonuola Alase ◽  
Miriam Wittmann ◽  
Paul Stewart ◽  
Ana Tiganescu
Keyword(s):  
Gene Regulation ◽  
Target Gene ◽  
Hydroxysteroid Dehydrogenase
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