Endoplasmic reticulum: a metabolic compartment |
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Authors: | Csala Miklós Bánhegyi Gábor Benedetti Angelo |
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Affiliation: | Department of Medical Chemistry, Semmelweis University and Endoplasmic Reticulum Research Group of the Hungarian Academy of Sciences, 1444 Budapest, Hungary. |
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Abstract: | Several biochemical reactions and processes of cell biology are compartmentalized in the endoplasmic reticulum (ER). The view that the ER membrane is basically a scaffold for ER proteins, which is permeable to small molecules, is inconsistent with recent findings. The luminal micro-environment is characteristically different from the cytosol; its protein and glutathione thiols are remarkably more oxidized, and it contains a separate pyridine nucleotide pool. The substrate specificity and activity of certain luminal enzymes are dependent on selective transport of possible substrates and co-factors from the cytosol. Abundant biochemical, pharmacological, clinical and genetic data indicate that the barrier function of the lipid bilayer and specific transport activities in the membrane make the ER a separate metabolic compartment. |
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Keywords: | ER, endoplasmic reticulum GSH, glutathione GSSG, glutathione disulfide GSD 1, glycogen storage disease type 1 CRD, cortisone reductase deficiency G6P, glucose-6-phosphate G6Pase, glucose-6-phosphatase G6PT, glucose-6-phosphate transporter H6PDH, hexose-6-phosphate dehydrogenase 11βHSDH1, 11β-hydroxysteroid dehydrogenase type 1 MHC, major histocompatibility complex RER, rough endoplasmic reticulum TAP, transporter associated with antigen processing UGA, UDP-glucuronic acid UGT, UDP-glucuronosyltransferase |
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