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      Heme oxygenase-1 comes back to endoplasmic reticulum.

      Biochemical and Biophysical Research Communications
      Animals, Endoplasmic Reticulum, enzymology, Heme Oxygenase-1, genetics, metabolism, Humans, Mice, Organelles, Stress, Physiological, Unfolded Protein Response

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          Abstract

          Originally identified as a rate-limiting enzyme for heme catabolism, heme oxygenase-1 (HO-1) has expanded its roles in anti-inflammation, anti-apoptosis and anti-proliferation for the last decade. Regulation of protein activity by location is well appreciated. Even though multiple compartmentalization of HO-1 has been documented, the functional implication of this enzyme at these subcellular organelles is only partially elucidated. In this review we discuss the endoplasmic reticulum (ER)-residing HO-1 and its cytoprotective activity against ER stress. Copyright © 2010 Elsevier Inc. All rights reserved.

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          Author and article information

          Journal
          21094129
          10.1016/j.bbrc.2010.11.067

          Chemistry
          Animals,Endoplasmic Reticulum,enzymology,Heme Oxygenase-1,genetics,metabolism,Humans,Mice,Organelles,Stress, Physiological,Unfolded Protein Response

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