Literature DB >> 34800278

Heme Oxygenase 1 in Vertebrates: Friend and Foe.

Rafael Cardoso Maciel Costa Silva1, Leonardo Holanda Travassos Correa2.   

Abstract

HO-1 is the inducible form of the enzyme heme-oxygenase. HO-1 catalyzes heme breakdown, reducing the levels of this important oxidant molecule and generating antioxidant, anti-inflammatory, and anti-apoptotic byproducts. Thus, HO-1 has been described as an important stress response mechanism during both physiologic and pathological processes. Interestingly, some findings are demonstrating that uncontrolled levels of HO-1 byproducts can be associated with cell death and tissue destruction as well. Furthermore, HO-1 can be located in the nucleus, influencing gene transcription, cellular proliferation, and DNA repair. Here, we will discuss several studies that approach HO-1 effects as a protective or detrimental mechanism in different pathological conditions. In this sense, as the major organs of vertebrates will deal specifically with distinct types of stresses, we discuss the HO-1 role in each of them, exposing the contradictions associated with HO-1 expression after different insults and circumstances.
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Brain; Gastrointestinal system; Heme-oxygenase; Kidneys; Liver; Lungs; Reproductive tract; Skin; Stress response

Mesh:

Substances:

Year:  2021        PMID: 34800278     DOI: 10.1007/s12013-021-01047-z

Source DB:  PubMed          Journal:  Cell Biochem Biophys        ISSN: 1085-9195            Impact factor:   2.194


  116 in total

Review 1.  The heme oxygenase system: a regulator of second messenger gases.

Authors:  M D Maines
Journal:  Annu Rev Pharmacol Toxicol       Date:  1997       Impact factor: 13.820

2.  Heme biosynthesis is coupled to electron transport chains for energy generation.

Authors:  Kalle Möbius; Rodrigo Arias-Cartin; Daniela Breckau; Anna-Lena Hännig; Katrin Riedmann; Rebekka Biedendieck; Susanne Schröder; Dörte Becher; Axel Magalon; Jürgen Moser; Martina Jahn; Dieter Jahn
Journal:  Proc Natl Acad Sci U S A       Date:  2010-05-19       Impact factor: 11.205

3.  The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase.

Authors:  R Tenhunen; H S Marver; R Schmid
Journal:  Proc Natl Acad Sci U S A       Date:  1968-10       Impact factor: 11.205

4.  Nitric oxide activation of peroxisome proliferator-activated receptor gamma through a p38 MAPK signaling pathway.

Authors:  Anetta Ptasinska; Shuibang Wang; Jianhua Zhang; Robert A Wesley; Robert L Danner
Journal:  FASEB J       Date:  2006-12-28       Impact factor: 5.191

5.  The Arabidopsis HY2 gene encodes phytochromobilin synthase, a ferredoxin-dependent biliverdin reductase.

Authors:  T Kohchi; K Mukougawa; N Frankenberg; M Masuda; A Yokota; J C Lagarias
Journal:  Plant Cell       Date:  2001-02       Impact factor: 11.277

6.  A role for oxygen radicals as second messengers.

Authors:  R Schreck; P A Baeuerle
Journal:  Trends Cell Biol       Date:  1991-08       Impact factor: 20.808

7.  Hemoprotein Bach1 regulates enhancer availability of heme oxygenase-1 gene.

Authors:  Jiying Sun; Hideto Hoshino; Kazuaki Takaku; Osamu Nakajima; Akihiko Muto; Hiroshi Suzuki; Satoshi Tashiro; Satoru Takahashi; Shigeki Shibahara; Jawed Alam; Makoto M Taketo; Masayuki Yamamoto; Kazuhiko Igarashi
Journal:  EMBO J       Date:  2002-10-01       Impact factor: 11.598

Review 8.  Transcriptional regulation of the heme oxygenase-1 gene via the stress response element pathway.

Authors:  J Alam; J L Cook
Journal:  Curr Pharm Des       Date:  2003       Impact factor: 3.116

Review 9.  The non-canonical functions of the heme oxygenases.

Authors:  Luca Vanella; Ignazio Barbagallo; Daniele Tibullo; Stefano Forte; Agata Zappalà; Giovanni Li Volti
Journal:  Oncotarget       Date:  2016-10-18
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