For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
15
views
21
references
 Top references
cited by
4
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      253
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: not found

      Effect of N-acetyl-cysteine on the hypoxic ventilatory response and erythropoietin production: linkage between plasma thiol redox state and O2 chemosensitivity

      Author(s): 1 , 1 , 1 , 1
      Publication date Created:
      Publication date (Print):
      Journal: Blood
      Publisher: American Society of Hematology

      Read this article at

      ScienceOpenPublisher
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Oxygen-sensing chemoreceptors contribute significantly to the regulation of the respiratory drive and arterial PO2levels. The hypoxic ventilatory response (HVR) decreases strongly with age and is modulated by prolonged hypoxia and physical exercise. Several earlier studies indicated that the regulation of the ventilatory response and erythropoietin (EPO) production by the respective oxygen sensors involves redox-sensitive signaling pathways, which are triggered by the O2-dependent production of reactive oxygen species. The hypothesis that HVR and EPO production are modulated by thiol compounds or changes in the plasma thiol–disulfide redox state (REDST) was investigated. It was demonstrated that both responses are enhanced by oral treatment with N-acetyl-cysteine (NAC) and that HVR is correlated with plasma thiol level and REDST. Results suggest the possibility that age-related changes in plasma REDST may account for the age-related changes in HVR.

          Related collections

          Most cited references21

          • Record: found
          • Abstract: found
          • Article: not found

          HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing.

          M Ivan, K Kondo, H. Yang … (2001)
          HIF (hypoxia-inducible factor) is a transcription factor that plays a pivotal role in cellular adaptation to changes in oxygen availability. In the presence of oxygen, HIF is targeted for destruction by an E3 ubiquitin ligase containing the von Hippel-Lindau tumor suppressor protein (pVHL). We found that human pVHL binds to a short HIF-derived peptide when a conserved proline residue at the core of this peptide is hydroxylated. Because proline hydroxylation requires molecular oxygen and Fe(2+), this protein modification may play a key role in mammalian oxygen sensing.
          Article 0 comments Cited 1075 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Oxygen sensing and molecular adaptation to hypoxia.

            H Bunn, Robert O Poyton (1996)
            This review focuses on the molecular stratagems utilized by bacteria, yeast, and mammals in their adaptation to hypoxia. Among this broad range of organisms, changes in oxygen tension appear to be sensed by heme proteins, with subsequent transfer of electrons along a signal transduction pathway which may depend on reactive oxygen species. These heme-based sensors are generally two-domain proteins. Some are hemokinases, while others are flavohemoproteins [flavohemoglobins and NAD(P)H oxidases]. Hypoxia-dependent kinase activation of transcription factors in nitrogen-fixing bacteria bears a striking analogy to the phosphorylation of hypoxia inducible factor-1 (HIF-1) in mammalian cells. Moreover, redox chemistry appears to play a critical role both in the trans-activation of oxygen-responsive genes in unicellular organisms as well as in the activation of HIF-1. In yeast and bacteria, regulatory operons coordinate expression of genes responsible for adaptive responses to hypoxia and hyperoxia. Similarly, in mammals, combinatorial interactions of HIF-1 with other identified transcription factors are required for the hypoxic induction of physiologically important genes.
            Article 0 comments Cited 105 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              S-nitrosothiols signal the ventilatory response to hypoxia.

              Eric Johnson, B Gastón, Paul Lieberman … (2001)
              Increased ventilation in response to hypoxia has been appreciated for over a century, but the biochemistry underlying this response remains poorly understood. Here we define a pathway in which increased minute ventilation (&Vdot;E ) is signalled by deoxyhaemoglobin-derived S-nitrosothiols (SNOs). Specifically, we demonstrate that S-nitrosocysteinyl glycine (CGSNO) and S-nitroso-l-cysteine (l-CSNO)-but not S-nitroso-d-cysteine (d-CSNO)-reproduce the ventilatory effects of hypoxia at the level of the nucleus tractus solitarius (NTS). We show that plasma from deoxygenated, but not from oxygenated, blood produces the ventilatory effect of both SNOs and hypoxia. Further, this activity is mediated by S-nitrosoglutathione (GSNO), and GSNO activation by gamma-glutamyl transpeptidase (gamma-GT) is required. The normal response to hypoxia is impaired in a knockout mouse lacking gamma-GT. These observations suggest that S-nitrosothiol biochemistry is of central importance to the regulation of breathing.
              Article 0 comments Cited 48 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Title: Blood
                Publisher: American Society of Hematology
                ISSN (Electronic): 1528-0020
                ISSN (Print): 0006-4971
                Publication date Created: March 01 2002
                Publication date (Print): March 01 2002
                Volume: 99
                Issue: 5
                Pages: 1552-1555
                Affiliations
                [1 ] From the Department of Immunochemistry, Deutsches Krebsforschungszentrum, Heidelberg; and the Department of Sports Medicine, University of Heidelberg, Germany.
                Article
                DOI: 10.1182/blood.V99.5.1552
                SO-VID: c787b091-c373-4d8a-9d9d-a7da267284a8
                Copyright © © 2002
                History

                Data availability:

                Comments

                Comment on this article

                scite_

                Similar content253

                See all similar

                Cited by3

                See all cited by

                Most referenced authors625

                See all reference authors