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      Involvement of Heme Oxygenase-1 in Orexin-A-induced Angiogenesis in Vascular Endothelial Cells

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          Abstract

          The cytoprotective enzyme heme oxygenase-1 (HO-1) influences endothelial cell survival, proliferation, inflammatory response, and angiogenesis in response to various angiogenic stimuli. In this study, we investigate the involvement of HO-1 in the angiogenic activity of orexin-A. We showed that orexin-A stimulates expression and activity of HO-1 in human umbilical vein endothelial cells (HUVECs). Furthermore, we showed that inhibition of HO-1 by tin (Sn) protoporphryin-IX (SnPP) reduced orexin-A-induced angiogenesis in vivo and ex vivo. Orexin-A-stimulated endothelial tube formation and chemotactic activity were also blocked in SnPP-treated vascular endothelial cells. Orexin-A treatment increased the expression of nuclear factor erythroid-derived 2 related factor 2 (Nrf2), and antioxidant response element (ARE) luciferase activity, leading to induction of HO-1. Collectively, these findings indicate that HO-1 plays a role as an important mediator of orexin-A-induced angiogenesis, and provide new possibilities for therapeutic approaches in pathophysiological conditions associated with angiogenesis.

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          Orexins and orexin receptors: a family of hypothalamic neuropeptides and G protein-coupled receptors that regulate feeding behavior.

          T Sakurai, A Amemiya, M Ishii … (1998)
          The hypothalamus plays a central role in the integrated control of feeding and energy homeostasis. We have identified two novel neuropeptides, both derived from the same precursor by proteolytic processing, that bind and activate two closely related (previously) orphan G protein-coupled receptors. These peptides, termed orexin-A and -B, have no significant structural similarities to known families of regulatory peptides. prepro-orexin mRNA and immunoreactive orexin-A are localized in neurons within and around the lateral and posterior hypothalamus in the adult rat brain. When administered centrally to rats, these peptides stimulate food consumption. prepro-orexin mRNA level is up-regulated upon fasting, suggesting a physiological role for the peptides as mediators in the central feedback mechanism that regulates feeding behavior.
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            The hypocretins: hypothalamus-specific peptides with neuroexcitatory activity.

            L de Lecea, T S Kilduff, C Peyron … (1998)
            We describe a hypothalamus-specific mRNA that encodes preprohypocretin, the putative precursor of a pair of peptides that share substantial amino acid identities with the gut hormone secretin. The hypocretin (Hcrt) protein products are restricted to neuronal cell bodies of the dorsal and lateral hypothalamic areas. The fibers of these neurons are widespread throughout the posterior hypothalamus and project to multiple targets in other areas, including brainstem and thalamus. Hcrt immunoreactivity is associated with large granular vesicles at synapses. One of the Hcrt peptides was excitatory when applied to cultured, synaptically coupled hypothalamic neurons, but not hippocampal neurons. These observations suggest that the hypocretins function within the CNS as neurotransmitters.
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              Ferritin: a cytoprotective antioxidant strategem of endothelium.

              G. Nguemba Balla, William Rosenberg, F S Apple … (1992)
              Phagocyte-mediated oxidant damage to vascular endothelium is likely involved in various vasculopathies including atherosclerosis and pulmonary leak syndromes such as adult respiratory distress syndrome. We have shown that heme, a hydrophobic iron chelate, is rapidly incorporated into endothelial cells where, after as little as 1 h, it markedly aggravates cytotoxicity engendered by polymorphonuclear leukocyte oxidants or hydrogen peroxide (H2O2). In contrast, however, if cultured endothelial cells are briefly pulsed with heme and then allowed to incubate for a prolonged period (16 h), the cells become highly resistant to oxidant-mediated injury and to the accumulation of endothelial lipid peroxidation products. This protection is associated with the induction within 4 h of mRNAs for both heme oxygenase and ferritin. After 16 h heme oxygenase and ferritin have increased approximately 50-fold and 10-fold, respectively. Differential induction of these proteins determined that ferritin is probably the ultimate cytoprotectant. Ferritin inhibits oxidant-mediated cytolysis in direct relation to its intracellular concentration. Apoferritin, when added to cultured endothelial cells, is taken up in a dose-responsive manner and appears as cytoplasmic granules by immunofluorescence; in a similar dose-responsive manner, added apoferritin protects endothelial cells from oxidant-mediated cytolysis. Conversely, a site-directed mutant of ferritin (heavy chain Glu62----Lys; His65----Gly) which lacks ferroxidase activity and is deficient in iron sequestering capacity, is completely ineffectual as a cytoprotectant. We conclude that endothelium and perhaps other cell types may be protected from oxidant damage through the iron sequestrant, ferritin.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Korean J Physiol Pharmacol
                Journal ID (iso-abbrev): Korean J. Physiol. Pharmacol
                Journal ID (publisher-id): KJPP
                Title: The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology
                Publisher: The Korean Physiological Society and The Korean Society of Pharmacology
                ISSN (Print): 1226-4512
                ISSN (Electronic): 2093-3827
                Publication date (Print): July 2015
                Publication date (Electronic): 30 June 2015
                Volume: 19
                Issue: 4
                Pages: 327-334
                Affiliations
                [1 ]Department of Oral Physiology, School of Dentistry, Pusan National University, Yangsan 626-870, Korea.
                [2 ]Department of Dental Pharmacology, School of Dentistry, Pusan National University, Yangsan 626-870, Korea.
                [3 ]Neuroprotection Research Laboratory, Department of Radiology and Neurology, Massachusetts General Hospital and Harvard Medical School, Charlestown, MA 02129, USA.
                Author notes
                Corresponding to: Moon-Kyoung Bae, Department of Oral Physiology, School of Dentistry, Pusan National University, 3-3 Beomeo-ri, Mulgeum, Yangsan 626-770, Korea. (Tel) 82-51-510-8239, (Fax) 82-51-510-8238, mkbae@ 123456pusan.ac.kr
                Article
                DOI: 10.4196/kjpp.2015.19.4.327
                PMC ID: 4499644
                PubMed ID: 26170736
                SO-VID: 9c02beef-da6c-46eb-b4ba-c04ab2f64572
                Copyright © Copyright © 2015 The Korean Physiological Society and The Korean Society of Pharmacology
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 23 January 2015
                Date revision received : 13 April 2015
                Date accepted : 23 April 2015
                Funding
                Funded by: National Research Foundation of Korea
                Award ID: 2010-0003750
                Funded by: Ministry of Health and Welfare
                Award ID: 1220080
                Categories
                Subject: Original Article

                Keywords: orexin-a,heme oxygenase-1,angiogenesis,vascular endothelial cells
                Data availability:
                Keywords: orexin-a, heme oxygenase-1, angiogenesis, vascular endothelial cells

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