| Enhanced neuropeptide Y synthesis during intermittent hypoxia in the rat adrenal medulla: role of reactive oxygen species-dependent alterations in precursor peptide processing. | |
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MedLine Citation:
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PMID: 20836657 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Intermittent hypoxia (IH) associated with recurrent apneas often leads to cardiovascular abnormalities. Previously, we showed that IH treatment elevates blood pressure and increases plasma catecholamines (CAs) in rats via reactive oxygen species (ROS)-dependent enhanced synthesis and secretion from the adrenal medulla (AM). Neuropeptide Y (NPY), a sympathetic neurotransmitter that colocalizes with CA in the AM, has been implicated in blood pressure regulation during persistent stress. Here, we investigated whether IH facilitates NPY synthesis in the rat AM and assessed the role of ROS signaling. IH increased NPY-like immunoreactivity in many dopamine-β-hydroxylase-expressing chromaffin cells with a parallel increase in preproNPY mRNA and protein. IH increased the activities of proNPY-processing enzymes, which were due, in part, to elevated protein expression and increased proteolytic processing. IH increased ROS generation, and antioxidants reversed IH-induced increases in ROS, preproNPY, and its processing to bioactive NPY in the AM. IH treatment increased blood pressure and antioxidants and inhibition of NPY amidation prevented this response. These findings suggest that IH-induced elevation in NPY expression in the rat AM is mediated by ROS-dependent augmentation of preproNPY mRNA expression and proNPY-processing enzyme activities and contributes to IH-induced elevation of blood pressure. |
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Authors:
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Gayatri Raghuraman; Apeksha Kalari; Rishi Dhingra; Nanduri R Prabhakar; Ganesh K Kumar |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2011-02-06 |
Journal Detail:
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Title: Antioxidants & redox signaling Volume: 14 ISSN: 1557-7716 ISO Abbreviation: Antioxid. Redox Signal. Publication Date: 2011 Apr |
Date Detail:
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Created Date: 2011-03-09 Completed Date: 2011-06-17 Revised Date: 2012-04-02 |
Medline Journal Info:
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Nlm Unique ID: 100888899 Medline TA: Antioxid Redox Signal Country: United States |
Other Details:
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Languages: eng Pagination: 1179-90 Citation Subset: IM |
Affiliation:
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The Center for Systems Biology of O2 Sensing, Department of Medicine, University of Chicago, Chicago, Illinois, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Acetylcysteine
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pharmacology Adrenal Cortex / metabolism Adrenal Medulla / cytology, metabolism* Animals Antioxidants / pharmacology Carboxypeptidase H / metabolism Cathepsin L / metabolism Cell Hypoxia Chromaffin Cells / metabolism Dopamine beta-Hydroxylase / metabolism Fatty Acids, Monounsaturated / pharmacology Male Metalloporphyrins / pharmacology Mixed Function Oxygenases / antagonists & inhibitors, metabolism Multienzyme Complexes / antagonists & inhibitors, metabolism Neuropeptide Y / genetics, metabolism* Proprotein Convertase 1 / metabolism Protein Processing, Post-Translational* Rats Rats, Sprague-Dawley Reactive Oxygen Species / metabolism* Superior Cervical Ganglion / metabolism Transcription, Genetic Up-Regulation |
| Grant Support | |
ID/Acronym/Agency:
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P01-HL-90554/HL/NHLBI NIH HHS; R01-HL-89616/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Antioxidants; 0/Fatty Acids, Monounsaturated; 0/Metalloporphyrins; 0/Mn(III) 5,10,15,20-tetrakis(N-methylpyridinium-2-yl)porphyrin; 0/Multienzyme Complexes; 0/Neuropeptide Y; 0/Reactive Oxygen Species; 2243-53-0/4-phenyl-3-butenoic acid; 616-91-1/Acetylcysteine; EC 1.-/Mixed Function Oxygenases; EC 1.14.17.1/Dopamine beta-Hydroxylase; EC 1.14.17.3/peptidylglycine monooxygenase; EC 3.4.17.10/Carboxypeptidase H; EC 3.4.21.93/Proprotein Convertase 1; EC 3.4.22.15/Cathepsin L; EC 3.4.22.15/Ctsl protein, rat |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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