| Oxidation of alpha 1-protease inhibitor: role of lipid peroxidation products. | |
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MedLine Citation:
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PMID: 2787317 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Previously we demonstrated that in vivo exposure of humans to NO2 resulted in significant inactivation of alpha 1-protease inhibitor (alpha 1-PI) in the bronchoalveolar lavage fluid. However, alpha 1-PI retains its elastase inhibitory activity in vitro when exposed to 10 times the concentration of NO2 used in vivo. We suggested exogenous oxidants such as O2 and NO2 exert their effect in vivo in part through lipid peroxidation. We investigated the mechanism of inactivation of alpha 1-PI in the presence or absence of lipids under oxidant atmosphere. alpha 1-PI in solutions containing phosphate buffer (control), 0.1 mM stearic acid (saturated fatty acid, 18:0), or 0.1 mM linoleic acid (polyunsaturated fatty acid, 18:2) was exposed to either N2 or NO2 (50 ppm for 4 h). Elastase inhibitory capacity of alpha 1-PI was significantly diminished in the presence of 0.1 mM linoleic acid and under NO2 atmosphere (75 +/- 8% of control, P less than 0.01), whereas there was no change in elastase inhibitory capacity of alpha 1-PI in the presence or absence (buffer only) of 0.1 mM stearic acid under a similar condition (109 +/- 11 and 94 +/- 6%, respectively). The inactivated alpha 1-PI as the result of peroxidized lipid could be reactivated by dithiothreitol and methionine sulfoxide peptide reductase, suggesting oxidation of methionine residue at the elastase inhibitory site. Furthermore the inhibitory effect of peroxidized lipid on alpha 1-PI could be prevented by glutathione and glutathione peroxidase and to some extent by alpha-tocopherol. |
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Authors:
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V Mohsenin; J L Gee |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of applied physiology (Bethesda, Md. : 1985) Volume: 66 ISSN: 8750-7587 ISO Abbreviation: J. Appl. Physiol. Publication Date: 1989 May |
Date Detail:
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Created Date: 1989-08-25 Completed Date: 1989-08-25 Revised Date: 2012-05-28 |
Medline Journal Info:
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Nlm Unique ID: 8502536 Medline TA: J Appl Physiol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 2211-5 Citation Subset: IM |
Affiliation:
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John B. Pierce Foundation Laboratory, Yale University School of Medicine, New Haven, Connecticut 06519. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Antioxidants
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pharmacology* Blood Proteins / metabolism* Dithiothreitol / pharmacology Humans Kinetics Linoleic Acid Linoleic Acids / pharmacology Lipid Bilayers Lipid Peroxidation* Lipid Peroxides / blood* Magnesium / pharmacology Magnesium Chloride Methionine Sulfoxide Reductases Oxidation-Reduction Oxidoreductases / metabolism Pancreatic Elastase / antagonists & inhibitors Protease Inhibitors / metabolism* Stearic Acids / pharmacology alpha 1-Antitrypsin |
| Chemical | |
Reg. No./Substance:
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0/Antioxidants; 0/Blood Proteins; 0/Linoleic Acids; 0/Lipid Bilayers; 0/Lipid Peroxides; 0/Protease Inhibitors; 0/Stearic Acids; 0/alpha 1-Antitrypsin; 2197-37-7/Linoleic Acid; 3483-12-3/Dithiothreitol; 57-11-4/stearic acid; 7439-95-4/Magnesium; 7786-30-3/Magnesium Chloride; EC 1.-/Oxidoreductases; EC 1.8.4.-/Methionine Sulfoxide Reductases; EC 1.8.4.11/methionine sulfoxide reductase; EC 3.4.21.36/Pancreatic Elastase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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