Source:http://linkedlifedata.com/resource/pubmed/id/12757849
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2003-5-21
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pubmed:abstractText |
Heme oxygenase (HO) is the rate-limiting enzyme in the degradation of heme; its inducible isozyme HO-1 protects against some types of acute tissue injury. The expression and functional role of HO-1 in rats with renal injury induced by potassium dichromate (K(2)Cr(2)O(7)) was investigated in this work. Rats were studied 24 h after a single injection of K(2)Cr(2)O(7). To address the possible protective effect of HO-1 in this experimental model, this enzyme was induced by an injection of stannous chloride (SnCl(2)) 12 h before K(2)Cr(2)O(7) administration. The functional role of HO-1 in K(2)Cr(2)O(7) + SnCl(2)-treated animals was tested by inhibiting HO activity with an injection of zinc (II) protoporphyrin IX (ZnPP) 18 h before K(2)Cr(2)O(7). In K(2)Cr(2)O(7)-treated rats: (i) renal HO-1 content, measured by Western blot, increased 2.6-fold; and, (ii) renal nitrotyrosine and protein carbonyl content, markers of oxidative stress, increased 3.5- and 1.36-fold, respectively. Renal damage and oxidative stress were ameliorated and HO-1 content was increased in the K(2)Cr(2)O(7) + SnCl(2) group. The attenuation of renal injury and oxidative stress was lost by the inhibition of HO activity in K(2)Cr(2)O(7) + SnCl(2) + ZnPP-treated animals. Our data suggest that HO-1 overexpression induced by SnCl(2) is responsible for the attenuation of renal damage and oxidative stress induced by K(2)Cr(2)O(7).
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-nitrotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Caustics,
http://linkedlifedata.com/resource/pubmed/chemical/Creatinine,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Dichromate,
http://linkedlifedata.com/resource/pubmed/chemical/Protoporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Tin Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/stannous chloride,
http://linkedlifedata.com/resource/pubmed/chemical/zinc protoporphyrin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0891-5849
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1390-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12757849-Animals,
pubmed-meshheading:12757849-Blotting, Western,
pubmed-meshheading:12757849-Caustics,
pubmed-meshheading:12757849-Creatinine,
pubmed-meshheading:12757849-Enzyme Induction,
pubmed-meshheading:12757849-Heme Oxygenase (Decyclizing),
pubmed-meshheading:12757849-Heme Oxygenase-1,
pubmed-meshheading:12757849-Kidney,
pubmed-meshheading:12757849-Kidney Diseases,
pubmed-meshheading:12757849-Male,
pubmed-meshheading:12757849-Oxidative Stress,
pubmed-meshheading:12757849-Potassium Dichromate,
pubmed-meshheading:12757849-Protoporphyrins,
pubmed-meshheading:12757849-Rats,
pubmed-meshheading:12757849-Rats, Wistar,
pubmed-meshheading:12757849-Tin Compounds,
pubmed-meshheading:12757849-Tyrosine
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pubmed:year |
2003
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pubmed:articleTitle |
HO-1 induction attenuates renal damage and oxidative stress induced by K2Cr2O7.
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pubmed:affiliation |
Department of Biology, School of Chemistry, Universidad Nacional Autónoma de México, Ciudad Universitaria, 04510 Mexico City, Mexico.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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