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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2010-3-19
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pubmed:abstractText |
Ceruloplasmin (Cp) is a multicopper oxidase and the most abundant copper binding protein in vertebrate plasma. Loss of function mutations in humans or experimental deletion in mice result in iron overload consistent with a putative ferroxidase function. Prior work suggested plasma may contain multiple ferroxidases. Studies were conducted in Holtzman rats (Rattusnorvegicus), albino mice (Mus musculus), Cp-/- mice, and adult humans (Homo sapiens) to investigate the copper-iron interaction. Dietary copper-deficient (CuD) rats and mice were produced using a modified AIN-76A diet. Results confirmed that o-dianisidine is a better substrate than paraphenylene diamine (PPD) for assessing diamine oxidase activity of Cp. Plasma from CuD rat dams and pups, and CuD and Cp-/- mice contained no detectable Cp diamine oxidase activity. Importantly, no ferroxidase activity was detectable for CuD rats, mice, or Cp-/- mice compared to robust activity for copper-adequate (CuA) rodent controls using western membrane assay. Immunoblot protocols detected major reductions (60-90%) in Cp protein in plasma of CuD rodents but no alteration in liver mRNA levels by qRT-PCR. Data are consistent with apo-Cp being less stable than holo-Cp. Further research is needed to explain normal plasma iron in CuD mice. Reduction in Cp is a sensitive biomarker for copper deficiency.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20170749-10485908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20170749-12055353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20170749-12572662,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20170749-2231026,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20170749-98070
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1532-0456
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Print
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pubmed:volume |
151
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
473-9
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pubmed:dateRevised |
2011-7-28
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pubmed:meshHeading |
pubmed-meshheading:20170749-Amine Oxidase (Copper-Containing),
pubmed-meshheading:20170749-Animal Feed,
pubmed-meshheading:20170749-Animals,
pubmed-meshheading:20170749-Ceruloplasmin,
pubmed-meshheading:20170749-Copper,
pubmed-meshheading:20170749-Deficiency Diseases,
pubmed-meshheading:20170749-Disease Models, Animal,
pubmed-meshheading:20170749-Female,
pubmed-meshheading:20170749-Food, Formulated,
pubmed-meshheading:20170749-Gene Expression,
pubmed-meshheading:20170749-Humans,
pubmed-meshheading:20170749-Male,
pubmed-meshheading:20170749-Mice,
pubmed-meshheading:20170749-Mice, Knockout,
pubmed-meshheading:20170749-RNA, Messenger,
pubmed-meshheading:20170749-Rats,
pubmed-meshheading:20170749-Rats, Sprague-Dawley,
pubmed-meshheading:20170749-Species Specificity
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pubmed:year |
2010
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pubmed:articleTitle |
Levels of plasma ceruloplasmin protein are markedly lower following dietary copper deficiency in rodents.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Minnesota Medical School Duluth, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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