| pubmed-article:15629125 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15629125 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:15629125 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:15629125 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15629125 | lifeskim:mentions | umls-concept:C0441994 | lld:lifeskim |
| pubmed-article:15629125 | lifeskim:mentions | umls-concept:C1151067 | lld:lifeskim |
| pubmed-article:15629125 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15629125 | pubmed:dateCreated | 2005-1-4 | lld:pubmed |
| pubmed-article:15629125 | pubmed:abstractText | Peptidylglycine-alpha-amidating monooxygenase (PAM) is a copper-dependent enzyme involved in peptide posttranslational activation. Dietary Cu deficiency (Cu-) was studied to determine if lower PAM activity was due to reduction in protein or cofactor limitation. PAM activity was lower in cardiac atria of Cu- rats than Cu-adequate (Cu+) rats and there was a 50% equivalent reduction in PAM protein. No reduction in Cu- rat midbrain PAM protein was detected although PAM activity was reduced 40%. In 12-day-old (P12) mouse pups derived from dams that began Cu deficiency on day 7 of gestation, there was a parallel reduction in brain PAM activity and protein of 40-50%. PAM mRNA levels assessed in atria and brains from Cu+ and Cu- rats and mice were not altered by dietary treatment, suggesting a posttranscriptional mechanism for lower PAM protein when Cu is limiting in the cell, perhaps due to enhanced apoprotein turnover. | lld:pubmed |
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| pubmed-article:15629125 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15629125 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15629125 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15629125 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15629125 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15629125 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:15629125 | pubmed:author | pubmed-author:ProhaskaJosep... | lld:pubmed |
| pubmed-article:15629125 | pubmed:author | pubmed-author:BrokateBruceB | lld:pubmed |
| pubmed-article:15629125 | pubmed:author | pubmed-author:BroderiusMarg... | lld:pubmed |
| pubmed-article:15629125 | pubmed:author | pubmed-author:GybinaAnna... | lld:pubmed |
| pubmed-article:15629125 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15629125 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15629125 | pubmed:volume | 434 | lld:pubmed |
| pubmed-article:15629125 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15629125 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15629125 | pubmed:pagination | 212-20 | lld:pubmed |
| pubmed-article:15629125 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15629125 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15629125 | pubmed:articleTitle | Peptidylglycine-alpha-amidating monooxygenase activity and protein are lower in copper-deficient rats and suckling copper-deficient mice. | lld:pubmed |
| pubmed-article:15629125 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Minnesota Medical School Duluth, 1035 University Drive, Duluth, MN 55812, USA. jprohask@d.umn.edu | lld:pubmed |
| pubmed-article:15629125 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15629125 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15629125 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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