Source:http://linkedlifedata.com/resource/pubmed/id/17805236
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2007-11-16
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pubmed:abstractText |
Carboxyl (C)-terminal fragments of parathyroid hormone (PTH) oppose the calcemic, phosphaturic, and bone-resorbing effects of active hormone. To study the action of these fragments on 1,25(OH)(2)D (1,25-dihydroxyvitamin D) synthesis, we infused parathyroidectomized rats with human or rat active 1-34 or 1-84 PTH at doses selected to produce similar calcemic responses. Human active PTH influenced neither phosphate nor 1,25(OH)(2)D concentrations. However, active 1-34 rat PTH decreased phosphate to the same level as vehicle-treated rats and increased 1,25(OH)(2)D to very high levels, whereas active 1-84 PTH decreased phosphate but maintained 1,25(OH)(2)D. As the latter effect could have been due to C-terminal fragment generation during its metabolic breakdown, we infused a mixture of rat C-terminal fragments alone or with rat 1-34. The C-terminal fragments decreased 1,25(OH)(2)D and prevented hypocalcemic-induced 1,25(OH)(2)D synthesis. When infused with active rat 1-34, they lowered the 1,25(OH)(2)D level to that seen with intact rat 1-84. The C-terminal fragments did not influence either basal or rat 1-34- or 1-84-induced CYP27B1 mRNA levels, suggesting that their inhibitory effects on 1,25(OH)(2)D synthesis appears to be post-transcriptional.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1,25-dihydroxyvitamin D,
http://linkedlifedata.com/resource/pubmed/chemical/25-Hydroxyvitamin D3...,
http://linkedlifedata.com/resource/pubmed/chemical/Parathyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin D,
http://linkedlifedata.com/resource/pubmed/chemical/carboxyl-terminal parathyroid...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0085-2538
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1330-5
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pubmed:meshHeading |
pubmed-meshheading:17805236-25-Hydroxyvitamin D3 1-alpha-Hydroxylase,
pubmed-meshheading:17805236-Animals,
pubmed-meshheading:17805236-Disease Models, Animal,
pubmed-meshheading:17805236-Humans,
pubmed-meshheading:17805236-Hypocalcemia,
pubmed-meshheading:17805236-Kidney,
pubmed-meshheading:17805236-Male,
pubmed-meshheading:17805236-Parathyroid Hormone,
pubmed-meshheading:17805236-Parathyroidectomy,
pubmed-meshheading:17805236-Peptide Fragments,
pubmed-meshheading:17805236-RNA, Messenger,
pubmed-meshheading:17805236-Rats,
pubmed-meshheading:17805236-Rats, Sprague-Dawley,
pubmed-meshheading:17805236-Vitamin D
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pubmed:year |
2007
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pubmed:articleTitle |
Parathyroid hormone fragments inhibit active hormone and hypocalcemia-induced 1,25(OH)2D synthesis.
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pubmed:affiliation |
Centre de Recherche, Centre hospitalier de l'Université de Montréal-Hôpital Saint-Luc, Montréal, Quebec, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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