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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6 Pt 2
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pubmed:dateCreated |
1992-8-4
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pubmed:abstractText |
The signal transduction pathways of the recently cloned porcine kidney calcitonin (CT) receptor were evaluated. This receptor, when stably transfected into MC-3T3 cells, avidly bound salmon CT (SCT) [dissociation constant (Kd) = 4 nM]. Incubation with SCT resulted in a dose-dependent accumulation of adenosine 3',5'-cyclic monophosphate (cAMP) [50% effective concentration (EC50) = 0.02 nM] in transfected cells (referred to as PC-1 cells). Binding kinetics and cAMP dose response relationships were similar to those of the native receptor in LLC-PK1 cells. PC-1 cells also responded to calcitonin gene-related peptide (CGRP), but the EC50 value for cAMP accumulation was more than three orders of magnitude higher than for SCT. Exposure of PC-1 cells to SCT (5 nM to 1 microM) produced a dose-dependent rise in cytosolic free Ca2+ concentration ([Ca2+]i), whereas CGRP did not. The initial rise in [Ca2+]i was not dependent on extracellular Ca2+, suggesting that SCT induced release of Ca2+ from intracellular stores. SCT also increased inositol trisphosphate production in PC-1 cells. In conclusion, the cloned, transfected porcine CT receptor functionally couples to and activates both adenylyl cyclase and phospholipase C. This dual coupling is also a characteristic of the parathyroid hormone receptor, which has significant homology in amino acid sequence with the CT receptor.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcitonin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitonin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
F1110-5
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1320332-Adenylate Cyclase,
pubmed-meshheading:1320332-Animals,
pubmed-meshheading:1320332-Calcitonin,
pubmed-meshheading:1320332-Calcium,
pubmed-meshheading:1320332-Cell Line,
pubmed-meshheading:1320332-Cloning, Molecular,
pubmed-meshheading:1320332-Culture Media,
pubmed-meshheading:1320332-Kidney,
pubmed-meshheading:1320332-Osmolar Concentration,
pubmed-meshheading:1320332-Receptors, Calcitonin,
pubmed-meshheading:1320332-Receptors, Cell Surface,
pubmed-meshheading:1320332-Salmon,
pubmed-meshheading:1320332-Signal Transduction,
pubmed-meshheading:1320332-Swine,
pubmed-meshheading:1320332-Type C Phospholipases
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pubmed:year |
1992
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pubmed:articleTitle |
A cloned porcine renal calcitonin receptor couples to adenylyl cyclase and phospholipase C.
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pubmed:affiliation |
Arthritis Unit, Massachusetts General Hospital, Boston 02114.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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