Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1994-10-24
|
pubmed:abstractText |
Parathyroid hormone (PTH) exerts its biological action by binding to membrane-bound, G-protein coupled receptors expressed predominantly in bone and kidney. In this study, we describe the production and characterization of a panel of cell lines, derived from a human embryonic kidney cell line (HEK-293), each of which stably express different amounts of the recombinant human PTH/parathyroid hormone-related protein (PTHrP) receptor (Rc). A total of 52 distinct clones displaying different levels of PTH-responsive cAMP production were analyzed; three clones were chosen for more detailed evaluation. These clones (and the receptor-lacking parental cell line) were examined for PTH binding, PTH-stimulated cyclic AMP accumulation and PTH/PTHrP Rc mRNA expression. Receptor-positive clones display a spectrum of PTH-responsiveness that correlates with receptor number/cell and level of receptor mRNA present. The interaction of a C-terminal hPTH-(52-84) peptide with the stably expressed human receptor was examined in cells expressing the highest amount of Rc (> 400,000 Rc/cell). There was no direct binding of hPTH-(52-84) or specific competition versus radiolabeled PTH-(1-34). However, competition versus radiolabeled PTH-(1-34) was observed with bPTH-(1-34), hPTH-(1-84) and hPTHrP-(1-34). These data suggest that hPTH-(52-84) does not interact with the only known form of the human PTH/PTHrP Rc. Therefore, the reported effects of PTH-(52-84) in other systems must be via an alternate (as yet unidentified) mechanism(s). The expression of various amounts of the human PTH/PTHrP Rc in a human target cell background should facilitate characterization of the ligand-binding properties and physiological signal transduction mechanism of the Rc.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
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/Receptor, Parathyroid Hormone...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Parathyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Teriparatide,
http://linkedlifedata.com/resource/pubmed/chemical/parathyroid hormone (53-84)
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0013-7227
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
135
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1713-6
|
pubmed:dateRevised |
2004-11-17
|
pubmed:meshHeading |
pubmed-meshheading:7925136-Cell Line,
pubmed-meshheading:7925136-Cyclic AMP,
pubmed-meshheading:7925136-DNA,
pubmed-meshheading:7925136-Humans,
pubmed-meshheading:7925136-Kidney,
pubmed-meshheading:7925136-Parathyroid Hormone,
pubmed-meshheading:7925136-Peptide Fragments,
pubmed-meshheading:7925136-RNA, Messenger,
pubmed-meshheading:7925136-Receptor, Parathyroid Hormone, Type 1,
pubmed-meshheading:7925136-Receptors, Parathyroid Hormone,
pubmed-meshheading:7925136-Recombinant Proteins,
pubmed-meshheading:7925136-Signal Transduction,
pubmed-meshheading:7925136-Teriparatide
|
pubmed:year |
1994
|
pubmed:articleTitle |
Generation and characterization of human kidney cell lines stably expressing recombinant human PTH/PTHrP receptor: lack of interaction with a C-terminal human PTH peptide.
|
pubmed:affiliation |
Thorndike and Dana Laboratories, Department of Medicine, Beth Israel Hospital, Boston, MA 02215.
|
pubmed:publicationType |
Journal Article
|