PTHrP fragments 1-16 and 1-23 do not bind to either the ET sub(A) or the ET sub(B) endothelin receptors

Because of some isofunctional similarities with endothelin-1 (ET-1), it has been suggested that PTHrP(1-16) and PTHrP(1-23) could interact with osteoblast cells via ET sub(A) receptors. To document this interaction, we used the thoracic rat aorta and the guinea-pig lung parenchyma paradigms as ET su...

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Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2005-01, Vol.26 (8), p.1436-1440
Main Authors: Langlois, Chantal, Letourneau, Myriam, Turcotte, Kathy, Detheux, Michel, Fournier, Alain
Format: Article
Language:English
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Summary:Because of some isofunctional similarities with endothelin-1 (ET-1), it has been suggested that PTHrP(1-16) and PTHrP(1-23) could interact with osteoblast cells via ET sub(A) receptors. To document this interaction, we used the thoracic rat aorta and the guinea-pig lung parenchyma paradigms as ET sub(A) and ET sub(B) models, respectively. In addition, we also performed a series of competition experiments against [ super(125)I]ET-1, using transfected cells expressing the ET sub(A) or ET sub(B) receptor. So far, no agonistic nor antagonistic activities were observed in the ET sub(A) and ET sub(B) bioassays with the PTHrP fragments. Furthermore, both fragments were unable to displace [ super(125)I]ET-1 bound to cells expressing the ET sub(A) or ET sub(B) receptor.
ISSN:0196-9781
DOI:10.1016/j.peptides.2005.03.017