甲状旁腺激素相关蛋白片段1 - 16和1 - 23既不与内皮素A受体也不与内皮素B受体结合。

PTHrP fragments 1-16 and 1-23 do not bind to either the ETA or the ETB endothelin receptors.

作者信息

Langlois Chantal, Létourneau Myriam, Turcotte Kathy, Detheux Michel, Fournier Alain

机构信息

Institut National de la Recherche Scientifique - Institut Armand-Frappier, Université du Québec, 245 boul. Hymus, Pointe-Claire (Montréal), QC, Canada H9R 1G6.

出版信息

Peptides. 2005 Aug;26(8):1436-40. doi: 10.1016/j.peptides.2005.03.017. Epub 2005 Apr 20.

DOI:10.1016/j.peptides.2005.03.017

PMID:16042983

Abstract

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 ETA receptors. To document this interaction, we used the thoracic rat aorta and the guinea-pig lung parenchyma paradigms as ETA and ETB models, respectively. In addition, we also performed a series of competition experiments against [125I]ET-1, using transfected cells expressing the ETA or ETB receptor. So far, no agonistic nor antagonistic activities were observed in the ETA and ETB bioassays with the PTHrP fragments. Furthermore, both fragments were unable to displace [125I]ET-1 bound to cells expressing the ETA or ETB receptor.

摘要

由于与内皮素 -1（ET-1）存在一些同功功能相似性，有人提出甲状旁腺激素相关蛋白（PTHrP）（1-16）和PTHrP（1-23）可能通过ETA受体与成骨细胞相互作用。为了证明这种相互作用，我们分别使用大鼠胸主动脉和豚鼠肺实质作为ETA和ETB模型。此外，我们还使用表达ETA或ETB受体的转染细胞，针对[125I]ET-1进行了一系列竞争实验。到目前为止，在使用PTHrP片段进行的ETA和ETB生物测定中，未观察到激动或拮抗活性。此外，这两个片段均无法取代与表达ETA或ETB受体的细胞结合的[125I]ET-1。