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Pharmacological properties of the mouse neurotensin receptor 3. Maintenance of cell surface receptor during internalization of neurotensin.

作者信息

Navarro V, Martin S, Sarret P, Nielsen M S, Petersen C M, Vincent J, Mazella J

机构信息

Institut de Pharmacologie Moléculaire et Cellulaire, CNRS, UMR 6097, 660 route des Lucioles, 06560 Valbonne, France.

出版信息

FEBS Lett. 2001 Apr 20;495(1-2):100-5. doi: 10.1016/s0014-5793(01)02367-5.

DOI:10.1016/s0014-5793(01)02367-5
PMID:11322955
Abstract

We recently reported the molecular identification of a new type of receptor for the neuropeptide neurotensin (NT), the neurotensin receptor 3 (NTR3), identical to sortilin, which binds receptor-associated protein. Here, we demonstrate that the cloned mouse NTR3 is expressed on the plasma membrane of transfected COS-7 cells. The mouse NTR3 is detectable by photoaffinity labeling and immunoblotting at the cell surface as a 100 kDa N-glycosylated protein. Biochemical analysis and confocal microscopic imaging clearly indicate that NT is efficiently internalized after binding to NTR3, and that despite this internalization, the amount of receptor present on the cell surface is maintained.

摘要

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