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

FEBS Letters

Vincent, Jean-Pierre¹  Nielsen, Morten S.²  Petersen, Claus M.²  Martin, Stéphane¹  Mazella, Jean¹  Navarro, Valérie¹  Sarret, Philippe¹ 

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

[2]Department of Medical Biochemistry, University of Aarhus, 8000 Aarhus, Denmark

关键词: Neurotensin;    Receptor;    Sortilin;    Internalization;    Cloning;    NTR;    neurotensin receptor;    NT;    neurotensin;    PheAsO;    phenylarsine oxide;    CHAPS;    3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid;    CHS;    cholesteryl hemisuccinate;    RAP;    receptor-associated protein;    PAGE;    polyacrylamide gel electrophoresis;    LpL;    lipoprotein lipase;    PM;    plasma membrane;    PCR;    protein-coupled receptor;    HDM;    high density microsomes;    LDM;    low density microsomes;    Cyto;    cytosol;   

DOI  :  10.1016/S0014-5793(01)02367-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown