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Pharmacological properties of the mouse neurotensin receptor 3. Maintenance of cell surface receptor during internalization of neurotensin
Author(s) -
Navarro Valérie,
Martin Stéphane,
Sarret Philippe,
Nielsen Morten S.,
Petersen Claus M.,
Vincent Jean-Pierre,
Mazella Jean
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02367-5
Subject(s) - neurotensin , internalization , receptor , neurotensin receptor , cell surface receptor , microbiology and biotechnology , neuropeptide , 5 ht5a receptor , biology , chemistry , biochemistry
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.