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Oligomer formation of histamine H2 receptors expressed in Sf9 and COS7 cells 1
Author(s) -
Fukushima Yasushi,
Asano Tomoichiro,
Saitoh Toshihito,
Anai Motonobu,
Funaki Makoto,
Ogihara Takehide,
Katagiri Hideki,
Matsuhashi Nobuyuki,
Yazaki Yoshio,
Sugano Kentaro
Publication year - 1997
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(97)00531-0
Subject(s) - histamine , oligomer , receptor , sf9 , chemistry , histamine receptor , biochemistry , polymer chemistry , biology , endocrinology , recombinant dna , gene , spodoptera , antagonist
A histamine H2 receptor, which had been mutated at its glycosylation site and tagged at its N‐terminus with an HA tag (HA‐H2 receptor), was expressed in Sf9 cells and COS7 cells. Immunoprecipitation and immunoblotting of HA–H2 receptors with αHA antibody revealed four bands of 31.5±2.5 kDa, 59.0±6.0 kDa, 80.5±4.5 kDa and 120 kDa. These bands were also detected by immunoblot using anti‐H2 receptor serum (C‐terminus). In addition, H2 receptors without the HA‐tag co‐immunoprecipitated with HA‐tagged H2 receptors devoid of the 51 C‐terminal amino acids, via immunoprecipitation with αHA antibody, when the two receptors were coexpressed. These results suggest that H2 receptors are present as receptor oligomers and that the C‐terminal portion is not involved in the formation of these oligomers.