Oligomer formation of histamine H2 receptors expressed in Sf9 and COS7 cells

FEBS Lett. 1997 Jun 9;409(2):283-6. doi: 10.1016/s0014-5793(97)00531-0.


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 alphaHA 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 coimmunoprecipitated with HA-tagged H2 receptors devoid of the 51 C-terminal amino acids, via immunoprecipitation with alphaHA 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COS Cells
  • Cloning, Molecular
  • Hemagglutinins / genetics
  • Immunoblotting
  • Molecular Weight
  • Precipitin Tests
  • Receptors, Histamine H2 / biosynthesis*
  • Receptors, Histamine H2 / chemistry*
  • Receptors, Histamine H2 / genetics
  • Spodoptera / cytology
  • Spodoptera / genetics
  • Spodoptera / metabolism


  • Hemagglutinins
  • Receptors, Histamine H2