Heterooligomer of Type 1 and Type 2 Inositol 1, 4, 5-Trisphosphate Receptor Expressed in Rat Liver Membrane Fraction Exists as Tetrameric Complex
| Autor: | Hitoshi Onoue, Hiroyuki Tanaka, Naoko Doira, Kiyoshi Tanaka, Yushi Ito |
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| Rok vydání: | 2000 |
| Předmět: |
Gene isoform
Macromolecular Substances Immunoprecipitation Dimer Blotting Western Molecular Sequence Data Biophysics Receptors Cytoplasmic and Nuclear Trimer Inositol 1 4 5-Trisphosphate Biochemistry Antibodies chemistry.chemical_compound Tetramer Cerebellum Animals Humans Inositol 1 4 5-Trisphosphate Receptors Inositol Amino Acid Sequence Rats Wistar Molecular Biology Cell Membrane Cell Biology Peptide Fragments Rats Cross-Linking Reagents Monomer Liver chemistry Electrophoresis Polyacrylamide Gel Calcium Channels Protein Multimerization Intracellular |
| Zdroj: | Biochemical and Biophysical Research Communications. 267:928-933 |
| ISSN: | 0006-291X |
| Popis: | Functional IP(3)-sensitive intracellular Ca(2+) release channel is considered to be a tetramer of IP(3)R. Heterooligomeric complexes composed of distinct types of IP(3)R have been reported, however, crucial evidences for them being tetramer have not appeared. Here we report that the heterooligomer composed of IP(3)R1 and IP(3)R2 also exists as tetramer. Cross-linked heterooligomer was immunoprecipitated with IP(3)R1-specific antibody and detected by agarose-PAGE/Western blot analysis with IP(3)R2-specific antibody. Tetramer, trimer, dimer, and possibly monomer were detected. The trimer, dimer, and monomer were likely to be originated from the tetramer, since: (1) the immunoprecipitating antibody (IP(3)R1-specific) does not recognize IP(3)R2, therefore IP(3)R2 monomer itself could not have been immunoprecipitated; and (2) tetramer was the major native product of IP(3)R complex containing type 2 isoform in liver membrane fraction. Thus we conclude tetramer is the native form of heterooligomer composed of IP(3)R1 and IP(3)R2. |
| Databáze: | OpenAIRE |
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