Heterooligomer of type 1 and type 2 inositol 1, 4, 5-trisphosphate receptor expressed in rat liver membrane fraction exists as tetrameric complex

Hitoshi Onoue, Hiroyuki Tanaka, Kiyoshi Tanaka, Naoko Doira, Yushi Ito

研究成果: ジャーナルへの寄稿記事

14 引用 (Scopus)

抄録

Functional IP3-sensitive intracellular Ca2+ release channel is considered to be a tetramer of IP3R. Heterooligomeric complexes composed of distinct types of IP3R have been reported, however, crucial evidences for them being tetramer have not appeared. Here we report that the heterooligomer composed of IP3R1 and IP3R2 also exists as tetramer. Cross-linked heterooligomer was immunoprecipitated with IP3RI-specific antibody and detected by agarose-PAGE/Western blot analysis with IP3R2-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 (IP3R1-specific) does not recognize IP3R2, therefore IP3R2 monomer itself could not have been immunoprecipitated; and (2) tetramer was the major native product of IP3R complex containing type 2 isoform in liver membrane fraction. Thus we conclude tetramer is the native form of heterooligomer composed of IP3R1 and IP3R2. (C) 2000 Academic Press.

元の言語英語
ページ(範囲)928-933
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
267
発行部数3
DOI
出版物ステータス出版済み - 1 27 2000

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Inositol 1,4,5-Trisphosphate Receptors
Liver
Rats
Monomers
Membranes
Dimers
Antibodies
Sepharose
Protein Isoforms
Western Blotting

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Heterooligomer of type 1 and type 2 inositol 1, 4, 5-trisphosphate receptor expressed in rat liver membrane fraction exists as tetrameric complex. / Onoue, Hitoshi; Tanaka, Hiroyuki; Tanaka, Kiyoshi; Doira, Naoko; Ito, Yushi.

:: Biochemical and Biophysical Research Communications, 巻 267, 番号 3, 27.01.2000, p. 928-933.

研究成果: ジャーナルへの寄稿記事

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abstract = "Functional IP3-sensitive intracellular Ca2+ release channel is considered to be a tetramer of IP3R. Heterooligomeric complexes composed of distinct types of IP3R have been reported, however, crucial evidences for them being tetramer have not appeared. Here we report that the heterooligomer composed of IP3R1 and IP3R2 also exists as tetramer. Cross-linked heterooligomer was immunoprecipitated with IP3RI-specific antibody and detected by agarose-PAGE/Western blot analysis with IP3R2-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 (IP3R1-specific) does not recognize IP3R2, therefore IP3R2 monomer itself could not have been immunoprecipitated; and (2) tetramer was the major native product of IP3R complex containing type 2 isoform in liver membrane fraction. Thus we conclude tetramer is the native form of heterooligomer composed of IP3R1 and IP3R2. (C) 2000 Academic Press.",
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AB - Functional IP3-sensitive intracellular Ca2+ release channel is considered to be a tetramer of IP3R. Heterooligomeric complexes composed of distinct types of IP3R have been reported, however, crucial evidences for them being tetramer have not appeared. Here we report that the heterooligomer composed of IP3R1 and IP3R2 also exists as tetramer. Cross-linked heterooligomer was immunoprecipitated with IP3RI-specific antibody and detected by agarose-PAGE/Western blot analysis with IP3R2-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 (IP3R1-specific) does not recognize IP3R2, therefore IP3R2 monomer itself could not have been immunoprecipitated; and (2) tetramer was the major native product of IP3R complex containing type 2 isoform in liver membrane fraction. Thus we conclude tetramer is the native form of heterooligomer composed of IP3R1 and IP3R2. (C) 2000 Academic Press.

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