@article{oai:showa.repo.nii.ac.jp:00000737,
 author = {HAYASHI, Takahiro and OYAMADA, Hideto and YAMAZAWA, Toshiko and MURAYAMA, Takashi and MATSUOKA, Tomoyuki and OHBA, Keiichiro and NAKANO, Masahide and OGUCHI, Katsuji},
 issue = {2},
 journal = {The Showa University journal of medical sciences},
 month = {2010-06, 2019-07-26},
 note = {The ryanodine receptor type 1 (RyR1) is capable of homotetrameric assembly to form a Ca2+ release channel at intracellular Ca2+ storage sites such as endoplasmic reticulum (ER). The mRNA transcript encoding full-length RyR1 is approximately 16kb and is mainly distributed in excitable cells. A 2.4-kb mRNA splice variant from the 3'-terminal region of the RyR1 gene coexists specifically in brain together with the full-length form, although the functions of this brain-specific splice variant remain unclear. To investigate the short form of RyR1 in intracellular Ca2+ signaling in brain at the cellular level, we established an experimental system whereby the green fluorescent protein (GFP) -tagged brain-specific variant of RyR1 is coexpressed with the full-length protein in the same cell. Both forms of RyR1 were localized in the ER. Caffeine-induced Ca2+-release activities in cells expressing both the brain-specific and full-length RyR1 were reduced compared to cells expressing only the full-length form of RyR1. These results suggested that coexpression of the brain-specific splice variant of RyR1 with its full-length counterpart modulates intracellular Ca2+ signaling by acting as a dominant-negative subunit of the Ca2+ release channel in a tissue-specific fashion.},
 pages = {105--115},
 title = {The Role of a Brain-specific Splice Variant of Ryanodine Receptor Type 1},
 volume = {22},
 year = {}
}