Localization of phospholipase Cβ isozymes in the mouse cerebellum

被引:31
作者
Sugiyama, T
Hirono, M
Suzuki, K
Nakamura, Y
Aiba, A
Nakamura, K
Nakao, K
Katsuki, M
Yoshioka, T
机构
[1] Waseda Univ, Sch Human Sci, Dept Mol Neurobiol, Tokorozawa, Saitama 3591192, Japan
[2] Waseda Univ, Adv Res Inst Res & Engn, Shinjuku Ku, Tokyo 1698555, Japan
[3] Univ Tokyo, Inst Med Sci, Res Ctr Anim Models Human Dis, Dept DNA Biol & Embryo Engn,Minato Ku, Tokyo 1088639, Japan
基金
日本学术振兴会;
关键词
D O I
10.1006/bbrc.1999.1628
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
To elucidate the role of phospholipase C beta (PLC beta) isozymes in the cerebellum, the distributions of PLC beta 3 and PLC beta 4 were examined in wild-type and PLC beta 4-deficient mutant mice using immunohistochemistry, and the functions were evaluated by measurement of type 1 metabotropic glutamate receptor (mGluR1)-mediated inward current and Ca2+ mobilization, In wild-type mice, PLC beta 4 was distributed equally in both rostral and caudal cerebellum, while PLC beta 3 was enriched in the caudal versus the rostral cerebellum. In PLC beta 4-deficient mice, there was no measurable inward current or intracellular Ca2+ elevation in the rostral cerebellum, whereas small responses were observed in the caudal cerebellum. In wild-type mice, the inward current was observed only following the release of caged GTP gamma S, not caged IP3. These results suggest that the signal transduction machinery, including receptors, G-proteins, PLC beta 3, PLC beta 4, and effecters, form a functional unit, and the deletion of PLC beta 4 alters this unit, markedly changing signal transduction efficacy. (C) 1999 Academic Press.
引用
收藏
页码:473 / 478
页数:6
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