| First Author | Sugiyama T | Year | 1999 |
| Journal | Biochem Biophys Res Commun | Volume | 265 |
| Issue | 2 | Pages | 473-8 |
| PubMed ID | 10558892 | Mgi Jnum | J:104142 |
| Mgi Id | MGI:3611276 | Doi | 10.1006/bbrc.1999.1628 |
| Citation | Sugiyama T, et al. (1999) Localization of phospholipase Cbeta isozymes in the mouse cerebellum. Biochem Biophys Res Commun 265(2):473-8 |
| abstractText | To elucidate the role of phospholipase Cbeta (PLCbeta) isozymes in the cerebellum, the distributions of PLCbeta3 and PLCbeta4 were examined in wild-type and PLCbeta4-deficient mutant mice using immunohistochemistry, and the functions were evaluated by measurement of type 1 metabotropic glutamate receptor (mGluR1)-mediated inward current and Ca(2+) mobilization. In wild-type mice, PLCbeta4 was distributed equally in both rostral and caudal cerebellum, while PLCbeta3 was enriched in the caudal versus the rostral cerebellum. In PLCbeta4-deficient mice, there was no measurable inward current or intracellular Ca(2+) 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 GTPgammaS, not caged IP(3). These results suggest that the signal transduction machinery, including receptors, G-proteins, PLCbeta3, PLCbeta4, and effectors, form a functional unit, and the deletion of PLCbeta4 alters this unit, markedly changing signal transduction efficacy. |
