CARBOXYL DOMAIN OF GLUTAMATE RECEPTOR DIRECTS ITS COUPLING TO METABOLIC PATHWAYS

被引:22
作者
GABELLINI, N [1 ]
MANEV, RM [1 ]
CANDEO, P [1 ]
FAVARON, M [1 ]
MANEV, H [1 ]
机构
[1] FIDIA RES LABS,VIA PONTE FABBRICA 3-A,I-35031 ABANO TERME,ITALY
关键词
METABOTROPIC GLUTAMATE RECEPTORS; MGLUR1; PHOSPHOINOSITIDE HYDROLYSIS; CAMP; FORSKOLIN; G-PROTEIN; PERTUSSIS TOXIN;
D O I
10.1097/00001756-199305000-00017
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
OF the six metabotropic glutamate receptors (mGluRs) only mGluR1 and mGluR5, which possess a large carboxyl terminal domain, are positively linked to phosphoinositide (PI) hydrolysis. We expressed a 3' deletion of mGluR1alpha (mGluR1T) lacking the terminal 290 codons and the full length mGluR1alpha cDNAs in human embryonic kidney 293 cells. Agonist stimulation of both mGluR1alpha and mGluR1T stimulated PI hydrolysis. Glutamate activation of PI hydrolysis was reduced by pertussis toxin when mediated via mGluR1alpha, while mGluR1T required the presence of extracellular Ca2+. Glutamate-mediated reduction of adenylyl cyclase stimulation by forskolin occurred only in mGluR1T-expressing cells. The results suggest that the carboxyl terminal extension directs the coupling of mGluR1 with different signal transduction pathways.
引用
收藏
页码:531 / 534
页数:4
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