NUCLEAR-LOCALIZATION AND SIGNALING ACTIVITY OF PHOSPHOINOSITIDASE-C-BETA IN SWISS 3T3 CELLS

被引:327
作者
MARTELLI, AM
GILMOUR, RS
BERTAGNOLO, V
NERI, LM
MANZOLI, L
COCCO, L
机构
[1] UNIV BOLOGNA, INST HUMAN ANAT, V IRNERIO 48, I-40126 BOLOGNA, ITALY
[2] UNIV FERRARA, INST HUMAN ANAT, I-44100 FERRARA, ITALY
[3] UNIV CHIETI, INST HUMAN ANAT, CHIETI, ITALY
[4] IST RIZZOLI, CNR, INST CYTOMORPHOL, I-40136 BOLOGNA, ITALY
[5] AFRC, INST ANIM PHYSIOL & GENET RES, CAMBRIDGE CB2 4AT, ENGLAND
关键词
D O I
10.1038/358242a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
THE hydrolysis of phosphatidylinositol 4,5-bisphosphate (PtdInsP2) is a widespread receptor-coupled signalling system at the plasma membrane of most eukaryotic cells. The existence of an entirely separate nuclear phosphoinositide signalling system is suggested from evidence that purified nuclei synthesize PtdInsP2 and phosphatidylinositol 4-phosphate (PtdInsP) in vitro1 and that a transient decrease in the mass of these lipids occurs when Swiss 3T3 cells are cultured in the presence of insulin-like growth factor-1 (IGF-1)2-4. These IGF-1-dependent changes in inositol lipids coincide with an increase in nuclear diacylglycerol4 and precede translocation to the nucleus and activation of protein kinase C (refs 5, 6). Circumstantial evidence that links these changes with mitosis comes from the isolation of a 3T3 clone that expresses the type-1 IGF receptor and binds IGF-1 peptide but does not respond mitogenically or show transient mass changes in nuclear inositol lipids7. A key question is how IGF-1 initiates the rapid breakdown of PtdInsP and PtdInsP2 in the nucleus. Here we present evidence that nuclei of 3T3 cells contain the beta-isozyme of phosphoinositidase C, whereas the gamma-isozyme is confined to the cytoplasm and that IGF-1 treatment stimulates exclusively the activity of nuclear phosphoinositidase C.
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页码:242 / 245
页数:4
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