Interactions of Gh/transglutaminase with phospholipase Cδ1 and with GTP

被引:83
作者
Murthy, SNP
Lomasney, JW
Mak, EC
Lorand, L
机构
[1] Northwestern Univ, Sch Med, Dept Cell & Mol Biol, Chicago, IL 60611 USA
[2] Northwestern Univ, Sch Med, Dept Pathol & Mol Pharmacol, Chicago, IL 60611 USA
[3] Northwestern Univ, Sch Med, Dept Biol Chem, Chicago, IL 60611 USA
[4] Northwestern Univ, Sch Med, Feinberg Cardiovasc Res Inst, Chicago, IL 60611 USA
关键词
D O I
10.1073/pnas.96.21.11815
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 inositol phosphate hydrolyzing activity of human phospholipase C delta 1 (PLC delta 1) is markedly inhibited when the enzyme is coexpressed with the human heart G(h)/transglutaminase (TG) in human embryonic kidney cells. Because the cotransfection does not affect the amount of PLC delta 1 in the cells, the depression of phospholipase activity probably is a result of a direct interaction between the two proteins. An ELISA procedure was employed to document the associations of purified TC preparations from a variety of tissues (human red cells, rabbit lens, guinea pig liver) with PLC delta 1. Nucleotides (GTP > GDP > ATP > GMP = ADP, in order of decreasing efficiency) interfered with the formation of the PLC delta 1:TG complex, A conformational change in the TG partner, occurring with nucleotide binding, is thought to be responsible for dissociating the two proteins. The structural rearrangement produces a remarkable shift in the anodic mobility of TG in electrophoresis: TG(slow) + GTP reversible arrow [TG:GTP](fast). Altogether, our findings indicate that GTP controls PLC delta 1 activity by releasing this protein from an inhibitory association with G(h)/transglutaminase.
引用
收藏
页码:11815 / 11819
页数:5
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