`Tissue' transglutaminase in cell death: a downstream or a multifunctional upstream effector?

FEBS Letters

Piacentini, Mauro¹  Melino, Gerry² 

[1]Department of Biology, University of Rome `Tor Vergata', 00133 Rome, Italy

[2]Biochemistry Laboratory, Istituto Dermopatico dell'Immacolata (IDI-IRCCS), Dept. Experimental Medicine (F153/D26), University of Rome `Tor Vergata', via Tor Vergata 135, 00133 Rome, Italy

关键词: Apoptosis;    Cell death;    Transglutaminase;    Protein cross-link;    Retinoblastoma protein;    Caspase;    S-Nitrosylation;    DAG;    1;    2-diacylglycerol;    PKC;    protein kinase C;    ICE;    interleukin 1β converting enzyme;    TGase;    transglutaminase;    tTG;    `tissue' TGase;    CE;    cornified envelope;    pRB;    retinoblastoma protein;    SPR;    small proline reach protein;   

DOI  :  10.1016/S0014-5793(98)00521-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Apoptotic cells show morphological modifications which occur as the result of complex molecular mechanisms involving several proteins including `tissue' transglutaminase (tTG). Although tTG was originally thought to be responsible for the protein crosslinks which prevent the leakage of intracellular components, thereby reducing inflammation and autoimmunity, recent evidence indicates that tTG is a multifunctional enzyme involved in the complex upstream regulation of the apoptotic machinery: (i) it functions as a GTP-binding protein to transduce signals; (ii) it binds/crosslinks only specific cytosolic and nuclear substrates, suggesting highly specific actions, e.g. on intermediate filaments and in cell cycle control; (iii) it is finely tuned by Ca²⁺, GTP, S-nitrosylation, polyamines. In light of these recent discoveries, the role of tTG in the regulation of the crucial balance between survival and death is clearly complex.

【 授权许可】

Unknown