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- W1485472521 abstract "Publisher Summary One of the most interesting biochemical features of TGase-2 is the fact that it shares sites for GTP-binding/GTP hydrolysis and acyl transferase activities on the same polypeptide chain. This chapter shows how the binding of guanine nucleotides to the rat TGase-2 negatively impacts its transamidation activity. A potentially important regulatory feature exhibited by TGase-2 is its responsiveness to Ca 2+ . The increased TGase-2 transamidation activity associated with some human cancer cells can contribute to oncogenesis by promoting drug-resistance. The study reviews many important questions surrounding the function of TGase-2 that are aimed at understanding the functional significance of its GTP-binding/GTP-hydrolytic cycle. There have been a number of suggestions that TGase-2 functions as a signal transducer, mediating the stimulation of phospholipase C activity by the α1-adrenergic receptor, as well as by the oxytocin and thrombaxin receptors. These shed important new light on the growth and survival of cells, and how these processes go awry during the development of the malignant state." @default.
- W1485472521 created "2016-06-24" @default.
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- W1485472521 date "2003-01-01" @default.
- W1485472521 modified "2023-09-26" @default.
- W1485472521 title "Tissue Transglutaminase: A Unique GTP-Binding/GTPase" @default.
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