A small molecule regulator of tissue transglutaminase conformation inhibits the malignant phenotype of cancer cells.

ABSTRACT: The protein crosslinking enzyme tissue transglutaminase (tTG) is an acyltransferase which catalyzes transamidation reactions between two proteins, or between a protein and a polyamine. It is frequently overexpressed in several different types of human cancer cells, where it has been shown to contribute to their growth, survival, and invasiveness. tTG is capable of adopting two distinct conformational states: a protein crosslinking active ("open") state, and a GTP-bound, crosslinking inactive ("closed") state. We have previously shown that the ectopic expression of mutant forms of tTG, which constitutively adopt the open conformation, are toxic to cells. This raises the possibility that strategies directed toward causing tTG to maintain an open state could potentially provide a therapeutic

SUBMITTER: Katt WP 

PROVIDER: S-EPMC6188150 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature