%0 Journal Article
%T The controversial role of phospholipase C epsilon (PLC¦Å) in cancer development and progression
%A Anna Dubrovska
%A Anna Tyutyunnykova
%A Gennady Telegeev
%J Journal of Cancer
%D 2017
%I Ivyspring International Publisher
%R 10.7150/jca.17779
%X The phospholipase C (PLC) enzymes are important regulators of membrane phospholipid metabolism. PLC proteins can be activated by the receptor tyrosine kinases (RTK) or G-protein coupled receptors (GPCR) in response to the different extracellular stimuli including hormones and growth factors. Activated PLC enzymes hydrolyze phosphoinositides to increase the intracellular level of Ca2+ and produce diacylglycerol, which are important mediators of the intracellular signaling transduction. PLC family includes 13 isozymes belonging to 6 subfamilies according to their domain structures and functions. Although importance of PLC enzymes for key cellular functions is well established, the PLC proteins belonging to the ¦Å, ¦Æ and ¦Ç subfamilies were identified and characterized only during the last decade. As a largest known PLC protein, PLC¦Å is involved in a variety of signaling pathways and controls different cellular properties. Nevertheless, its role in carcinogenesis remains elusive.
%K Phospholipase C¦Å
%K cancer development
%K intracellular signaling
%K oncogene
%K tumor suppressor
%U http://www.jcancer.org/v08p0716.htm