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Phosphoinositide-specific phospholipase C in health and disease
Cocco, Lucio,Follo, Matilde Y.,Manzoli, Lucia,Suh, Pann-Ghill American Society for Biochemistry and Molecular Bi 2015 Journal of lipid research Vol.56 No.10
<P>Phospholipases are widely occurring and can be found in several different organisms, including bacteria, yeast, plants, animals, and viruses. Phospholipase C (PLC) is a class of phospholipases that cleaves phospholipids on the diacylglycerol (DAG) side of the phosphodiester bond producing DAGs and phosphomonoesters. Among PLCs, phosphoinositide-specific PLC (PI-PLC) constitutes an important step in the inositide signaling pathways. The structures of PI-PLC isozymes show conserved domains as well as regulatory specific domains. This is important, as most PI-PLCs share a common mechanism, but each of them has a peculiar role and can have a specific cell distribution that is linked to a specific function. More importantly, the regulation of PLC isozymes is fundamental in health and disease, as there are several PLC-dependent molecular mechanisms that are associated with the activation or inhibition of important physiopathological processes. Moreover, PI-PLC alternative splicing variants can play important roles in complex signaling networks, not only in cancer but also in other diseases. That is why PI-PLC isozymes are now considered as important molecules that are essential for better understanding the molecular mechanisms underlying both physiology and pathogenesis, and are also potential molecular targets useful for the development of innovative therapeutic strategies.</P>
PLCγ1: Potential arbitrator of cancer progression
Jang, Hyun-Jun,Suh, Pann-Ghill,Lee, Yu Jin,Shin, Kyeong Jin,Cocco, Lucio,Chae, Young Chan Elsevier 2018 Advances in biological regulation Vol.67 No.-
<P><B>Abstract</B></P> <P>Phospholipase C (PLC) is an essential mediator of cellular signaling. PLC regulates multiple cellular processes by generating bioactive molecules such as inositol-1,4,5-triphosphate (IP<SUB>3</SUB>) and diacylglycerol (DAG). These products propagate and regulate cellular signaling via calcium (Ca<SUP>2+</SUP>) mobilization and activation of protein kinase C (PKC), other kinases, and ion channels. PLCγ1, one of the primary subtypes of PLC, is directly activated by membrane receptors, including receptor tyrosine kinases (RTKs), and adhesion receptors such as integrin. PLCγ1 mediates signaling through direct interactions with other signaling molecules via SH domains, as well as its lipase activity. PLCγ1 is frequently enriched and mutated in various cancers, and is involved in the processes of tumorigenesis, including proliferation, migration, and invasion. Although many studies have suggested that PLCγ functions in cell mobility rather than proliferation in cancer, questions remain as to whether PLCγ regulates mitogenesis and whether PLCγ promotes or inhibits proliferation. Moreover, how PLCγ regulates cancer-associated cellular processes and the interplay among other proteins involved in cancer progression have yet to be fully elucidated. In this review, we discuss the current understanding of the role of PLCγ1 in cancer mobility and proliferation.</P>
Selective Activation of Nuclear PI-PLCbeta1 During Normal and Therapy-Related Differentiation
Mongiorgi, Sara,Y. Follo, Matilde,Ryoul Yang, Yong,Ratti, Stefano,Manzoli, Lucia,A. McCubrey, James,Maria Billi, Anna,Suh, Pann-Ghill,Cocco, Lucio Bentham Science 2016 CURRENT PHARMACEUTICAL DESIGN Vol.22 No.16
Inositide-dependent signaling pathways as new therapeutic targets in myelodysplastic syndromes
Mongiorgi, Sara,Finelli, Carlo,Yang, Yong Ryoul,Clissa, Cristina,McCubrey, James A.,Billi, Anna Maria,Manzoli, Lucia,Suh, Pann-Ghill,Cocco, Lucio,Follo, Matilde Y. Informa UK (Ashley Publications) 2016 Expert opinion on therapeutic targets Vol.20 No.6