Expression of phosphoinositide-specific phospholipase C isoenzymes in cultured astrocytes

✍ Scribed by Vincenza Rita Lo Vasco; Cinzia Fabrizi; Marco Artico; Lucio Cocco; Anna Maria Billi; Lorenzo Fumagalli; Francesco Antonio Manzoli

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 230 KB
• Volume: 100
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.21048

✦ Synopsis

Abstract

Signal transduction from plasma membrane to cell nucleus is a complex process depending on various components including lipid signaling molecules, in particular phosphoinositides and their related enzymes, which act at cell periphery and/or plasma membrane as well as at nuclear level. As far as the nervous system may concern the inositol lipid cycle has been hypothesized to be involved in numerous neural as well as glial functions. In this context, however, a precise panel of glial PLC isoforms has not been determined yet. In the present experiments we investigated astrocytic PLC isoforms in astrocytes obtained from foetal primary cultures of rat brain and from an established cultured (C6) rat astrocytoma cell line, two well known cell models for experimental studies on glia. Identification of PLC isoforms was achieved by using a combination of RT‐PCR and immunocytochemistry experiments. While in both cell models the most represented PI‐PLC isoforms were β4, γ1, δ4, and ε, isoforms PI‐PLC β2 and δ3 were not detected. Moreover, in primary astrocyte cultures PI‐PLC δ3 resulted well expressed in C6 cells but was absent in astrocytes. Immunocytochemistry performed with antibodies against specific PLC isoforms substantially confirmed this pattern of expression both in astrocytes and C6 glioma cells. In particular while some isoenzymes (namely isoforms β3 and β4) resulted mainly nuclear, others (isoforms δ4 and ε) were preferentially localized at cytoplasmic and plasma membrane level. J. Cell. Biochem. 100: 952–959, 2007. © 2006 Wiley‐Liss, Inc.