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Updated: Aug 8, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
Published on: July 28, 2014
Impaired antigen receptor induced calcium mobilization in a phospholipase C-gamma1 deficient B cell line
Natarajan Muthusamy1, Do Joon Park, Hei-Won Rho
1Center for Molecular and Human Genetics, The Department of Pediatrics, Columbus Children's Research Institute, The Ohio State University Columbus, OH 43205, USA. rmuthusa@chi.osu.edu
Abstract:
B lymphocytes express phospholipase C-gamma(1) (PLC-gamma(1)) and phospholipase C-gamma(2) (PLC-gamma(2)) isozymes. However, the relative importance of these two isozymes in B cell signaling is not known. We report here the identification and analysis of a B cell line deficient in PLC-gamma(1). Mature splenic B lymphocytes and a panel of cell lines representing pre-B, immature and mature B cell stages expressed phospholipase C-gamma (PLC-gamma), but not the beta or delta isoforms of phospholipase C (PLC). While all the tested B cell lines and primary splenic B cells expressed PLC-gamma(1) and PLC-gamma(2) isozymes, the L1.2 B cell line exclusively expressed PLC-gamma(2), but not PLC-gamma(1) isozyme. The PLC-gamma(1) deficient L1.2 B cells expressed levels of surface IgM comparable to that of PLC-gamma(1) positive 70Z/3 B cell line. However, stimulation through the antigen receptor induced Ca(++) response in 70Z/3, but not L1.2 B cells, suggesting a requirement for PLC-gamma(1) in antigen receptor induced Ca(++) signaling in these cells. The possible use for L1.2 cells in testing the regulation of PLC-gamma(1) and PLC-gamma(2) dependent calcium mobilization in B lymphocytes is discussed.
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