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Updated: Aug 18, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Carboxyl terminal sequence of human phospholipase Cgamma2
F Ozdener1, S P Kunapuli, J L Daniel
1Department of Pharmacology, Temple University School of Medicine, Philadelphia, PA 19140, USA. fozdener@astro.temple.edu
Abstract:
Phospholipase Cgamma2 (PLCgamma2), the predominant isoform of phospholipase C expressed in platelets, plays a major role in activation of platelets by collagen. Although PLCgamma2 has been shown to be tyrosine phosphorylated upon collagen-induced activation, the phosphorylation sites are yet to be determined. We have sequenced the 3' terminal cDNA of human phospholipase C-gamma-2 and found it different from the human PLCgamma2 cDNA sequence previously reported by Ohta et al. (Ohta S, Matsui A, Nazawa Y, Kagawa Y. FEBS Lett 1988; 242: 31-5). There is an extra guanosine at position 3723 which causes a shift in the reading frame. The new carboxyl terminal amino acid (aa) sequence beyond the frame shift is 88% identical to that of rat (21 out of 24 aa residues) which is considerably higher than the identity with published sequence (26% identity). The new deduced aa sequence contains two tyrosine residues at positions 1245 and 1264 which might be phosphorylated upon stimulation and hence might be important for the activation of the PLCgamma2.
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