Phospholipase C$ (PLC-& is a phospholipid-converting enzyme which, upon receptor stimulation, is activated within membrane-bound signalllng complexes. In contrast to the highly ubiquitous PLCy', PLCJ is expressed predominantly in B-lymphocytes. Associated with antigen-coupling receptors it is activated by tyrosine phosphorylation after the triggering of Bcell surface immunoglobulin. We have cloned and sequenced the human PLCJ promoter. Primer extension analysis reveals the existence of a major transcriptional start site. The TATA-less promoter contains G+C-rich stretches with a cluster of contiguous SPl consensus sites, an NFl, and an AP2 site between bp -220 to -70. A construct containing the region from -189 to +78 confers full promoter activity, as shown by fusion to a luciferase reporter gene construct. The distal part of the promoter between bp -662 to -293 containing an SRE, EBF and CACCC box contributed negatively to promoter activity in the B-cell line Raji but not in three adherent cell lines. In Raji cells, PLCJ mRNA is expressed at low levels with a half life greater than 4 h. After treatment with serum, TPA, retinoic acid, or with 5azacytidine increased levels of PLC? mRNA were induced in B-cells.