Activation of phospholipase A2 by 1,25 (OH)2 vitamin D3 and cell growth in monocytic U937 and Mono Mac 6 cells

Cell Biochem Funct. 1995 Mar;13(1):19-23. doi: 10.1002/cbf.290130106.


Soluble phospholipase A2 activity was characterized in two human monocytic cell lines, U937 and Mono Mac 6. The enzyme showed an absolute requirement for Ca++, an alkaline pH optimum and Michaelis-Menten kinetics in both cell lines. Differentiation of U937 and Mono Mac 6 cells with 1,25 (OH)2 vitamin D3 (10 nM, 72 h) enhanced PLA2 activity by 82 per cent and 56 per cent, respectively. Furthermore, kinetic experiments revealed that enzyme activity increased within 3 h when cells were brought from the nonproliferative phase of growth to the start of a new cycle of cell proliferation. This initial activation of PLA2 could be inhibited by cycloheximide and actinomycin D, indicating the requirement of gene transcription. Taken together, these results suggest a role of cytosolic, Ca(++)-dependent PLA2 in differentiation and growth of monocytic cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcitriol / pharmacology*
  • Calcium / physiology
  • Cell Differentiation / drug effects
  • Cycloheximide / pharmacology
  • Dactinomycin / pharmacology
  • Enzyme Activation / drug effects
  • Enzyme Induction / drug effects
  • Humans
  • Hydrogen-Ion Concentration
  • Kinetics
  • Monocytes / drug effects*
  • Monocytes / enzymology
  • Phospholipases A / metabolism*
  • Phospholipases A2
  • Protein Biosynthesis / drug effects
  • Transcription, Genetic / drug effects
  • Tumor Cells, Cultured


  • Dactinomycin
  • Cycloheximide
  • Phospholipases A
  • Phospholipases A2
  • Calcitriol
  • Calcium