Mukhopadhyay N K, Saha A K, Smith W, Dowling J N, Hiserodt J, Glew R H
Department of Microbiology, University of Pittsburgh, School of Medicine, PA 15261.
Clin Chim Acta. 1989 Jun 15;182(1):31-40. doi: 10.1016/0009-8981(89)90147-2.
The major acid phosphatase of human seminal fluid was purified to homogeneity by chromatography on Sephadex G-150, and DEAE-Sephadex, and by isoelectric focusing (pI, 4.3). This purified preparation of seminal fluid acid phosphatase blocked superoxide anion production by neutrophils stimulated with fMet-Leu-Phe (fMLP) by 50%. The phosphatase also hydrolysed myo-inositol 1,4,5-trisphosphate (IP3) in vitro, an intracellular second messenger which releases Ca2+ from intracellular pools, at nearly one-third the rate at which the nonphysiologic substrate 4-methylumbelliferylphosphate (MUP) was cleaved. In contrast, two phosphoinositide lipids, namely phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 4-monophosphate, were poor phosphatase substrates. Following fMLP stimulation of [3H]inositol-labeled neutrophils, the quantity of IP3 produced by phosphatase-treated cells was reduced by 69%. These results indicate that the human seminal fluid acid phosphatase may compromise the neutrophil's microbicidal response to the organism by hydrolyzing a second messenger (IP3) which is directly involved in the regulation of intracellular Ca2+ concentrations. The seminal fluid phosphatase also inhibited by 85% the ability of murine natural killer (NK) cells to inactivate target cells.
