RAT SEMINAL-VESICLE PROTEIN SV-IV AND ITS TRANSGLUTAMINASE-SYNTHESIZED POLYAMINATED DERIVATIVE SPD2-SV-IV INDUCE CYTOKINE RELEASE FROM HUMAN RESTING LYMPHOCYTES AND MONOCYTES IN-VITRO

Micromolar amounts of SV-IV, one of the major proteins secreted from t he rat seminal vesicle epithelium, induce in vitro a marked release of a variety of cytokines (interferon-gamma, tumor necrosis factor-alpha , interleukin 6, and granulocyte-monocyte colony-stimulating factor) f rom human resting peripheral blood mononuclear cells as well as from i solated resting lymphocytes and monocytes, This effect was found to be significantly higher when the spermidine adduct of SV-IV (Spd(2)-SV-I V), synthesized in vitro by the enzyme trans glutaminase, was used ins tead of the native protein, Furthermore, the pretreatment of monocytes with transglutaminase caused an increase of the inducing effect of bo th native and modified SV-TV on the release of interleukin 6 from thes e cells. The inducing effect of these proteins on the cytokine release was markedly inhibited by actinomycin D and cycloheximide. (C) 1996 A cademic Press, Inc.