Rat Seminal Vesicle Protein SV-IV and Its Transglutaminase-Synthesized Polyaminated Derivative SPD2-SV-IV Induce Cytokine Release from Human Resting Lymphocytes and Monocytesin Vitro

Abstract

Micromolar amounts of SV-IV, one of the major proteins secreted from the rat seminal vesicle epithelium, inducein vitroa marked release of a variety of cytokines (interferon-γ, tumor necrosis factor-α, interleukin 6, and granulocyte–monocyte colony-stimulating factor) from human resting peripheral blood mononuclear cells as well as from isolated resting lymphocytes and monocytes. This effect was found to be significantly higher when the spermidine adduct of SV-IV (Spd2-SV-IV), synthesizedin vitroby the enzyme transglutaminase, was used instead of the native protein. Furthermore, the pretreatment of monocytes with transglutaminase caused an increase of the inducing effect of both native and modified SV-IV on the release of interleukin 6 from these cells. The inducing effect of these proteins on the cytokine release was markedly inhibited by actinomycin D and cycloheximide.