Exportation of mouse vas deferens protein, a protein without a signal peptide, from mouse vas deferens epithelium: A model of apocrine secretion

Abstract

Mouse vas deferens protein (MVDP) is a major androgen-dependent protein of deferential fluid. It is specifically expressed in the epithelium of the mouse vas deferens. Its amino acid sequence as deduced from the nucleotidic sequence of its cDNA does not possess a signal sequence characteristic of secretory proteins. In vitro, transcription of MVDP cDNA followed by translation of mRNA in the rabbit reticulocyte system, in the absence or the presence of microsomes, demonstrated that there was no internalization of MVDP into microsomes that could protect it from degradation by proteinase K; this confirmed the absence of signal sequence. Moreover, MVDP has its NH2- terminus blocked. To understand how MVDP can be exported, its ultrastructural distribution and secretion process were analyzed by means of electron microscopy. Immunolocalization of MVDP revealed that it was distributed in the whole cytoplasm; it was never detected in the lumen of endoplasmic reticulum, Golgi apparatus, or vesicles but was abundant in apical protrusions and in the fluid, where it was associated with cellular material undergoing degradation. These data clearly demonstrated that exportation of MVDP into the luminal fluid does not occur in the classical manner for secretory proteins but rather involves an apocrine secretion process.