Peptidases often generate bioactive peptides that regulate and mediate intercellular communication. Although processing of peptide precursors is initiated intracellularly, additional modifications by peptidases are often completed extracellularly. Plasma membrane microvesicles (MVs or microparticles) can carry membrane‐associated molecules, including proteins, when released from their parental cells. Thimet oligopeptidase (TOP) is a biologically significant peptidase that is known to be secreted to the extracellular space. Since TOP has been localized on the external face of the cell plasma membrane, we asked whether TOP might be carried by cellular MVs into the extracellular space, and whether this process is influenced by steroid hormones. DU145 androgen‐sensitive prostate cancer cells were treated with dihydrotestosterone (DHT). The cell culture supernatant was subjected to ultracentrifugation to pellet MVs. Western blot analysis of the homogenized MV sample revealed that TOP protein is, indeed, carried by the MVs of both DHT‐treated and control cells. MVs isolated from PC3 androgen‐sensitive prostate cancer cells treated with a calcium ionophore also carry TOP. Thus, our studies strongly suggest that, in addition to the soluble form, extracellular TOP also exists in MVs. This is a novel form of the extracellular peptidase that may play important pathophysiological roles.