Lectin cytochemistry was carried out on thin sections of 6th-instar cricket testis using two GalNAc-specific lectins, Dolichos biflorus agglutinin (DBA) and Helix pomatia agglutinin (HPA), and the binding sites in primary spermatocytes were surveyed. Gold particles showing DBA-binding are observed specifically in dense-body clusters. These bodies are about 100-300 nm in diameter and exhibit multilaminar or multivesicular structure. HPA can bind to the dense-body clusters and another kind of larger multivesicular structures. These bodies seem to contain some heterogeneous substances, and sometimes show an autophagosome-like structure. The ultrastructures of these organelles surveyed in conventional Epon sections confirmed the structures of these multilaminar/vesicular bodies in cricket spermatocytes, which may play certain roles in intracellular circulation and degradation of glycoconjugates.