Abstract
Conclusion. Cationized ferritin (CF) was internalized via clathrin-mediated endocytosis. This process depends on clathrin, actin filaments, and microtubules. Microperoxidase (MPO) was internalized via a clathrin- and caveolin-independent endocytic pathway, which was partially dependent on microtubules but independent of clathrin and actin filaments. Objective. We investigated the role of actin filaments and microtubules in the transport of endocytic carrier vesicles (ECVs) from the plasma membrane to the early sorting endosomes, using CF and MPO as tracers. Materials and methods. Fifty-five guinea pigs were used. The animals were divided into a CF endocytosis group and an MPO endocytosis group. These groups consisted of control, nocodazole-treated, cytochalasin (Cyt D)-treated, Cyt D + nocodazole-treated, and geldanamycin-treated subgroups. Results. For CF endocytosis, the following results were obtained. In the nocodazole experiment, in which microtubules were disrupted to form monomeric tubulin, the number of ECVs loaded with CF was greatly decreased. In the Cyt D experiment, in which the actin filaments were disrupted to form monomers, the number of ECVs labeled with CF was also greatly decreased. In the geldanamycin experiment, in which clathrin-mediated endocytosis was regulated and actin stress fibers were dissolved, the endocytosis of CF was severely inhibited. For MPO endocytosis, in the nocodazole experiment, the endocytosis of MPO was markedly suppressed.