Entamoeba histolytica trophozoites activated by collagen type I and Ca(2+) have a structured cytoskeleton during collagenase secretion.

A peculiar characteristic of Entamoeba histolytica trophozoites is their capacity to invade human tissues. One of the cellular determinants of invasion may include adhesion to extracellular matrix components such as collagen, induction, and secretion of electron-dense granules (EDG) and tissue digestion. The mechanism and receptors involved in this process are not well understood. Previous results suggested that cytoskeleton plays a very important role during EDG secretion. We present evidence suggesting that adhesion to collagen and activation of EDG secretion are integrin-dependent events, since beta1 subunits detected by antibodies are concentrated at membrane sites where collagen and actin were colocalized. Furthermore, the involvement of actin, vimentin, and tubulin in restructuring cytoskeleton during EDG secretion was evident, since cytoskeleton isolation was possible exclusively in activated cells. Studies of immunolocalization of tubulin, actin, and vimentin by immunofluorescence and transmission electron microscopy suggest a role for cytoskeleton in EDG secretion. Copyright 2001 Wiley-Liss, Inc.