BFA-sensitive and insensitive exocytic pathways in Entamoeba histolytica trophozoites: their relationship to pathogenesis.
Entamoeba histolytica manifests its pathogenicity through several cellular processes triggered by external stimuli that activate signal transduction pathways. The intense secretory activity resulting from stimulation is not correlated with a typical endoplasmic reticulum (ER) or Golgi organization, and little is known in this parasite about endocytic/exocytic pathways. The interactions of trophozoites with fibronectin (FN) and cultured mammalian cells, which elicit secretory activities, were chosen to study mechanisms that regulate cytoplamic traffic. Results showed that Brefeldin A (BFA) induced redistribution of the vesicular network recognized by antibodies against amoebic proteins PDI and ERD2. Furthermore, BFA diminished traffic to the plasma membrane of the beta1 integrin-like FN receptor and the heavy subunit of the Gal/GalNAc lectin, required for adhesion to FN and target cells, respectively. However, BFA did not prevent thiol-proteinase secretion or inhibit the traffic of de novo synthesized proteinases. These data suggest that two distinct transport systems occur in E. histolytica, one similar to classical membrane protein transport and another independent of BFA and inducible by external stimuli. Actin-myosin contractility of the cortical cytoskeleton seems necessary for the final release of exported proteinases and the proper function of the surface proteins involved in adhesion.
Manning-Cela
Rebeca
R
Departamento de Biomedicina Molecular, Centro de Investigacion y de Estudios Avanzados del IPN, Apartado 14-740, Mexico, DF 07000, Mexico. rmanning@mail.cinvestav.mx
Marquez
Claudia
C
Franco
Elizabeth
E
Talamas-Rohana
Patricia
P
Meza
Isaura
I
D000199:Actins / Q000378:metabolism; D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D020126:Brefeldin A / Q000494:pharmacology*; D002448:Cell Adhesion / Q000187:drug effects; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism; D003931:Diacetyl / Q000031:analogs & derivatives* / Q000494:pharmacology; D004285:Dogs; D004748:Entamoeba histolytica / Q000187:drug effects / Q000378:metabolism* / Q000472:pathogenicity*; D005089:Exocytosis / Q000187:drug effects*; D006023:Glycoproteins / Q000378:metabolism; D039081:Integrin alpha5beta1 / Q000378:metabolism; D037102:Lectins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D021381:Protein Transport / Q000187:drug effects; D015800:Protozoan Proteins / Q000378:metabolism
D000199:Actins; D006023:Glycoproteins; D039081:Integrin alpha5beta1; D037102:Lectins; D008565:Membrane Proteins; D011500:Protein Synthesis Inhibitors; D015800:Protozoan Proteins; C004717:diacetylmonoxime; D020126:Brefeldin A; D003546:Cysteine Endopeptidases; D003931:Diacetyl