Literature DB >> 8674132

Characterization of adhesion plates induced by the interaction of Entamoeba histolytica trophozoites with fibronectin.

J Vázquez1, E Franco, G Reyes, I Meza.   

Abstract

Entamoeba histolytica trophozoites are pleiomorphic and highly motile cells. Although scarce fibrous material can be identified in the cytoplasm as elements of an organized cytoskeleton, clearly defined actin-containing structures are formed at the site of cell-matrix contact upon the interaction of trophozoites with fibronectin (FN) and other cellular matrix substrates. The structures are reminiscent of the adhesion plaques or focal contacts found in higher eukaryotic cells, where actin filament bundles insert into specialized regions of the plasma membrane and function as signal transduction organelles. Thus, the formation of adhesion plates in this parasitic ameba could be related to the specific signaling responses involved in its invasive behavior. Here, we report the isolation of amebic adhesion plates and the results of their structural and molecular analyses. Filaments, with the characteristic diameter of F-actin, radiating from an electron-dense matrix, are the main feature. Actin is one of the main protein components of the plate; other proteins identified are a FN-binding protein--previously reported as a "putative" FN receptor--the actin-binding proteins myosin II, myosin I, alpha-actinin, vinculin, and tropomyosin. The presence of the isolated plates of several proteases and protein kinases, in particular pp125FAK, is also demonstrated. our results suggest that adhesion plates in amebas are dynamic membrane-cytoskeletal complexes participating not only in the attachment to FN substrates but also providing the structural basis for their involvement in parasite locomotion and invasiveness.

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Year:  1995        PMID: 8674132     DOI: 10.1002/cm.970320105

Source DB:  PubMed          Journal:  Cell Motil Cytoskeleton        ISSN: 0886-1544


  15 in total

1.  The invasiveness of Entamoeba histolytica - a continuing enigma.

Authors:  J P Ackers
Journal:  Clin Mol Pathol       Date:  1996-08

Review 2.  Rab GTPases take centre stage in understanding Entamoeba histolytica biology.

Authors:  Kuldeep Verma; Vijay Kumar Srivastava; Sunando Datta
Journal:  Small GTPases       Date:  2018-10-13

3.  Activation of MAPK kinase pathway by Gal/GalNAc adherence lectin of E. histolytica: gateway to host response.

Authors:  Seema Rawal; S Majumdar; H Vohra
Journal:  Mol Cell Biochem       Date:  2005-01       Impact factor: 3.396

4.  Exposure to host ligands correlates with colocalization of Gal/GalNAc lectin subunits in lipid rafts and phosphatidylinositol (4,5)-bisphosphate signaling in Entamoeba histolytica.

Authors:  Amanda M Goldston; Rhonda R Powell; Amrita B Koushik; Lesly A Temesvari
Journal:  Eukaryot Cell       Date:  2012-04-13

5.  Invadosome-Mediated Human Extracellular Matrix Degradation by Entamoeba histolytica.

Authors:  Muhammad M Hasan; Jose E Teixeira; Christopher D Huston
Journal:  Infect Immun       Date:  2018-08-22       Impact factor: 3.441

Review 6.  Cysteine proteinases and the pathogenesis of amebiasis.

Authors:  X Que; S L Reed
Journal:  Clin Microbiol Rev       Date:  2000-04       Impact factor: 26.132

Review 7.  Pathogenesis of intestinal amebiasis: from molecules to disease.

Authors:  M Espinosa-Cantellano; A Martínez-Palomo
Journal:  Clin Microbiol Rev       Date:  2000-04       Impact factor: 26.132

8.  Involvement of raft-like plasma membrane domains of Entamoeba histolytica in pinocytosis and adhesion.

Authors:  Richard C Laughlin; Glen C McGugan; Rhonda R Powell; Brenda H Welter; Lesly A Temesvari
Journal:  Infect Immun       Date:  2004-09       Impact factor: 3.441

9.  Host-parasite interaction: parasite-derived and -induced proteases that degrade human extracellular matrix.

Authors:  Carolina Piña-Vázquez; Magda Reyes-López; Guillermo Ortíz-Estrada; Mireya de la Garza; Jesús Serrano-Luna
Journal:  J Parasitol Res       Date:  2012-06-26

10.  Identification of putative cytoskeletal protein homologues in the protozoan host Hartmannella vermiformis as substrates for induced tyrosine phosphatase activity upon attachment to the Legionnaires' disease bacterium, Legionella pneumophila.

Authors:  C Venkataraman; L Y Gao; S Bondada; Y A Kwaik
Journal:  J Exp Med       Date:  1998-08-03       Impact factor: 14.307

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