ArticleThe Journal of cell biology1988
Interaction between pathogenic amebas and fibronectin: substrate degradation and changes in cytoskeleton organization.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 97 citations in OpenAlex.
- Live Cells Imaging and Comparative Phosphoproteomics Uncover Proteins from the Mechanobiome inInternational journal of molecular sciences · 2023Article
- The Gal/GalNac lectin as a possible acetylcholine receptor inFrontiers in cellular and infection microbiology · 2023Article
- Detection and Sequencing of Iron Superoxide Dismutase Gene inArchives of Razi Institute · 2021Article
- Bioimage Analysis and Cell Motility.Patterns (New York, N.Y.) · 2021Review
- Rab GTPases take centre stage in understandingSmall GTPases · 2020Review
- EhRab21 associates with the Golgi apparatus in Entamoeba histolytica.Parasitology research · 2020Article
- Invadosome-Mediated Human Extracellular Matrix Degradation by Entamoeba histolytica.Infection and immunity · 2018Article
- Morphodynamics of the Actin-Rich Cytoskeleton inFrontiers in cellular and infection microbiology · 2018Article
- Antiamoebic Activity of Adenophyllum aurantium (L.) Strother and Its Effect on the Actin Cytoskeleton of Entamoeba histolytica.Frontiers in pharmacology · 2016Article
- Small GTPase Rab21 mediates fibronectin induced actin reorganization in Entamoeba histolytica: implications in pathogen invasion.PLoS pathogens · 2015Article
- The cell surface proteome of Entamoeba histolytica.Molecular & cellular proteomics : MCP · 2014Article
- GH3 tumor pituitary cell cytoskeleton and plasma membrane arrangement are determined by extracellular matrix proteins: implications on motility, proliferation and hormone secretion.International journal of physiology, pathophysiology and pharmacology · 2014Article
- Proteases from Entamoeba spp. and Pathogenic Free-Living Amoebae as Virulence Factors.Journal of tropical medicine · 2013Article
- Exposure to host ligands correlates with colocalization of Gal/GalNAc lectin subunits in lipid rafts and phosphatidylinositol (4,5)-bisphosphate signaling in Entamoeba histolytica.Eukaryotic cell · 2012Article
- Pathogenic Naegleria fowleri and non-pathogenic Naegleria lovaniensis exhibit differential adhesion to, and invasion of, extracellular matrix proteins.Microbiology (Reading, England) · 2012Article
- Host-parasite interaction: parasite-derived and -induced proteases that degrade human extracellular matrix.Journal of parasitology research · 2012Article
- Host-microbe interactions and defense mechanisms in the development of amoebic liver abscesses.Clinical microbiology reviews · 2009Review
- Entamoeba histolytica: lipid rafts are involved in adhesion of trophozoites to host extracellular matrix components.Experimental parasitology · 2008Article
- Pathogenesis of intestinal amebiasis: from molecules to disease.Clinical microbiology reviews · 2000Review
- Cysteine proteinases and the pathogenesis of amebiasis.Clinical microbiology reviews · 2000Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Invasion of human tissues by the parasitic protozoan Entamoeba histolytica is a multistep process involving, as a first step, the recognition of surface molecules on target tissues by the amebas or trophozoites. This initial contact is followed by the release of proteolytic and other activities that lyse target cells and degrade the extracellular matrix. In other parasitic diseases, as well as in certain cancers, the interaction of invasive organisms or cells with fibronectin (FN) through specific receptors has been shown to be the initial step in target cell recognition. Interaction with FN triggers the release of proteolytic activities necessary for the effector cell migration and invasion. Here, we describe the specific interaction of Entamoeba histolytica trophozoites with FN, and identify a 37-kD membrane peptide as the putative receptor for FN. The interaction between the parasite and FN leads to a response reaction that includes the secretion of proteases that degrade the bound FN and the rearrangement of amebic actin into "adhesion plates" at sites of contact with FN-coated surfaces. The kinetics of the interaction was determined by measuring the binding of soluble 125I-FN to the trophozoites and visualization of the bound protein using specific antibodies. Degradation of FN was measured by gel electrophoresis and the release of radioactivity into the incubation medium. Focal degradation of FN was visualized as black spots under the trophozoites at contact sites with fluorescent FN. We conclude that the interaction of E. histolytica with FN occurs through a specific surface receptor. The interaction promotes amebic cytoskeleton changes and release of proteases from the parasite. The binding and degradation of extracellular matrix components may facilitate the migration and penetration of amebas into tissues, causing the lesions seen in human hosts.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.