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Gene Review

10.t00003  -  actin

Entamoeba histolytica HM-1:IMSS

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Disease relevance of 10.t00003

 

Psychiatry related information on 10.t00003

  • These data suggested that, as well as the motor activity, myosin IB in E. histolytica plays a structural role on the actin network owing to its ability to cross-link filaments [4].
 

High impact information on 10.t00003

  • The results demonstrate a rapid, recognition-specific stimulation of reorganization of the actin cytoskeleton of E. histolytica induced by binding to target cells [5].
  • Challenge with latex beads of similar size and number, which E. histolytica phagocytized more slowly than RBC, induced neither a detectable increase in polymerized actin content nor appearance of polymerized actin at the contact interface [5].
  • Many trophozoite-target interfaces were outlined with a ring of polymerized amoeba actin, revealed by rhodamine-phalloidin staining of glutaraldehyde-fixed and Triton-X 100-extracted cells [5].
  • By methanol extraction and spectrofluorimetric measurement of bound rhodamine-phalloidin we were able to quantitate polymerized actin in amoebae [5].
  • An Escherichia coli-derived plasmid vector was constructed (pA5'A3'NEO) containing the NEO coding region flanked by untranslated 5' and 3' sequences of an Ent. histolytica actin gene [6].
 

Biological context of 10.t00003

  • Nucleotide sequence analysis of three independent cDNA clones and one genomic clone reveals a highly unusual codon bias and the absence of intervening sequences in E. histolytica actin [1].
  • Analysis of actin genes from E. histolytica was initiated by devising methods for the isolation of biologically active nucleic acids, which allowed the preparation of cDNA and genomic DNA libraries [1].
  • These monoclonal anti-actin antibodies bind to intact L cells and modulate DNA synthesis and cell proliferation, much like affinity-purified polyclonal rabbit antibody to the same Mr 42,000 actin [7].
  • These results indicate that EhCaBP1 may be involved in dynamic membrane restructuring at the time of cell pseudopod formation, phagocytosis and endocytosis in a process mediated by direct binding of EhCaBP1 to actin, affecting the bundling of actin filaments [8].
  • Activation of phosphokinase C or adenylyl cyclase induces protein phosphorylation, actin gene expression and reorganization of the actin cytoskeleton to form adhesive structures that promote interaction with the substrate and the release of proteases [9].
 

Anatomical context of 10.t00003

  • Fractionation of the extracts by DEAE-cellulose and Sephadex G-150 chromatography yielded a purified actin that would copolymerize with rabbit skeletal muscle actin or polymerize alone into long filaments at 24 degrees C upon addition of 100 mM KC1 and 2 mM MgCl2 [2].
  • In cellular extracts, Entamoeba actin would copolymerize with muscle actin, but would not bind to DNase I or form microfilaments [2].
  • Stimulation by target cell membrane lipid of actin polymerization and phagocytosis by Entamoeba histolytica [10].
  • Myosin IB, an actin-binding protein, localizes to the phagocytic cup and, with time, surrounds the internalized phagosome itself [11].
  • Here, anti-chitinase antibodies identified hundreds of small secretory vesicles in encysting E. invadens parasites and in E. histolytica trophozoites overexpressing chitinase under an actin gene promoter [12].
 

Associations of 10.t00003 with chemical compounds

  • Analysis of the staining patterns in the presence and absence of actin dynamics inhibitors, jasplakinolide and cytochalasin D suggested that EhCaBP1 and polymerized F-actin co-localize on membrane protrusions [8].
  • Liposome-stimulated actin polymerization occurred only if the vesicle contained negatively charged phospholipid [13].
  • Synthetic liposomes containing a variety of individual glycosphingolipids bearing neutral, straight-chain oligomeric glycans with galactose or N-acetylgalactosamine termini stimulated rapid (90-s) polymerization of amoeba actin [14].
  • Glycoprotein-bearing liposomes bound to amoebae and did enhance actin polymerization, as do recognized glycosphingolipid-bearing liposomes (G. B. Bailey, E. D. Nudelman, D. B. Day, C. F. Harper, and J. R. Gilmour, Infect. Immun. 58:43-47, 1990) [13].
  • The subunits of the lectin were also observed in high-density, actin-rich fractions of the sucrose gradient [15].
 

Physical interactions of 10.t00003

 

Analytical, diagnostic and therapeutic context of 10.t00003

References

  1. Genomic and cDNA actin sequences from a virulent strain of Entamoeba histolytica. Edman, U., Meza, I., Agabian, N. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  2. Isolation and characterization of actin from Entamoeba histolytica. Meza, I., Sabanero, M., Cazares, F., Bryan, J. J. Biol. Chem. (1983) [Pubmed]
  3. Host tissue invasion by Entamoeba histolytica is powered by motility and phagocytosis. Labruyère, E., Guillén, N. Arch. Med. Res. (2006) [Pubmed]
  4. Overexpression of myosin IB in living Entamoeba histolytica enhances cytoplasm viscosity and reduces phagocytosis. Marion, S., Wilhelm, C., Voigt, H., Bacri, J.C., Guillén, N. J. Cell. Sci. (2004) [Pubmed]
  5. Rapid polymerization of Entamoeba histolytica actin induced by interaction with target cells. Bailey, G.B., Day, D.B., Gasque, J.W. J. Exp. Med. (1985) [Pubmed]
  6. Transfection and continuous expression of heterologous genes in the protozoan parasite Entamoeba histolytica. Hamann, L., Nickel, R., Tannich, E. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  7. Mitogen-like monoclonal anti-actin antibodies. Rosenblatt, H.M., Parikh, N., McClure, J.E., Meza, I., Hwo, S.Y., Bryan, J., Shearer, W.T. J. Immunol. (1985) [Pubmed]
  8. Calcium binding protein 1 of the protozoan parasite Entamoeba histolytica interacts with actin and is involved in cytoskeleton dynamics. Sahoo, N., Labruyère, E., Bhattacharya, S., Sen, P., Guillén, N., Bhattacharya, A. J. Cell. Sci. (2004) [Pubmed]
  9. Extracellular matrix-induced signaling in Entamoeba histolytica: its role in invasiveness. Meza, I. Parasitol. Today (Regul. Ed.) (2000) [Pubmed]
  10. Stimulation by target cell membrane lipid of actin polymerization and phagocytosis by Entamoeba histolytica. Bailey, G.B., Day, D.B., Nokkaew, C., Harper, C.C. Infect. Immun. (1987) [Pubmed]
  11. New insights into the role of the cytoskeleton in phagocytosis of Entamoeba histolytica. Voigt, H., Guillén, N. Cell. Microbiol. (1999) [Pubmed]
  12. Chitinase secretion by encysting Entamoeba invadens and transfected Entamoeba histolytica trophozoites: localization of secretory vesicles, endoplasmic reticulum, and Golgi apparatus. Ghosh, S.K., Field, J., Frisardi, M., Rosenthal, B., Mai, Z., Rogers, R., Samuelson, J. Infect. Immun. (1999) [Pubmed]
  13. Roles of target cell membrane carbohydrate and lipid in Entamoeba histolytica interaction with mammalian cells. Bailey, G.B., Gilmour, J.R., McCoomer, N.E. Infect. Immun. (1990) [Pubmed]
  14. Specificity of glycosphingolipid recognition by Entamoeba histolytica trophozoites. Bailey, G.B., Nudelman, E.D., Day, D.B., Harper, C.F., Gilmour, J.R. Infect. Immun. (1990) [Pubmed]
  15. Involvement of raft-like plasma membrane domains of Entamoeba histolytica in pinocytosis and adhesion. Laughlin, R.C., McGugan, G.C., Powell, R.R., Welter, B.H., Temesvari, L.A. Infect. Immun. (2004) [Pubmed]
  16. Molecular cloning and cellular localization of an unusual bipartite Entamoeba histolytica polypeptide with similarity to actin binding proteins. Ebert, F., Guillén, N., Leippe, M., Tannich, E. Mol. Biochem. Parasitol. (2000) [Pubmed]
  17. Proteinase inhibitors TPCK and TLCK prevent Entamoeba histolytica induced disturbance of tight junctions and microvilli in enteric cell layers in vitro. Lauwaet, T., Oliveira, M.J., Callewaert, B., De Bruyne, G., Mareel, M., Leroy, A. Int. J. Parasitol. (2004) [Pubmed]
  18. Chromosome walk in Entamoeba histolytica: the gene encoding for ribosomal protein L21 neighbors one of the actin genes. Petter, R., Rozenblatt, S., Nuchamowitz, Y., Mirelman, D. Arch. Med. Res. (1992) [Pubmed]
  19. Proteomic analysis of phagocytosis in the enteric protozoan parasite Entamoeba histolytica. Okada, M., Huston, C.D., Mann, B.J., Petri, W.A., Kita, K., Nozaki, T. Eukaryotic Cell (2005) [Pubmed]
 
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