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Parva  -  parvin, alpha

Mus musculus

Synonyms: 2010012A22Rik, 5430400F08Rik, AI225929, AU042898, Actopaxin, ...
 
 
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Disease relevance of Parva

 

High impact information on Parva

 

Chemical compound and disease context of Parva

  • Recently, we reported the expression and production of different parts of p67 as fusions to either GFP or to the baculovirus GP64 envelope glycoprotein in insect cells, which resulted in stable proteins recognized by a monoclonal specific for native p67 [8].
  • Ehrlich ascites tumour (EAT) cells were fused with Theileria parva-infected bovine lymphoid (C2) cells using inactivated Sendai virus [9].
 

Biological context of Parva

 

Anatomical context of Parva

 

Associations of Parva with chemical compounds

  • Mutations at the alpha-parvin N-terminal proline-directed serine phosphorylation sites reduced its complex formation with ILK and resulted in defects in podocyte adhesion, architecture, and survival [10].
  • P. leucopus and C. parva were more sensitive than M. musculus to MMS [12].
  • Only valinomycin and, more particularly, gramicidin D were significantly active against B. rodhaini and T. parva [15].
  • When cells were grown in hypoxanthine/aminopterin/thymidine medium (HAT), T parva appeared to be selectively killed by the aminopterin present; this finding would seem to militate against the use of a HAT selection system to clone parasitised hybrids [9].
 

Other interactions of Parva

  • Disruption of the PINCH-1-ILK-alpha-parvin complex significantly reduced the podocyte-matrix adhesion and foot process formation [10].
  • This suggests a parasite-mediated event, involving the recruitment and activation of the host IkappaB kinase (IKK) complex, as has been observed with the related protozoan Theileria parva [16].
 

Analytical, diagnostic and therapeutic context of Parva

References

  1. Role of the integrin-linked kinase/PINCH1/alpha-parvin complex in cardiac myocyte hypertrophy. Chen, H., Huang, X.N., Yan, W., Chen, K., Guo, L., Tummalapali, L., Dedhar, S., St-Arnaud, R., Wu, C., Sepulveda, J.L. Lab. Invest. (2005) [Pubmed]
  2. Comparative growth of bovine lymphosarcoma cells and lymphoid cells infected with Theileria parva in athymic (nude) mice. Irvin, A.D., Brown, C.G., Kanhai, G.K., Stagg, D.A. Nature (1975) [Pubmed]
  3. Identification of a surface antigen on Theileria parva sporozoites by monoclonal antibody. Dobbelaere, D.A., Shapiro, S.Z., Webster, P. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  4. Linear peptide specificity of bovine antibody responses to p67 of Theileria parva and sequence diversity of sporozoite-neutralizing epitopes: implications for a vaccine. Nene, V., Gobright, E., Bishop, R., Morzaria, S., Musoke, A. Infect. Immun. (1999) [Pubmed]
  5. Production in ascites fluid of biosynthetically labelled monoclonal antibody to Theileria parva sporozoites. Dobbelaere, D.A., Spooner, P.R. J. Immunol. Methods (1985) [Pubmed]
  6. ILK, PINCH and parvin: the tIPP of integrin signalling. Legate, K.R., Montañez, E., Kudlacek, O., Fässler, R. Nat. Rev. Mol. Cell Biol. (2006) [Pubmed]
  7. Phosphorylation of actopaxin regulates cell spreading and migration. Clarke, D.M., Brown, M.C., LaLonde, D.P., Turner, C.E. J. Cell Biol. (2004) [Pubmed]
  8. Improved immunogenicity of novel baculovirus-derived Theileria parva p67 subunit antigens. Kaba, S.A., Schaap, D., Roode, E.C., Nene, V., Musoke, A.J., Vlak, J.M., van Oers, M.M. Vet. Parasitol. (2004) [Pubmed]
  9. Attempts to produce Theileria parva-infected mouse cells using cell fusion techniques. Irvin, A.D., Stagg, D.A., Kanhai, G.K. Res. Vet. Sci. (1976) [Pubmed]
  10. Formation and phosphorylation of the PINCH-1-integrin linked kinase-alpha-parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture, and survival. Yang, Y., Guo, L., Blattner, S.M., Mundel, P., Kretzler, M., Wu, C. J. Am. Soc. Nephrol. (2005) [Pubmed]
  11. Genome analysis of Theileria parva. Morzaria, S.P., Young, J.R. Parasitol. Today (Regul. Ed.) (1993) [Pubmed]
  12. Feasibility of micronucleus methods for monitoring genetic damage in two feral species of small mammals. Meier, J.R., Wernsing, P., Torsella, J. Environ. Mol. Mutagen. (1999) [Pubmed]
  13. Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans. Korenbaum, E., Olski, T.M., Noegel, A.A. Gene (2001) [Pubmed]
  14. De novo expression of T cell markers on Theileria parva-transformed lymphoblasts in cattle. Naessens, J., Newson, J., Bensaid, A., Teale, A.J., Magondu, J.G., Black, S.J. J. Immunol. (1985) [Pubmed]
  15. Evaluation of a range of antimicrobial agents against the parasitic protozoa, Plasmodium falciparum, Babesia rodhaini and Theileria parva in vitro. McColm, A.A., McHardy, N. Ann. Trop. Med. Parasitol. (1984) [Pubmed]
  16. Detection of a novel parasite kinase activity at the Toxoplasma gondii parasitophorous vacuole membrane capable of phosphorylating host IkappaBalpha. Molestina, R.E., Sinai, A.P. Cell. Microbiol. (2005) [Pubmed]
  17. Identification of a Theileria mutans-specific antigen for use in an antibody and antigen detection ELISA. Katende, J.M., Goddeeris, B.M., Morzaria, S.P., Nkonge, C.G., Musoke, A.J. Parasite Immunol. (1990) [Pubmed]
  18. Lack of reactivity of sera from Theileria parva-infected and recovered cattle against cell membrane antigens of Theileria parva transformed cell lines. Creemers, P. Vet. Immunol. Immunopathol. (1982) [Pubmed]
 
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