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Exosc10  -  exosome component 10

Mus musculus

Synonyms: Autoantigen PM/Scl 2 homolog, Exosome component 10, PM-Scl, PM/Scl-100, Pmscl2, ...
 
 
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Disease relevance of Exosc10

  • BACKGROUND: The major house dust mite allergen Der p 2 has been regarded as an important allergen involved in the immunopathogenesis of allergic asthma and eczema [1].
  • The results thus indicated that the change of pi class forms in adenomas is caused mainly by alteration in the p-1 level and the contribution of p-2 is minimal [2].
  • Recombinant p-1 and p-2 proteins were expressed in Escherichia coli [2].
  • After LNIT, there was a reduction of airway hypersensitivity at 30 min after allergen challenge in the rDer p 2-and Der p-sensitized mice, with a significant decrease only in rDer p 2-sensitized mice [3].
 

High impact information on Exosc10

  • Cell-to-cell fusion, translocation of phosphatidylserine, and inhibition of fusion of pG-transfected cells defined the p9 + p2 (fragment 11, sequence 56-110) as a fragment with higher specific activity for anionic phospholipid aggregation than the previously reported p2 [4].
  • From Edman radiosequencing of 32P-labeled p1, p2, and p3 and the amino acid sequence of the mouse receptor, the location of each phosphopeptide within the beta subunit was determined [5].
  • Further characterization of these phosphopeptides revealed that p1 and p2 represent the triply and doubly phosphorylated forms, respectively, of the region within the tyrosine kinase domain containing tyrosines 1148, 1152, and 1153 [5].
  • CD4(+)CD25(+) T cells from GF mice showed a lower relative gene expression of fork head box p3 gene (Foxp3) and were not as potent suppressors in vitro as CD4(+)CD25(+) T cells from conv animals [6].
  • In E11.5 spinal cord, Olig3 was transiently expressed in the lateral margin of the subventricular zone as three ventral clusters at the level of the p3, p2 and p0 domains, as well as in the dorsal neural tube [7].
 

Biological context of Exosc10

  • To probe further an effect involving RNA degradation pathways, the inhibition by RNA interference of Rent1, a factor essential for nonsense-mediated decay and Exosc10, a specific nuclear component of the exosome, was analysed and shown to similarly impair Xist upregulation and XCI [8].
  • Complete mouse Pmscl1 and Pmscl2 cDNA sequences, chromosomal localizations, exon/intron structure, and promoter region sequences of the mouse Pmscl2 gene are presented [9].
  • In addition, the genomic DNA sequences of Der p 2 which were obtained by PCR amplification using the environmental mites isolated from Taiwan and Australia have helped to confirm the authenticity of the polymorphisms detected in the cDNA clones generated from CSL cultured mites [1].
  • METHODS: Isolation of cDNA clones was performed by screening the cDNA libraries with Der p 2 cDNA probe and the genomic sequences for Der p 2 were obtained by PCR amplification from environmental dust mites with Der p 2-specific primers [1].
  • In contrast, mice immunized with construct p52 showed a mixed TH1/TH2 phenotype and produced substantial circulating Der p 2 protein [10].
 

Anatomical context of Exosc10

  • In the diencephalon of Pax6Sey-1Neu/Pax6Sey-1Neu mice there is an apparent enlargement of the zona limitans (the boundary region between prosomeres p2 and p3), and a blurring of the p1-p2 boundary [11].
  • Along the caudo-rostral axis, the territory in which PMP-22 was detected spanned the mesencephalon and the prosencephalon, extending caudally from the limit between the isthmus and the mesencephalon, and rostrally to the boundary between prosomeres 4 and 5 (p4/p5) [12].
  • In p2 and p3, ventral markers are expressed more dorsally than normal, and this is accompanied in p3 by a reduction in the size of the zona incerta [11].
  • RESULTS: LNIT with rDer p 2 in conjunction with FIP could downregulate the lymphocyte infiltration in both rDer p 2- and Der p-induced airway inflammation [3].
 

Associations of Exosc10 with chemical compounds

  • RESULTS: In this study, we have characterized the sequences of three different gene alleles coding for the major house dust mite allergen Der p 2 at the cDNA level [1].
  • All mimotopes included Gly at p2 and either Val or Ile at p4, suggesting a requirement for a hydrophobic residue with specific conformation [13].
  • Unlike p-1, the p-2 protein did not show any significant activity towards 1-chloro-2,4-dinitrobenzene and did not bind to S-hexylglutathione-Sepharose despite immunological cross-reactivity [2].
 

Analytical, diagnostic and therapeutic context of Exosc10

  • To clarify which of the two genes for pi class glutathione S-transferases (GSTs) (p-1 and p-2) is dominantly expressed in mouse hepatic adenomas, the relative mRNA levels were examined by means of the reverse transcription-polymerase chain reaction (RT-PCR) [2].
  • This study evaluated and characterized the immune responses induced by three DNA constructs encoding different forms of Der p 2 for safe and efficacious vaccination against mite allergy [10].
  • The circulating Der p 2 protein was detected by sandwich ELISA [10].
  • After intratracheal challenge with rDer p 2 and Der p, the airway inflammation was determined by analyzing the cell subpopulation and cytokine concentration in the bronchoalveolar lavage fluid [3].

References

  1. Analysis of sequence polymorphism of a major mite allergen, Der p 2. Chua, K.Y., Huang, C.H., Shen, H.D., Thomas, W.R. Clin. Exp. Allergy (1996) [Pubmed]
  2. Identification of glutathione S-transferase p-1 as the class pi form dominantly expressed in mouse hepatic adenomas. Ookawa, K., Nakano, H., Kakizaki, I., Hatayama, I., Kajihara-Kano, H., Kimura, J., Hayakari, M., Takahata, T., Satoh, K., Tsuchida, S. Jpn. J. Cancer Res. (1998) [Pubmed]
  3. Production of salivary immunoglobulin A and suppression of Dermatophagoides pteronyssinus-induced airway inflammation by local nasal immunotherapy. Liu, Y.H., Tsai, J.J. Int. Arch. Allergy Immunol. (2005) [Pubmed]
  4. A protein G fragment from the salmonid viral hemorrhagic septicemia rhabdovirus induces cell-to-cell fusion and membrane phosphatidylserine translocation at low pH. Estepa, A.M., Rocha, A.I., Mas, V., Pérez, L., Encinar, J.A., Nuñez, E., Fernandez, A., Gonzalez Ros, J.M., Gavilanes, F., Coll, J.M. J. Biol. Chem. (2001) [Pubmed]
  5. Substrate phosphorylation catalyzed by the insulin receptor tyrosine kinase. Kinetic correlation to autophosphorylation of specific sites in the beta subunit. Flores-Riveros, J.R., Sibley, E., Kastelic, T., Lane, M.D. J. Biol. Chem. (1989) [Pubmed]
  6. Impaired regulatory T cell function in germ-free mice. Ostman, S., Rask, C., Wold, A.E., Hultkrantz, S., Telemo, E. Eur. J. Immunol. (2006) [Pubmed]
  7. Non-overlapping expression of Olig3 and Olig2 in the embryonic neural tube. Takebayashi, H., Ohtsuki, T., Uchida, T., Kawamoto, S., Okubo, K., Ikenaka, K., Takeichi, M., Chisaka, O., Nabeshima, Y. Mech. Dev. (2002) [Pubmed]
  8. Nuclear mRNA degradation pathway(s) are implicated in Xist regulation and X chromosome inactivation. Ciaudo, C., Bourdet, A., Cohen-Tannoudji, M., Dietz, H.C., Rougeulle, C., Avner, P. PLoS Genet. (2006) [Pubmed]
  9. Structure and localization of mouse Pmscl1 and Pmscl2 genes. Bliskovski, V., Liddell, R., Ramsay, E.S., Miller, M.J., Mock, B.A. Genomics (2000) [Pubmed]
  10. Intramuscular immunization with DNA construct containing Der p 2 and signal peptide sequences primed strong IgE production. Tan, L.K., Huang, C.H., Kuo, I.C., Liew, L.M., Chua, K.Y. Vaccine (2006) [Pubmed]
  11. Disruption of PAX6 function in mice homozygous for the Pax6Sey-1Neu mutation produces abnormalities in the early development and regionalization of the diencephalon. Grindley, J.C., Hargett, L.K., Hill, R.E., Ross, A., Hogan, B.L. Mech. Dev. (1997) [Pubmed]
  12. PMP-22 expression in the central nervous system of the embryonic mouse defines potential transverse segments and longitudinal columns. Parmantier, E., Braun, C., Thomas, J.L., Peyron, F., Martinez, S., Zalc, B. J. Comp. Neurol. (1997) [Pubmed]
  13. Identification of mimotopes for the H4 minor histocompatibility antigen. Strausbauch, M.A., Nevala, W.K., Roopenian, D.C., Stefanski, H.E., Wettstein, P.J. Int. Immunol. (1998) [Pubmed]
 
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