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Cpsf3  -  cleavage and polyadenylation specificity...

Mus musculus

Synonyms: 73 kDa, CPSF 73 kDa subunit, Cleavage and polyadenylation specificity factor 73 kDa subunit, Cleavage and polyadenylation specificity factor subunit 3, Cpsf73, ...
 
 
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Disease relevance of Cpsf3

 

High impact information on Cpsf3

  • We report the narrowing of the candidate region to a 2.6-cM interval between D8S1051 and D8S1831 and the identification of the transmembrane protein 76 gene (TMEM76), which encodes a 73-kDa protein with predicted multiple transmembrane domains and glycosylation sites, as the gene that causes MPS IIIC when it is mutated [4].
  • Competition with ribonuclease A and stimulation by ATP/Mg(2+) and the heat shock cognate protein of 73 kDa show that the lysosomal uptake of the fusion protein also occurs by this pathway [5].
  • SAP-A, -B, -C, and -D derive from proteolysis of a 73-kDa glycoprotein, the SAP precursor [6].
  • It contains an open reading frame which encodes a type II membrane protein of 73 kDa with a cytoplasmic region of about 35 amino acids, a Ca2+ binding consensus sequence, and a single N-glycosylation site [7].
  • Cytotoxic activity and production of toxic nitrogen oxides by macrophages treated with IFN-gamma and monoclonal antibodies against the 73-kDa lipopolysaccharide receptor [8].
 

Biological context of Cpsf3

  • Sequence analysis of the B94 cDNA reveals an open reading frame encoding a 73-kDa polypeptide that has no homology to any known protein [9].
  • Four proteins (100, 89, 67, and 15 kDa) increased and two proteins (97, 73 kDa) decreased their phosphorylation state significantly [10].
  • The cDNA isolated from a mouse 3T3 cDNA library encodes a 73 kDa type II membrane protein with a cytoplasmic region of approximately 35 amino acids and a large C-terminal region that contains a consensus Ca(2+)-binding sequence [11].
  • This cDNA encodes a type II membrane protein of 73 kDa that is 94% identical in amino acid sequence to the murine alpha1,2-mannosidase IB (Herscovics et al., 1994, J. Biol. Chem., 269, 9864-9871) [12].
  • Transfection of COS 1 cells with the Man9-mannosidase cDNA gave rise to a > 30-fold over-expression of a 73-kDa protein whose catalytic properties, including substrate specificity, susceptibility towards alpha-mannosidase inhibitors and metal ion requirements, were similar to those of the 49-kDa enzyme fragment [13].
 

Anatomical context of Cpsf3

  • The hamster IgM mAb 5D3 is specific for an 73-kDa LPS receptor on murine leukocytes [8].
  • A 73 kDa protein was identified by this analysis: this protein is highly enriched in cell lines of B lymphoid origin as compared to pancreatic beta-cells and fibroblast cells [14].
  • Mouse brain and cochlea homogenates reveal at least two ChT1 isoforms: a nonglycosylated approximately 73 kDa protein and a glycosylated approximately 45 kDa protein [15].
  • Additionally, three protein bands each in murine ova and two-cell embryos (M(r) 108, 81, 73 kDa, respectively), and four protein bands of late blastocyst (M(r) 108, 73; 133 and 18 kDa, respectively) stage embryos were also revealed [16].
  • Additionally, radioiodinated P. gingivalis LPS, similarly to E. coli LPS, bound to a 73-kDa protein on C3H/HeJ as well as C3H/HeN B-cells [17].
 

Associations of Cpsf3 with chemical compounds

  • Insulin also induces tyrosine phosphorylation of a 73 kDa protein that is coprecipitated with the tyrosine-phosphorylated insulin receptor in CSV3-1 cells but not in 3T3T cells [18].
  • Injection (i.p.) of RA in dimethyl sulfoxide (DMSO), at a dose sufficient to cause significant proximal-distal reduplication of the pattern in 50% of animals treated, resulted in increased synthesis and accumulation of a 73-kDa protein with a pI of approximately 6.75 [19].
 

Other interactions of Cpsf3

 

Analytical, diagnostic and therapeutic context of Cpsf3

  • Radioimmunoprecipitation analysis showed that the HMSA-5 reactive antigen was a glycoprotein of M(r) 69 to 73 kDa [22].
  • SDS-PAGE of the 32P-labeled cellular proteins revealed that OdN treatment caused a decrease in phosphorylation of the 26 and 73 kDa cellular proteins in the cells [23].
  • Analysis of the molecular forms of Gus mRNA and protein by Northern and Western blotting revealed that the different types of cells all produced a single mature 2.7 kb transcript and a 73 kDa polypeptide [24].
  • The three constitutive and two induced soluble peroxidases of rat had a native molecular mass of 73 kDa by gel filtration and they showed a similar mobility in native PAGE [25].
  • In immunoblotting analysis, antibodies raised against this molecule recognized polypeptides of 73 kDa in T. rangeli medium supernatant (TrSialr) and of 70 kDa in the cell lysates of T. rangeli (TrSials) and T. cruzi (TcSialL) epimastigotes [26].

References

  1. Activation of macrophages for cytolysis of virally infected cells by monoclonal antibody to the 73-kDa lipopolysaccharide receptor. LeBlanc, P.A. J. Leukoc. Biol. (1994) [Pubmed]
  2. Monoclonal antibodies against African swine fever viral antigens. Whyard, T.C., Wool, S.H., Letchworth, G.J. Virology (1985) [Pubmed]
  3. Lipopolysaccharide (LPS) binding to 73-kDa and 38-kDa surface proteins on lymphoreticular cells: preferential inhibition of LPS binding to the former by Rhodopseudomonas sphaeroides lipid A. Lei, M.G., Qureshi, N., Morrison, D.C. Immunol. Lett. (1993) [Pubmed]
  4. Mutations in TMEM76 Cause Mucopolysaccharidosis IIIC (Sanfilippo C Syndrome). Hrebicek, M., Mrazova, L., Seyrantepe, V., Durand, S., Roslin, N.M., Noskova, L., Hartmannova, H., Ivanek, R., Cizkova, A., Poupetova, H., Sikora, J., Urinovska, J., Stranecky, V., Zeman, J., Lepage, P., Roquis, D., Verner, A., Ausseil, J., Beesley, C.E., Maire, I., Poorthuis, B.J., van de Kamp, J., van Diggelen, O.P., Wevers, R.A., Hudson, T.J., Fujiwara, T.M., Majewski, J., Morgan, K., Kmoch, S., Pshezhetsky, A.V. Am. J. Hum. Genet. (2006) [Pubmed]
  5. Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. Salvador, N., Aguado, C., Horst, M., Knecht, E. J. Biol. Chem. (2000) [Pubmed]
  6. Biosynthesis, processing, and targeting of sphingolipid activator protein (SAP )precursor in cultured human fibroblasts. Mannose 6-phosphate receptor-independent endocytosis of SAP precursor. Vielhaber, G., Hurwitz, R., Sandhoff, K. J. Biol. Chem. (1996) [Pubmed]
  7. Isolation of a mouse Golgi mannosidase cDNA, a member of a gene family conserved from yeast to mammals. Herscovics, A., Schneikert, J., Athanassiadis, A., Moremen, K.W. J. Biol. Chem. (1994) [Pubmed]
  8. Cytotoxic activity and production of toxic nitrogen oxides by macrophages treated with IFN-gamma and monoclonal antibodies against the 73-kDa lipopolysaccharide receptor. Green, S.J., Chen, T.Y., Crawford, R.M., Nacy, C.A., Morrison, D.C., Meltzer, M.S. J. Immunol. (1992) [Pubmed]
  9. Cloning of a novel tumor necrosis factor-alpha-inducible primary response gene that is differentially expressed in development and capillary tube-like formation in vitro. Sarma, V., Wolf, F.W., Marks, R.M., Shows, T.B., Dixit, V.M. J. Immunol. (1992) [Pubmed]
  10. Effects of heat shock on neuroblastoma (N1E 115) cell proliferation and differentiation. Stoklosinski, A., Kruse, H., Richter-Landsberg, C., Rensing, L. Exp. Cell Res. (1992) [Pubmed]
  11. Characterization of a novel mouse recombinant processing alpha-mannosidase. Schneikert, J., Herscovics, A. Glycobiology (1994) [Pubmed]
  12. Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha1,2-mannosidase gene involved in N-glycan maturation. Tremblay, L.O., Campbell Dyke, N., Herscovics, A. Glycobiology (1998) [Pubmed]
  13. Man9-mannosidase from pig liver is a type-II membrane protein that resides in the endoplasmic reticulum. cDNA cloning and expression of the enzyme in COS 1 cells. Bieberich, E., Treml, K., Völker, C., Rolfs, A., Kalz-Füller, B., Bause, E. Eur. J. Biochem. (1997) [Pubmed]
  14. Cell-specific expression of helix-loop-helix transcription factors encoded by the E2A gene. Aronheim, A., Shiran, R., Rosen, A., Walker, M.D. Nucleic Acids Res. (1993) [Pubmed]
  15. The final stage of cholinergic differentiation occurs below inner hair cells during development of the rodent cochlea. Bergeron, A.L., Schrader, A., Yang, D., Osman, A.A., Simmons, D.D. J. Assoc. Res. Otolaryngol. (2005) [Pubmed]
  16. Protein phosphorylation pattern and role of products of c-erbB-1 and c-abl proto-oncogenes in murine preimplantation embryonic development. Ahmad, K., Naz, R.K. Am. J. Reprod. Immunol. (1994) [Pubmed]
  17. Splenic B-cell activation in lipopolysaccharide-non-responsive C3H/HeJ mice by lipopolysaccharide of Porphyromonas gingivalis. Shimauchi, H., Ogawa, T., Uchida, H., Yoshida, J., Ogoh, H., Nozaki, T., Okada, H. Experientia (1996) [Pubmed]
  18. Increased tyrosine phosphorylation of the insulin receptor, the insulin receptor substrate-1 and a 73 kDa protein associated with insulin-induced mitogenesis in SV40-transformed 3T3T cells. Wang, H. Mol. Cell. Biochem. (1999) [Pubmed]
  19. Retinoic acid stimulates the synthesis of a novel heat shock protein in the regenerating forelimb of the newt. Carlone, R.L., Boulianne, R.P., Vijh, K., Karn, H., Fraser, G.A. Biochem. Cell Biol. (1993) [Pubmed]
  20. Characterization of the murine gene encoding the hyaluronan receptor RHAMM. Entwistle, J., Zhang, S., Yang, B., Wong, C., Li, Q., Hall, C.L., A, J., Mowat, M., Greenberg, A.H., Turley, E.A. Gene (1995) [Pubmed]
  21. Protein kinases share a common structural motif outside the conserved catalytic domain. Véron, M., Radzio-Andzelm, E., Tsigelny, I., Taylor, S. Cell. Mol. Biol. (Noisy-le-grand) (1994) [Pubmed]
  22. A murine monoclonal antibody, MoAb HMSA-5, against a melanosomal component highly expressed in early stages, and common to normal and neoplastic melanocytes. Der, J.E., Dixon, W.T., Jimbow, K., Horikoshi, T. Br. J. Cancer (1993) [Pubmed]
  23. Rapid sequence-independent cellular response to oligodeoxynucleotides. Balakireva, L.A., Levashova, Z.B., Chroboczek, J., Vlassov, V.V. FEBS Lett. (1997) [Pubmed]
  24. Multi-level regulation of lysosomal gene expression in lymphocytes. Olsen, I., Adams, G., Watson, G., Chain, B., Abraham, D. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  25. Tissue distribution of constitutive and induced soluble peroxidase in rat. Purification and characterization from lacrimal gland. De, P.K. Eur. J. Biochem. (1992) [Pubmed]
  26. Antigenic significance of a Trypanosoma rangeli sialidase. Saldaña, A., Harris, R.A., Orn, A., Monroy, C., Ortega-Barria, E., Sousa, O.E. J. Parasitol. (2002) [Pubmed]
 
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