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C3  -  complement component 3

Bos taurus

 
 
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Disease relevance of C3

  • The substrates were the same GTP-binding proteins serving as the substrate of an ADP-ribosyltransferase C3 which was produced by a type C strain of Clostridium botulinum [1].
  • The substrate of the brain enzyme was specific for GTP-binding proteins serving as the substrate of botulinum C3 enzyme; the alpha-subunits of trimeric GTP-binding proteins which served as the substrate of cholera or pertussis toxin were not ADP-ribosylated by the endogenous enzyme [1].
  • Rho A protein that had been expressed in E. coli and subsequential purified was readily ADP-ribosylated by the C3 enzyme even in the absence of the activating factors [2].
  • This was followed by absorption of the IgG1 fraction with Staphylococcus aureus containing protein A to remove minor IgG2 contaminants and gel filtration to exclude traces of the third component of complement (C3) [3].
  • The acute phase behavior of C-reactive protein (C-RP), the third component of complement (C3) and total haemolytic complement activity was studied during the course of acute serum sickness (ASS) in rabbits [4].
 

High impact information on C3

  • Fusion proteins containing C3 linked to the C terminus of Ia were transported most efficiently into cells like wild type Ia in an Ib-dependent manner that was blocked by bafilomycin A1 [5].
  • We show that deposition of milk C3 component occurred on six different isolates of S. aureus and that the alternative pathway was the sole complement pathway operating in milk of uninflamed mammary gland [6].
  • Complement-mediated opsonisation by complement component 3 (C3) binding is an important component of the innate immune system [6].
  • The total (13)C content allows one to distinguish between glycerol from plants with the C-4 carbon fixation pathway (maize, mean delta(13)C = -14.4 per thousand) and that from plants with the C-3 pathway (mean delta(13)C = -30.7 per thousand) [7].
  • The C3 and MUT genes, therefore, are likely to be good candidates to study as markers of bTB resistance using functional genomics in animal model systems [8].
 

Anatomical context of C3

  • The activity of an endogenous enzyme, having the same substrate as botulinum C3 enzyme, was also found in brain cytosol [2].
  • Complement (C3) was similarly adsorbed to erythrocytes during infection [9].
 

Analytical, diagnostic and therapeutic context of C3

  • With a quantitative ELISA assay, C3 could be demonstrated in both uterine and vaginal washes [10].
  • When purified bovine C3 was incubated for varying time periods with trichomonad extracellular proteinases, SDS-PAGE gels revealed digestion of the alpha chain to small fragments [10].

References

  1. Identification of a botulinum C3-like enzyme in bovine brain that catalyzes ADP-ribosylation of GTP-binding proteins. Maehama, T., Takahashi, K., Ohoka, Y., Ohtsuka, T., Ui, M., Katada, T. J. Biol. Chem. (1991) [Pubmed]
  2. Characterization of botulinum C3-catalyzed ADP-ribosylation of rho proteins and identification of mammalian C3-like ADP-ribosyltransferase. Maehama, T., Sekine, N., Nishina, H., Takahashi, K., Katada, T. Mol. Cell. Biochem. (1994) [Pubmed]
  3. Protein constituency of unbound fraction of bovine serum applied to anion exchange columns at different pHs and molarities with or without ethylenediamine tetraacetic acid. Application to preparation of bovine IgG1. Nielsen, K., Duncan, J.R. Vet. Immunol. Immunopathol. (1985) [Pubmed]
  4. Studies of the acute phase response in experimental serum sickness. Martyn, P., Charlesworth, J.A., Peake, P.W., Pussell, B.A. Journal of clinical & laboratory immunology. (1990) [Pubmed]
  5. Clostridium perfringens iota toxin. Mapping of the Ia domain involved in docking with Ib and cellular internalization. Marvaud, J.C., Stiles, B.G., Chenal, A., Gillet, D., Gibert, M., Smith, L.A., Popoff, M.R. J. Biol. Chem. (2002) [Pubmed]
  6. Milk complement and the opsonophagocytosis and killing of Staphylococcus aureus mastitis isolates by bovine neutrophils. Barrio, M.B., Rainard, P., Poutrel, B. Microb. Pathog. (2003) [Pubmed]
  7. delta(13)C- and delta(18)O-values of glycerol of food fats. Fronza, G., Fuganti, C., Grasselli, P., Serra, S., Reniero, F., Guillou, C. Rapid Commun. Mass Spectrom. (2001) [Pubmed]
  8. Characterization of selected genes upregulated in non-tuberculous European wild boar as possible correlates of resistance to Mycobacterium bovis infection. Naranjo, V., Ayoubi, P., Vicente, J., Ruiz-Fons, F., Gortazar, C., Kocan, K.M., de la Fuente, J. Vet. Microbiol. (2006) [Pubmed]
  9. Detection of antibodies to platelets and erythrocytes during infection with haemorrhage-causing Trypanosoma vivax in Ayrshire cattle. Assoku, R.K., Gardiner, P.R. Vet. Parasitol. (1989) [Pubmed]
  10. Degradation of bovine complement C3 by trichomonad extracellular proteinase. Kania, S.A., Reed, S.L., Thomford, J.W., BonDurant, R.H., Hirata, K., Corbeil, R.R., North, M.J., Corbeil, L.B. Vet. Immunol. Immunopathol. (2001) [Pubmed]
 
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