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Gene Review

DNAJC5  -  DnaJ (Hsp40) homolog, subfamily C, member 5

Bos taurus

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Disease relevance of DNAJC5

  • Six soluble antigens prepared from Brucella abortus were compared with a salt-extractable protein (CSP) antigen in an enzyme-linked immunosorbent assay for the detection of antibody to B. abortus in cattle sera [1].
  • Soluble salt-extractable protein antigens (CSP) from Brucella abortus may be of potential value as a vaccine and as a diagnostic reagent for the prevention and diagnosis of bovine brucellosis [2].

High impact information on DNAJC5

  • In contrast, Csp overexpression, which also inhibited the extent of exocytosis, also modified the kinetics of the individual release events seen as an increase in the rise time and a broadening of the residual amperometric spikes in Csp-transfected cells [3].
  • Here we have examined the effect of overexpression of a dominant negative alpha-SNAP mutant or Csp on exocytosis of dense-core granules in single chromaffin cells monitored using amperometry to detect released catecholamine [3].
  • Various other proteins may also have important roles in the processes leading to membrane fusion via interaction with the SNARE proteins, including the secretory vesicle cysteine string protein (Csp) [3].
  • We have characterized mutations in the HPD motif of the synaptic vesicle protein cysteine-string protein (Csp) [4].
  • Mutation of the histidine (H43Q) or aspartic acid (D45A) residues of this motif reduced the ability of Csp to stimulate the ATPase activity of mammalian Hsc70 [4].

Chemical compound and disease context of DNAJC5

  • Salt-extractable protein antigens (CSP) from Brucella abortus strains 19 and 2308 (vaccine and virulent strains, respectively) were analysed by crossed immunoelectrophoresis (CIE) using rabbit antisera to protein antigens and by isoelectricfocusing (IEF) in polyacrylamide gels [5].

Biological context of DNAJC5


Anatomical context of DNAJC5


Associations of DNAJC5 with chemical compounds


Analytical, diagnostic and therapeutic context of DNAJC5


  1. Specific enzyme-linked immunosorbent assay for detection of bovine antibody to Brucella abortus. Tabatabai, L.B., Deyoe, B.L. J. Clin. Microbiol. (1984) [Pubmed]
  2. Biochemical and biological properties of soluble protein preparations from Brucella abortus. Tabatabai, L.B., Deyoe, B.L. Dev. Biol. Stand. (1984) [Pubmed]
  3. Comparison of cysteine string protein (Csp) and mutant alpha-SNAP overexpression reveals a role for csp in late steps of membrane fusion in dense-core granule exocytosis in adrenal chromaffin cells. Graham, M.E., Burgoyne, R.D. J. Neurosci. (2000) [Pubmed]
  4. The molecular chaperone function of the secretory vesicle cysteine string proteins. Chamberlain, L.H., Burgoyne, R.D. J. Biol. Chem. (1997) [Pubmed]
  5. Characterization of salt-extractable protein antigens from Brucella abortus by crossed immunoelectrophoresis and isoelectricfocusing. Tabatabai, L.B., Deyoe, B.L. Vet. Microbiol. (1984) [Pubmed]
  6. Vaccination of cattle with chemically modified and unmodified salt-extractable proteins from Brucella abortus. Confer, A.W., Tabatabai, L.B., Deyoe, B.L., Oltjen, S.L., Hall, S.M., Oltjen, J.W., Morton, R.J., Fulnechek, D.L., Smith, R.E., Smith, R.A. Vet. Microbiol. (1987) [Pubmed]
  7. Cysteine string proteins are associated with chromaffin granules. Chamberlain, L.H., Henry, J., Burgoyne, R.D. J. Biol. Chem. (1996) [Pubmed]
  8. Identification of a novel cysteine string protein variant and expression of cysteine string proteins in non-neuronal cells. Chamberlain, L.H., Burgoyne, R.D. J. Biol. Chem. (1996) [Pubmed]
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