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Articles by N Baba
Total Records ( 2 ) for N Baba
  N Baba , M Rubio and M. Sarfati

The balance between effector CD4+ T cells secreting IL-17 (Th17) and regulatory T cells (Treg) plays an important role in autoimmune disorders that include rheumatoid arthritis (RA) and Crohn's disease. Tumor necrosis factor (TNF)- is a key pro-inflammatory cytokine that contributes to disease pathogenesis. We investigated the interplay between CD45RA+ Treg and TNF- in the regulation of human Th17 differentiation. We found that CD45RA+ Treg promoted while TNF- inhibited naive CD4+ T-cell differentiation into IL-17 and CCL20 co-expressing Th17 cells without influencing their IL-22 release. Unexpectedly, CD45RA+ Treg depletion abrogated TNF- suppressive function. Finally, dendritic cell-derived TNF- suppressed the development of IL-17+CCL20+ expressing Th17 cells. In conclusion, CD45RA+ Treg positively governs human Th17 development, which is impaired by TNF-. We propose that TNF- may represent a negative feedback mechanism to control IL-17/CCL20- but not IL-22-associated autoimmune pathologies.

  K Akita , N Hieda , N Baba , S Kawaguchi , H Sakamoto , Y Nakanishi , M Yamanishi , K Mori and T. Toraya

The methods of homologous high-level expression and simple large-scale purification for coenzyme B12-dependent ethanolamine ammonia-lyase of Escherichia coli were developed. The eutB and eutC genes in the eut operon encoded the large and small subunits of the enzyme, respectively. The enzyme existed as the heterododecamer 6β6. Upon active-site titration with adeninylpentylcobalamin, a strong competitive inhibitor for coenzyme B12, the binding of 1 mol of the inhibitor per mol of the β unit caused complete inhibition of enzyme, in consistent with its subunit structure. EPR spectra indicated the formation of substrate-derived radicals during catalysis and the binding of cobalamin in the base-on mode, i.e. with 5,6-dimethylbenzimidazole coordinating to the cobalt atom. The purified wild-type enzyme underwent aggregation and inactivation at high concentrations. Limited proteolysis with trypsin indicated that the N-terminal region is not essential for catalysis. His-tagged truncated enzymes were similar to the wild-type enzyme in catalytic properties, but more resistant to p-chloromercuribenzoate than the wild-type enzyme. A truncated enzyme was highly soluble even in the absence of detergent and resistant to aggregation and oxidative inactivation at high concentrations, indicating that a short N-terminal sequence is sufficient to change the solubility and stability of the enzyme.

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