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NF-κB activation by CD26 antigen is independent of dipeptidyl peptidase IV activity (1997)

Blàzquez, M. V. ; Ortiz, C. ; Aranda, E. ; [et al.]

Springer

Protoplasma 197 (1997), S. 26-33

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ISSN: 1615-6102

Keywords: CD26 antigen ; Dipeptidyl peptidase IV ; NF-κB transcription factor ; Tumor cells

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary CD26 antigen distribution among lymphoid and non lymphoid cells is widely documented. This antigen contains dipeptidyl peptidase IV (DPP-IV) enzymatic activity and it is thought to play an important role in the processes of cellular activation. We show that cell activation through the CD26 pathway induces DNA binding of the NF-κB/rel family of transcription factors in human peripheral T lymphocytes, in the hepatoma cell line HepG2, and in Hela cells. The functional significance of the NF-κB in the CD26 mediated signal transduction pathway is demonstrated by transient transfection analysis, since treatment of HepG2 and Hela cells with the anti-CD26 monoclonal antibodies 134-2C2 and 1F7 resulted in transactivation of a luciferase reported construct driven by three κB sites. The ability of CD26 to activate NF-κB seems to be independent of its DPP-IV activity but it is likely that CD26 activation results in an increase of intracellular levels of reactive oxygen intermediates as deduced from the antioxidant pyrrolidine dithiocarbamate blocking of the induction of NF-κB activity on CD26 activated cells. These results provide new evidence that the CD26 antigen plays a pivotal role in the mechanisms of activation of CD26 expressing cells.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01279881

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The transfer coefficient of the electrochemical reduction of cephalosporins and cefamycins (1993)

Muñoz, E. ; Avila, J. L. ; Doctor, J. Pérez ; [et al.]

Weinheim : Wiley-Blackwell

Electroanalysis 5 (1993), S. 325-331

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ISSN: 1040-0397

Keywords: Cephalosporin ; Cefamycin ; Reduction ; Voltammetry ; Chemistry ; Polymer and Materials Science

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: The electrochemical reduction at a mercury electrode of three cephalosporins and one cefamycin bearing a common R3 substituent was studied. The first one-electron transfer of the reduction process was found to be the rate-determining step in all four cases. In addition, the process took place via species adsorbed on the electrode. The analysis of the voltammetric peaks obtained in the absence of diffusion allowed us to establish the variation of the apparent transfer coefficient, αap, throughout the peak. This was found to be a linear function of the faradic current, which is consistent with the assumption that the free energy of adsorption of the antibiotics is a linear function of the coverage. In addition, the transfer coefficient was found to be markedly dependent on the nature of substituent R-and on the character of the cephalosporin or cefamycin.

Additional Material: 7 Ill.