Effect of zinc and calcium ions on the rat kidney membrane-bound form of dipeptidyl peptidase IV


Por: Gómez H., Chappé M., Valiente P.A., Pons T., Chavez, MD, Charli, JL, Pascual I.

Publicada: 1 sep 2013
Resumen:
Dipeptidyl peptidase IV (DPP-IV) is an ectopeptidase with many roles, and a target of therapies for different pathologies. Zinc and calcium produce mixed inhibition of porcine DPP-IV activity. To investigate whether these results may be generalized to mammalian DPP-IV orthologues, we purified the intact membrane-bound form from rat kidney. Rat DPP-IV hydrolysed Gly-Pro-p-nitroanilide with an average V-max of 0.86 +/- 0.01 mu mol min(-1)mL(-1) and K-M of 76 +/- 6 mu M. The enzyme was inhibited by the DPP-IV family inhibitor L-threo-Ile-thiazolidide (K-i=64.0 +/- 0.53 nM), competitively inhibited by bacitracin (K-i=0.16 +/- 0.01 mM) and bestatin (K-i=0.23 +/- 0.02 mM), and irreversibly inhibited by TLCK (IC50 value of 1.20 +/- 0.11 mM). The enzyme was also inhibited by divalent ions like Zn2+ and Ca2+, for which a mixed inhibition mechanism was observed (K-i values of the competitive component: 0.15 +/- 0.01 mM and 50.0 +/- 1.05 mM, respectively). According to bioinformatic tools, Ca2+ ions preferentially bound to the beta-propeller domain of the rat and human enzymes, while Zn2+ ions to the alpha-beta hydrolase domain; the binding sites were essentially the same that were previously reported for the porcine DPP-IV. These data suggest that the cationic susceptibility of mammalian DPP-IV orthologues involves conserved mechanisms.

Filiaciones:
Gómez H.:
 Centro de Estudios de Proteínas (CEP), Facultad de Biología, Universidad de la Habana, Calle 25 No. 455, Vedado, La Habana 10400, Cuba

 Departament de Química, Universitat Autònoma de Barcelona, Bellaterra, Barcelona 08193, Spain

Chappé M.:
 Centro de Estudios de Proteínas (CEP), Facultad de Biología, Universidad de la Habana, Calle 25 No. 455, Vedado, La Habana 10400, Cuba

Valiente P.A.:
 Centro de Estudios de Proteínas (CEP), Facultad de Biología, Universidad de la Habana, Calle 25 No. 455, Vedado, La Habana 10400, Cuba

Pons T.:
 Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), C/Melchor Fernández Almagro 3, Madrid E-28029, Spain

Charli, JL:
 UNAM, Inst Biotecnol, Dept Genet Desarrollo & Fisiol Mol, Cuernavaca 62210, Morelos, Mexico

Pascual I.:
 Centro de Estudios de Proteínas (CEP), Facultad de Biología, Universidad de la Habana, Calle 25 No. 455, Vedado, La Habana 10400, Cuba
ISSN: 02505991
Editorial
INDIAN ACAD SCIENCES, C V RAMAN AVENUE, SADASHIVANAGAR, P B #8005, BANGALORE 560 080, INDIA, India
Tipo de documento: Article
Volumen: 38 Número: 3
Páginas: 461-469
WOS Id: 000323854800003
ID de PubMed: 23938379

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