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Hysteretic Behavior of Proprotein Convertase 1/3 (PC1/3)

2011; Public Library of Science; Volume: 6; Issue: 9 Linguagem: Inglês

10.1371/journal.pone.0024545

1932-6203

Marcelo Yudi Icimoto, Nilana M.T. Barros, Juliana C. Ferreira, Marcelo F. Marcondes, Douglas Andrade, Maurício F.M. Machado, María A. Juliano, Wagner Alves de Souza Júdice, Luiz Juliano, Vitor Oliveira,

Protease and Inhibitor Mechanisms

The proprotein convertases (PCs) are calcium-dependent proteases responsible for processing precursor proteins into their active forms in eukariotes. The PC1/3 is a pivotal enzyme of this family that participates in the proteolytic maturation of prohormones and neuropeptides inside the regulated secretory pathway. In this paper we demonstrate that mouse proprotein convertase 1/3 (mPC1/3) has a lag phase of activation by substrates that can be interpreted as a hysteretic behavior of the enzyme for their hydrolysis. This is an unprecedented observation in peptidases, but is frequent in regulatory enzymes with physiological relevance. The lag phase of mPC1/3 is dependent on substrate, calcium concentration and pH. This hysteretic behavior may have implications in the physiological processes in which PC1/3 participates and could be considered an additional control step in the peptide hormone maturation processes as for instance in the transformation of proinsulin to insulin.