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|Title:||Hysteretic Behavior of Proprotein Convertase 1/3 (PC1/3)|
|Authors:||Icimoto, Marcelo Y. [UNIFESP]|
Barros, Nilana M.
Ferreira, Juliana C. [UNIFESP]
Marcondes, Marcelo F. [UNIFESP]
Andrade, Douglas [UNIFESP]
Machado, Mauricio F. [UNIFESP]
Juliano, Maria A. [UNIFESP]
Judice, Wagner A.
Juliano, Luiz [UNIFESP]
Oliveira, Vitor [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Univ Mogi das Cruzes
|Publisher:||Public Library Science|
|Citation:||Plos One. San Francisco: Public Library Science, v. 6, n. 9, 7 p., 2011.|
|Abstract:||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.|
|Appears in Collections:||Em verificação - Geral|
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