Poster
# 75
Poster |
|
6th Internet World Congress for Biomedical Sciences |
María Jesús García-López(1), María Jesús Ramírez-Expósito(2), José Manuel Martínez-Martos(3), María Dolores Mayas-Torres(4), Isabel Prieto-Gómez(5), Garbiñe Arechaga-Maza(6), Manuel Ramírez-Sánchez(7)
(1)(3)(4)(5)(6)(7)Unit of Physiology. University of Jaén - Jaén. Spain
(2)Unit of Physiology. University of Jaen - Jaén. Spain
|
 |
|
|
|
|
[Biochemistry] |
[Endocrinology] |
[Neuroscience] |
[Physiology] |
Aminopeptidases (AP) are generally zinc-metalloenzimes distributes in tissues and corporal fluids. These AP hydrolized the amino-terminal extreme of active peptides and polipeptides, so AP play a physiological role in the regulation of circullating biologically active peptides (Mc Donald and Barret, 1986; Sanderik et al., 1988). Therefore, hormonal changes in serum may be reflected in thes enzymatic activity. However, although their hydrolitic action on peptides or artificial substrates has been extensively studies. The actual physiological role of these enzymes and their own mechanism of regulation are not well known. Previous results have suggested an influence of gonadal steroids on serum AP activities (Gandarias et al., 1989;Martínez et al., 1997) raising the possibility that such substances help to create a biochemical enviroment that regulate, in part, the activity of these enzimes. One of these aminopeptidases is pyroglutamil aminopeptidase (pGluAP). pGluAP can be classified as an omega-peptidase which removes pyroglutamyl N-terminal residues from peptides, proteins and arylamidases derivaties in a highly selective manner (1,2). This enzime may be implicated in the regulation of several process in the CNS, and thyrotropin-releasing hormone (TRH) is considered as a possible endogenous substrate.
|
|
|
|
|
|
|
|
[Biochemistry] |
[Endocrinology] |
[Neuroscience] |
[Physiology] |
