Cystyl aminopeptidase activity in the plasma, viscera and brain of the snake Bothrops jararaca

• Published in: Comparative biochemistry and physiology. Part A, Molecular & integrative physiology Molecular & integrative physiology, 2005-07, Vol.141 (3), p.336-352
• Main Authors: Alponti, Rafaela Fadoni, Zambotti-Villela, Leonardo, Murena-Nunes, Cristiane, Marinho, Camila Eduardo, do Amaral Olivo, Renata, Silveira, Paulo Flavio
• Format: Article
• Language: English
• Subjects: Angiotensinase; Animals; Blood Proteins - drug effects; Body Weight - drug effects; Bothrops - anatomy & histology; Bothrops - metabolism; Bothrops jararaca; Brain - enzymology; Cystinyl Aminopeptidase - blood; Cystinyl Aminopeptidase - metabolism; Diencephalon - enzymology; Female; Histofluorescence; Hydrodynamics; Kallidinase; Male; Mapping; Osmolar Concentration; Osmoregulation; Oxytocinase; Peptidases; Rats; Sodium Chloride - pharmacology; Vasopressinase; Vasotocinase; Viscera - enzymology
• ISSN: 1095-6433; 1531-4332
• DOI: 10.1016/j.cbpb.2005.06.005

The relationship between plasma osmolality and cystyl aminopeptidase was characterized in the snake Bothrops jararaca and comparisons were made with the emerging picture of this relationship in rats. The profile of cystyl aminopeptidase activity under basal conditions was determined in the soluble and membrane-bound forms in visceral organs and in the central nervous system in comparison with that of alanyl aminopeptidase. The regional localization of cystyl and alanyl aminopeptidase activities was studied in the central nervous system. The basal level of plasma cystyl aminopeptidase, four- to six-fold higher than in rats, suggests its importance to help regulate circulating levels of neurohypophysial peptides in B. jararaca snake. The osmotic sensitivity of this plasma enzyme, undetectable in male, but about three-fold higher in female snakes than in rats, reveals a sexual dimorphism. In marked contrast to those observed in rats, low levels of soluble and particulate forms in the kidney indicate that cystyl aminopeptidase plays a minor metabolizing role at this anatomical location in B. jararaca. Despite of the regional-specific divergence between the levels of rat and snake enzymes, the bilaterally symmetric pattern of the diencephalic distribution of alanyl aminopeptidase reflects functional homologies between these two distantly related species.