Bonner, A.B. and Ahmed, S. and Mantle, D. and Preedy, V.R. (2006) An array of brain protease activities and their modulation by the toxic effects of cyanamide. Toxicology, 226 (1). pp. 62-63. ISSN 0300-483X.
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Brain proteolytic enzymes have been implicated in a variety of disorders though most studies have focused on a few components such as the ATP-ubiquitin pathway. In this study we assayed a broad range of representative proteolytic enzyme types, to address the hypothesis that their activities are perturbed in cyanamide toxicity. We dosed maleWistar rats (approximately 0.1 kg BW) with either saline (0.15 mol/l NaCl) or cyanamide, an inhibitor of aldehyde dehydrogenase (ALDH) (0.5 mmol/kg BW; ip). After 3 h rats were killed and cerebellum dissected. Using fluorimetry, we measured the activities of the cytoplasmic enzymes alanyl-aminopeptidase (ALAAP), arginyl-aminopeptidase (ARGAP), leucylaminopeptidase (LEUAP), dipeptidyl-aminopeptidase IV (DIA-IV), tripeptidyl aminopetidase (TRI-AP) and proline endopeptidase (PROAP), as well as the lysosomal enzymes cathepsins B (CATHB), D (CATHD), H (CATHH) and L (CATHL), dipeptidyl aminopeptidases I (DIA-I) and II (DIA-II) and proteasomal chymotrypsin-like (PRCHY) and trypsin-like (PRTRP) activities (Table 1). There was a wide range of proteolytic activities (Table 1). The highest activity was found in arginyl aminopeptidase whereas proteosomal activities were low. In response to cyanamide dosage in vivo, there were significant increases in the in vitro activities of cerebellum DIA-IV (P < 0.05). There were also reductions in DIA-I and CATHL (P < 0.001). In conclusions, impaired proteolysis may contribute to, or reflect, the cellular toxicity of cyanamide.
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R Medicine > RS Pharmacy and materia medica
|Divisions:||Faculties > University wide - Teaching/Research Groups > Centre for Cognitive Neuroscience and Cognitive Systems|
|Depositing User:||M.P. Stone|
|Date Deposited:||08 Aug 2009 10:44|
|Last Modified:||08 Aug 2009 10:44|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/12028 (The current URI for this page, for reference purposes)|
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