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An array of brain protease activities and their modulation by the toxic effects of cyanamide

Bonner, Adrian B., Ahmed, Sohail, Mantle, David, Preedy, Victor 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. (doi:10.1016/j.tox.2006.05.082) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:12028)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL
http://dx.doi.org/10.1016/j.tox.2006.05.082

Abstract

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.

Item Type: Article
DOI/Identification number: 10.1016/j.tox.2006.05.082
Additional information: This item is a Meeting abstract.
Subjects: R Medicine
R Medicine > RS Pharmacy and materia medica
Divisions: Divisions > Division of Human and Social Sciences > School of Psychology
Depositing User: M.P. Stone
Date Deposited: 08 Aug 2009 10:44 UTC
Last Modified: 16 Nov 2021 09:50 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/12028 (The current URI for this page, for reference purposes)
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