In:
Future Medicinal Chemistry, Future Science Ltd, Vol. 5, No. 4 ( 2013-03), p. 399-409
Abstract:
The lysosomal serine carboxypeptidase CatA has a very important and well-known structural function as well as a, so far, less explored catalytic function. A complete loss of the CatA protein results in the lysosomal storage disease galactosialidosis caused by intralysosomal degradation of β-galactosidase and neuraminidase 1. However, mice with a catalytically inactive CatA enzyme show no signs of this disease. This observation establishes a clear distinction between structural and catalytic functions of the CatA enzyme. Recently, several classes of orally bioavailable synthetic inhibitors of CatA have been identified. Pharmacological studies in rodents indicate a remarkable influence of CatA inhibition on cardiovascular disease progression and identify CatA as a promising novel target for the treatment of heart failure.
Type of Medium:
Online Resource
ISSN:
1756-8919
,
1756-8927
Language:
English
Publisher:
Future Science Ltd
Publication Date:
2013
SSG:
15,3