open access
Vol 45, No 4 (2007)
Original paper
Submitted: 2011-12-19
Published online: 2008-01-01
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Cathepsin D inhibitors.
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Folia Histochem Cytobiol 2007;45(4):291-313.
open access
Vol 45, No 4 (2007)
ORIGINAL PAPERS
Submitted: 2011-12-19
Published online: 2008-01-01
Abstract
Inhibitors of cathepsin D belong to chemical compounds that estrify carboxyl groups of the Asp33 and Asp231 residues of its catalytic site, penta-peptides containing statin, i.e. the amino acid similar in structure to the tetraedric indirect product, and polypeptides found in the spare organs of many plants and forming permanent noncovalent complexes with cathepsin. Cathepsin D activity is also inhibited by alpha2-macroglobulin and antibodies directed against this enzyme. Methods used to determine the activity and concentration of these inhibitors and their analytical, preparative and therapeutic applications are discussed.
Abstract
Inhibitors of cathepsin D belong to chemical compounds that estrify carboxyl groups of the Asp33 and Asp231 residues of its catalytic site, penta-peptides containing statin, i.e. the amino acid similar in structure to the tetraedric indirect product, and polypeptides found in the spare organs of many plants and forming permanent noncovalent complexes with cathepsin. Cathepsin D activity is also inhibited by alpha2-macroglobulin and antibodies directed against this enzyme. Methods used to determine the activity and concentration of these inhibitors and their analytical, preparative and therapeutic applications are discussed.
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About this articleTitle
Cathepsin D inhibitors.
Journal
Folia Histochemica et Cytobiologica
Issue
Article type
Original paper
Pages
291-313
Published online
2008-01-01
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3111
Bibliographic record
Folia Histochem Cytobiol 2007;45(4):291-313.
Authors
Marek Gacko
Alina Minarowska
Alicja Karwowska
Łukasz Minarowski
