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Effect of procathepsin D activation peptide on gene expression of breast cancer cells

โœ Scribed by Petr Benes; Aruna Vashishta; Sujata Saraswat-Ohri; Martin Fusek; Sarka Pospisilova; Boris Tichy; Vaclav Vetvicka

Book ID
116333912
Publisher
Elsevier Science
Year
2006
Tongue
English
Weight
171 KB
Volume
239
Category
Article
ISSN
0304-3835

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Cathepsin D, a lysosomal aspartic proteinase, is secreted in the form of enzymatically inactive proenzyme by many types of human breast cancer tissue and exerts mitogenic activity toward these tissues. Flow cytometry was used to test the binding of procathepsin D purified from the secretion of the b

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A simple procedure for the affinity purification of procathepsin D from tissue culture medium conditioned by breast-cancer cells is described. This procedure yielded 2 pg of procathepsin D/ I00 ml medium. The procathepsin D was approximately 95% pure as judged by silver staining of polyacrylamide ge