Analysis of the interaction of procathepsin D activation peptide with breast cancer cells

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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Bibliographic Details
Published in:International journal of cancer 1997-11, Vol.73 (3), p.403-409
Main Authors: Vetvicka, Vaclav, Vetvickova, Jana, Hilgert, Ivan, Voburka, Zdenek, Fusek, Martin
Format: Article
Language:English
Subjects:
Animal tumors. Experimental tumors
Animals
Antibodies - pharmacology
Biological and medical sciences
Breast Neoplasms - chemistry
Breast Neoplasms - metabolism
Cathepsin D - analysis
Cathepsin D - antagonists & inhibitors
Cathepsin D - metabolism
Cell Line
Enzyme Activation
Enzyme Precursors - analysis
Enzyme Precursors - antagonists & inhibitors
Enzyme Precursors - metabolism
Experimental tumors, general aspects
Fluorescein-5-isothiocyanate - metabolism
Fluorescent Dyes - metabolism
Humans
Medical sciences
Mice
Mice, Inbred BALB C
Mice, Nude
Neoplasm Transplantation
Receptor, IGF Type 2 - metabolism
Receptors, Growth Factor - metabolism
Tumors
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Summary: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 breast cancer cell line ZR‐75‐1 to human breast cancer cells. No previously known surface antigens or soluble M6P‐R or anti‐M6P‐R antibodies were found to inhibit the specific binding of procathepsin D‐FITC. Similarly, none of these potential inhibitors was found to inhibit growth factor activity of procathepsin D. Our results indicate that procathepsin D growth factor activity is mediated by a new, previously unknown receptor moiety and that the binding activity can be localized in position 27–44 of the activation peptide of procathepsin D. Furthermore, in vivo experiments indicate that treatment with anti‐procathepsin D antibodies can reverse the growth of human breast tumors in athymic nude mice. Int. J. Cancer 73:403–409, 1997. © 1997 Wiley‐Liss, Inc.
ISSN:0020-7136
1097-0215
DOI:10.1002/(SICI)1097-0215(19971104)73:3<403::AID-IJC15>3.0.CO;2-D