Analysis of breast-tissue cathepsin-d isoforms from patients with breast-cancer, benign breast disease and from normal controls.
Publication/Presentation Date
10-1-1994
Abstract
The isoform composition of cathepsin D has been investigated by isoelectric focusing of breast tissue supernatant fluids from patients with breast cancer, benign breast disease and from normal controls. The results indicated the presence of several acid protease isoforms between pi values of 2 to 8. Three of these isoforms (with approximate pIs of 6.0, 6.4 and 7.0) were pepstatin-inhibitable but not inhibitable by a mixture of protease inhibitors for seryl, cysteinyl and metalloproteases. These three isoforms, and not the more acidic isoforms, contained a 31 kD protein band which was recognized by polyclonal antibodies against cathepsin D, suggesting that these isoforms are cathepsin D. Further evidence that these isoforms are cathepsin D came from studies in which the pepstatin-inhibitable protease activity and not the pepstatin-uninhibitable protease activity, bound to and was elutable from, an immunoaffinity resin made by coupling anticathepsin D polyclonal antibodies to agarose. The mean relative percentage of the total breast tissue protease activity associated with pepstatin-inhibitable activity (i.e. cathepsin D) was significantly increased (p
Volume
5
Issue
4
First Page
847
Last Page
853
ISSN
1019-6439
Published In/Presented At
Bazel, S., Ferry, K., Shoarinejad, F., Laurykleintop, L., Lange, M., Tachovsky, T., Longo, S., Tucker, S., & Alhadeff, J. (1994). Analysis of breast-tissue cathepsin-d isoforms from patients with breast-cancer, benign breast disease and from normal controls. International journal of oncology, 5(4), 847–853. https://doi.org/10.3892/ijo.5.4.847
Disciplines
Medicine and Health Sciences
PubMedID
21559651
Department(s)
Department of Surgery
Document Type
Article