Cancer Poster Session
Prieto, I. (Unit of Physiology, Faculty of Experimental Sciences, University of Jaen, Spain)
Ramirez-Exposito, M.J. (Unit of Physiology, Faculty of Experimental Sciences, University of Jaen, Spain)
Cueva, C. (Ciudad de Jaen General Hospital of Specialities, Spain.)
Alba, F. (Department of Biochemistry and Molecular Biology, University of Granada, Spain)
Ramirez, M. (Unit of Physiology, Faculty of Experimental Sciences, University of Jaen, Spain)
Aminopeptidases (AP), have been involved in the metabolism of several physiologically relevant circulant and local peptides. To evaluate the local role of AP in BC, we measured alanyl- (AlaAP), arginyl- (ArgAP), cystinyl- (CysAP), glutamyl- (GluAP), aspartyl- (AspAP) and pyroglutamyl- (pGluAP) aminopeptidase activities, in their soluble and membrane-bound forms, in BC tissue after surgery, from which we separated samples of neoplastic tissue, adjacent tumoral tissue and non affected surrounding tissue. Comparing with non affected tissue, the results demonstrated highly significant modifications of speific soluble and membrane-bound AP activities, esentially in neoplastic tissue. Samples of neoplastic tissue demonstrated a significant increase of soluble AlaAP, ArgAP and CysAP, as well as membrane-bound ArgAP. However, membrane-bound AspAP and pGluAP activities decreased significantly, respectively in neoplastic tissue and in neoplastic and adjacent tissues. These results may reflect the functional status of their substrates, which could be selectively activated or inhibited locally in the affected tissue, due to the specific conditions that implies the tumoral process.
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|Martinez, J.M.; Prieto, I.; Ramirez-Exposito, M.J.; Cueva, C.; Alba, F.; Ramirez, M.; (1998). Aminopeptidase Activities in Breast Cancer Tissue.. Presented at INABIS '98 - 5th Internet World Congress on Biomedical Sciences at McMaster University, Canada, Dec 7-16th. Available at URL http://www.mcmaster.ca/inabis98/cancer/martinez0389/index.html|
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