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Titolo:
A GROWTH-REGULATED PROTEASE ACTIVITY THAT IS INHIBITED BY THE ANTICARCINOGENIC BOWMAN-BIRK PROTEASE INHIBITOR
Autore:
BILLINGS PC; HABRES JM;
Indirizzi:
UNIV PENN,SCH MED,DEPT RADIAT ONCOL PHILADELPHIA PA 19104
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 7, volume: 89, anno: 1992,
pagine: 3120 - 3124
SICI:
0027-8424(1992)89:7<3120:AGPATI>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
RADIATION-INDUCED TRANSFORMATION; C3H-10T1/2 CELLS; DIETARY ADDITION; MOUSE SKIN; DIMETHYLHYDRAZINE; CARCINOGENESIS; CANCER; TUMORIGENESIS; FIBROBLASTS; SUPPRESSION;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
P.C. Billings e J.M. Habres, "A GROWTH-REGULATED PROTEASE ACTIVITY THAT IS INHIBITED BY THE ANTICARCINOGENIC BOWMAN-BIRK PROTEASE INHIBITOR", Proceedings of the National Academy of Sciences of the United Statesof America, 89(7), 1992, pp. 3120-3124

Abstract

The Bowman-Birk protease inhibitor (BBI) has been shown to be an effective suppressor of carcinogenesis in vivo and in vitro. To elucidate the mechanism(s) by which BBI suppresses carcinogenesis, we believe itwill be necessary to identify and characterize the target enzymes that specifically interact with the BBI. We have shown previously that several cellular proteins in C3H/10T1/2 mouse embryo fibroblast cells specifically bind to a BBI affinity resin. In the current report, we demonstrate that one of these proteins has proteolytic activity as judgedby its ability to degrade gelatin. The enzyme has a mass of 45 kDa and subcellular fractionation experiments demonstrate that this enzyme is located in the cytosol. Furthermore, the proteolytic activity was inhibited by diisopropyl-fluorophosphate but was not affected by EDTA, indicating that this enzyme is a serine protease. Higher levels of protease activity were found in logarithmic-phase C3H/10T1/2 cells compared with nondividing (confluent) cells, suggesting that this protease activity is growth regulated. Similar levels of this activity were present in nontransformed and in radiation-transformed C3H/10T1/2 cells. Treatment of nontransformed C3H/10T1/2 cells with phorbol 12-myristate 13-acetate increased the specific activity of this protease 5- to 10-fold. Our results suggest that this protease is a target enzyme of the BBI in these cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 02:26:21