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Projects / Programmes source: ARIS

Proteaze in proteazni inhibitorji v napredovanju raka: možna uporaba v prognozi, preventivi in antimetastatski terapiji (Slovene)

Research activity

Code Science Field Subfield
3.04.00  Medical sciences  Oncology   

Code Science Field
P004  Natural sciences and mathematics  Biochemistry, Metabolism 
B200  Biomedical sciences  Cytology, oncology, cancerology 
Keywords
cystatins, cathepsins, proteolytic enzymes, protease inhibitors, cysteine proteinases, cancer, invasion, brain tumors, breast tumors, prevention, therapy.
Evaluation (rules)
source: COBISS
Researchers (11)
no. Code Name and surname Research area Role Period No. of publicationsNo. of publications
1.  06989  PhD Andrej Blejec  Mathematics  Researcher  1998 - 1999  287 
2.  10291  PhD Nina Cimerman  Pharmacy  Researcher  1997 - 1999  117 
3.  09892  PhD Metka Filipič  Biology  Researcher  1998 - 1999  585 
4.  13983  PhD Snježana Frković Grazio  Oncology  Researcher  1997 - 1999  212 
5.  02686  PhD Rastko Golouh  Oncology  Researcher  1997 - 1999  364 
6.  10502  PhD Nataša Kopitar Jerala  Biochemistry and molecular biology  Researcher  1997 - 1999  239 
7.  04648  PhD Janko Kos  Biotechnical sciences  Researcher  1997 - 1999  1,159 
8.  06394  Marta Krašovec  Pharmacy  Researcher  1997 - 1999  83 
9.  07802  PhD Tamara Lah Turnšek  Biology  Head  1998 - 1999  1,020 
10.  17096  Andreja Sekirnik  Biochemistry and molecular biology  Researcher  1997 - 1999  30 
11.  10974  PhD Irena Zajc  Biochemistry and molecular biology  Researcher  1998 - 1999  134 
Organisations (4)
no. Code Research organisation City Registration number No. of publicationsNo. of publications
1.  0105  National Institute of Biology  Ljubljana  5055784  13,265 
2.  0106  Jožef Stefan Institute  Ljubljana  5051606000  90,706 
3.  0259  Krka, tovarna zdravil, d.d., Novo mesto (Slovene)  Novo mesto  5043611  3,799 
4.  0302  Institute of Oncology Ljubljana  Ljubljana  5055733000  15,468 
Abstract
Proteinases play an important role in distinct steps during tumor progression and most likely contribute in cascade proteolytic events which help tumor cells during the three-step process of invasion. Presumably, lysosomal proteinases, cathepsins, are involved in the cascade. In this study, cathepsins B and L and their endogenous inhibitors, stefins A and B are evaluated in: 1) Breast carcinoma at various stages of progression. We compare the enzyme activities and protein content of these biological markers with other proteolytic systems, with clinical and histo-pathological properties of breast tumors and with the patients survival- (2) Brain tumors, where we elucidate gene regulation of this proteolytic system: we will measure and compare the levels (mRNA, protein and activity) of cathepsins and stefins in benign and malignant tumors. (3) Brain and breast tumor cell lines with different in vitro invasive potential. In the in vitro invasion assay, which we developed, we are evaluating the effect of various proteolytic enzymes on cell adhesion, chemotaxis and chemo-invasion. The results of these studies will elucidate: (a) the role and possible correlation of cysteine cathepsins with the tumor cell invasivness, (b) possible application of proteases and inhibitors in the prognosis of breast cancer and possible application of protease inhibitors in preventing invasion of metastatic cells and consequently their use in cancer therapy.
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