전립선암에 특이한 Ribonuclease Isozyme의 작용기전에 관한 연구 = Mechanism of Action of Ribonuclease Isozume specific to Prostate Cancer

다국어 초록 (Multilingual Abstract)

One of the RNase isozymes presumed to be specific to prostate cancer was isolated and purified from prostate cancer tissue by a DEAE-cellulose column chromatography and high performance liquid chromatography(HLPC). The substrate specificity and product analysis for the RNase isozyme were studied to investigate the role of the isozyme in processes of carcinogenesis and suppression of the prostate cancer.
Neutral RNases in the prostate cancer was separated by a DEAE-cellulose column chromatography into 4 isozymes and a single neutral RNase isozyme present in the control benign prostate hypertrophy tissue was not found in the cancer tissue. The RNase isozyme V from the prostate cancer tissue was further separated and purified by HPLC into 3 protein peaks, of which the third protein peak exhibited RNase activity(Rnase isozyme V(8-14). The isolation pattern of proteins and RNase in prostate cancer tissue was similar to, but not identical with that in the control tissue, suggesting the RNase isozyme V(8-14) from the prostate cancer tissue might be different in nature from that from the control tissue.
The RNase isozyme V(8-14) isolated and purified by a HPLC from the prostate cancer tissue was not active toward polydeoxyribonucleotide and ds polyribonucleotide, but active toward ss polyribonucleotide, preferentially hydrolyzing C-C, A-C, A-U and C-U linkages. A little difference in the substrate specificity was observed between the RNase isozyme V (8-14) from the prostate cancer and the isozyme from the control tissue. The observation that majority of products of poly C digest by the RNase isozyme V (8-14) from the prostate cancer tissue was oligoribonucleotides indicated that the enzyme was endoribonuclease in nature.
The present study indicated that the RNase isozyme V(8-14) from the prostate cancer tissue appeared to be specific to the cancer, the isozyme was active toward C-C, A-C, A-U and C-U linkages of ss polyribonucleotides and the isozyme was endoribonuclease in nature, suggesting that the enzyme had suppressive action on the prostate cancer.