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KMID : 0382619930130010319
Hanyang Journal of Medicine
1993 Volume.13 No. 1 p.319 ~ p.332
Role of Ribonuclease in Processes involved in Suppression of Osteosarcoma.



Abstract
Neutral ribonuclease(RNase) highly active toward polycytidylate (poly C) was isolated from osteosarcoma tissue by a DEAE-cellulose column chromatography and was found to be specific to the bone sarcoma by means of a high performance lipuid
chromatography(HPLC) and polyacrylamide gel electrophroesis(PAGE). Also studied were substrate specificity and the product analysis of the neutral RNase to understand the role of the enzyme specific to osteosarcoma in pathogenesis of the neutral
RNase
to understand the role of the enzyme specific to osteosarcoma in pathognesis of the bone sarcoma.
Neutral RNase activity was greatly increased in osteosarcoma tissue, suggesting that it could be used as a marker for the bone sarcoma. Neutral RNases in osteosarcoma tissue were separated by a DEAE-cellulose column chromatography into 5 peaks,
of
which
peaks VI and VII RNase isozymes were not found in the control bone tissue. The activity of peak I RNase isozyme was most active among the RNase isozymes separate.
HPLC and PAGE patterns for the proteins associated with the peak I neutral RNase of osteosarcoma appeared to be different from those of the control, suggesting that the enzyme might be specific to the bone sarcoma. The peak I neutral RNase
isozyme
specific to the osteosarcoma was found to be active toward ss polyribonucleotide *highly active toward C-C, C-U and A-U linkages).
Majority of the poly C digest by the RNase specific to the osteosarcoma was observed to be oligoribonucleotides with chain length of 4-25, indicating that the enzyme was enzonuclease in nature.
The present study indicate that 1) neutral RNase activity was greatly increased in osteosarcoma tissue, 2) the enzyme could be used ass a marker for osteosarcoma. 3) the peak I neutral RNase isozyme isolated from osteosarcoma tissue might be
specific to
the bone sarcoma, 4) the RNase isozyme was active toward ss polyribonucleotide and 5) the RNase isozyme was endoribonuclease in nature, suggesting a possible role of the RNase isozyme in the suppression of the osteosarcoma.
KEYWORD
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