암세포의 증식과정에서 20 kDa 단백질의 arginine 메칠화 반응에 관한 연구 = Study on Arginine Methylation of 20 kDa Protein During Cell Proliferation in Cancer Cells

다국어 초록 (Multilingual Abstract)

Enzymatic methylation of endogenous protein (s) by protein arginine N-methyl- transferase(EC. 2.1.1.23) in several cancer cell lines was investigated in an attempt to understand possible regulatory role of the modification in relation to cellular proliferation. When several cancer cells (HeLa, HCT-48, A549, HepG2) were incubated with S-adenosyl-L-〔rnethyl-³H〕methionine, the endogenous 20- kDa species in the extracts were most intensely 〔methyl-³H 〕-labeled compared to that in normal colon tissues. Whether the 〔methyl-³H 〕-labeld 20-kDa is due to carboxyl-O-methylation, the alkali-lability of the purified and methylated 20- kDa species were examined at pH 9-11, at 37℃ for 60 min. The results indicated that 〔methyl-³H 〕-label on the 20-kDa species of HCT-48 cells did not decrease after alkali treatment quantified by Fuji BAS 2500 Bio-Image analyzer. The methylation of 20-kDa did not increase in the presence of 4 mM GTPγS, further indicating the methylation is not due to C-terminal farnesylated cysteine carboxyl methylation. Also, none of purified histones showed the same mobility on SDS-PAGE as the 20-kDa endogenoiis substrate. In conclusion, in the present study, a new novel endogenous 20-kDa methyl accepting protein for protein arginine methyltransferase was found which is closely correlated with cell proliferation suggesting a possible role of this post-translational modification during cellular proliferation.