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당뇨병 쥐에서 Protein Carboxyl Methylation의 변화

Title
당뇨병 쥐에서 Protein Carboxyl Methylation의 변화
Other Titles
Changes of Protein Carboxyl Methylation in Diabetic Rats
Authors
공덕희
Issue Date
1988
Department/Major
교육대학원 과학교육전공화학교육분야
Keywords
당뇨병 쥐Protein Carboxyl MethylationDiabetic Rats
Publisher
이화여자대학교 교육대학원
Degree
Master
Abstract
Protein carboxyl methyltransferase(S-adenosyl methionine : protein carboxyl O-methyltransferase, EC 2.1.1.77) catalyzed the methyl esterification of free α-carboxyl group in L-isoaspartyl residue of its substrate protein using S-adenosyl-L-methionine as a methyl donor. For the purpose of showing the physiological role of methyl esterifiaction by protein carboxyl methyltransferase(PCM), we have investigated the carboxyl methylation of glucose transport protein in the erythrocytes from normal and alloxan-diabetic rats. The enzyme activities and methylatabilities of other tissues(brain, liver and testis) have been measured. The physiological significance of this methylation reaction is not clear but PCM appears to recognize the altered aspartyl residues, D-aspartate and L-isoaspartate in a variety of peptides and proteins. PCM has been proposed to play a role in the repair or degradation of damaged proteins. The level of cytosolic PCM activities and methylatabilities of membrane proteins have increased according to diabetes. Erythrocyte membrane protein was separated by CPC/PAGE in order to show protein participated in methylation. Band 3 and 4. are a good substrate for the PCM.;Methyl donor로 S-adenosyl-L-methionine을 사용해서 기질 단백질의 free carbxyl group을 메칠화 시키는 반응을 촉매하는 Protein Carboxyl Methyltransferase(PCM, EC2.1.1.77)가 당뇨병과 어떠한 연관을 가지고 있는가를 연구하기 위하여 alloxan에 의해 당뇨병이 유발된 쥐에서 단계별로 PCM 활성도와 메칠기 수용 능력을 관찰하였다. 그 결과 PCM 활성도가 정상 쥐 보다 당뇨병 쥐에서 현저한 증가를 나타내었고, 생리적 조건에서 메칠기 수용 능력도 증가하였다. 정상 쥐에 비해 당뇨병 쥐에서 메칠기 수용 능력의 증가는 생체내 손상에 의해 비정상 단백질(D-Aspartyl 또는 L-Isoaspartyl 잔기)의 증가로 사료된다. 메칠화 반응에 관여하는 단백질의 종류를 알아보기 위해, 전기 영동에 의한 당뇨병 쥐의 적혈구 막 단백질을 분리해 본 결과, band 3와 4.5의 methylatability가 정상 쥐에 비해 증가함을 관찰하였다.
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