• Title/Summary/Keyword: protein methylases

Search Result 5, Processing Time 0.016 seconds

Studies of the Activities of Protein Methylases in Pancreatic Tissues (취조직내 Protein Methylases 활성도에 관한 연구)

  • 이명연;홍성렬;이춘우
    • YAKHAK HOEJI
    • /
    • v.27 no.4
    • /
    • pp.295-301
    • /
    • 1983
  • Among the many protein modifications methylation is being investigated actively with regard to bacterial chemotaxis, gene regulation, muscle contraction, cytochrome c methylation, and the synthesis of the acyl transporter, carnitine. In this study the activities of protein methylase I, II, and III in pancreatic tissues of rat, mouse, and guinea pig were examined. Furthermore, the effect of cholinergic agents on the activity of protein methylases in pancreatic fragment of guinea pig was also examined in order to test the relationship between protein methylation and pancreatic secretion. The results are as follows. 1) The activities of protein methylases were generally high in pancreatic tissues of guinea pig and mouse but low in the tissue of rat. 2) The cholinergic stimulants, acetylcholine and carbachol at a concentration of $10^{-5}M$ decreased the activities of protein methylase I, II, and III compared with unstimulated control. 3) The inhibitory effect of the cholinergic stimulant on the activities of protein methylases was not blocked by atropine at a concentration of $10^{-5}M$.

  • PDF

Effects of Carbon Tetrachloride-induced Hepatotoxicity on the Activities of Protein Methylases and SAM-Synthetase in Rat Liver (단백질 메틸화효소류 및 S-아데노실-L-메치오닌 연결효소의 활성도에 미치는 사염화탄소-유발 간독성의 영향)

  • Namkoong, Suck-Min;Yoo, Tae-Moo;Hong, Sung-Youl;Lee, Hyang-Woo
    • YAKHAK HOEJI
    • /
    • v.36 no.1
    • /
    • pp.66-72
    • /
    • 1992
  • In order to test relationships between hepatotoxicity and transmethylation, activities of protein methylases and SAM (S-adenosyl-L-methionine)-synthetase were examined in liver tissues of rats treated with $CCl_4$. Also the concentrations of SAM and SAH were measured by HPLC in rat liver. The results are as follows. (1). Activities of protein methylases were not significantly changed in 24 hours after $CCl_4$ treatment. However, in 48 hours, activities of protein methylases were significantly increased in comparison with that of control. (2). Activity of SAM-synthetase was increased steadily in the time course after $CCl_4$ treatment. (3). S-adenosyl-L-methionine concentration of liver tissues in $CCl_4$-treated group was elevated in 24 hours, and then declined thereafter. But the SAH concentration was slightly decreased in the time course after $CCl_4$ treatment. These results indicate that SAM was very actively used in transmethylation reactions of $CCl_4$ damaged rat liver, suggesting the strong relationships between hepatotoxicity and transmethylation phenomena.

  • PDF

Effect of Adrenergic and Cholinergic Agents on the Activities of Protein Methylases in Pancreatic Tissue (생쥐 췌조직내 Protein Methylase에 대한 자율신경계약물의 영향)

  • 유태무;박선미;이향우
    • YAKHAK HOEJI
    • /
    • v.35 no.4
    • /
    • pp.341-347
    • /
    • 1991
  • It was reported that protein carboxymethylation is involved in amylase secretion of parotid gland by isoproterenot. It was also suggested that a small part of the total cellular protein carboxymethylation is directly involved in pancreatic enzyme secretion. On the contrary, other authors reported that there is no relationship between protein carboxymethylation and secretion in pancreas and parotid gland. In recent study, it was proposed that a methyl acceptor protein plays a limited modulatory role in the coupling of cytosolic $Ca^{++}$ accumulation and exocytosis. In this study, the effects of cholinergic and adrenergic agents on the activities of protein methylase II in pancreatic tissues were examined to test the relationship between protein methylation and pancreatic secretion. The results are as follows. The activity of amylase was slightly increased at the concentration of $10^{-5}$ M of isoproterenol and norepinephrine. The activities of protein methylase I and II were decreased by isoproterenol and norepinephrine, but the activities of protein methylase III were hardly changed. The cholinergic stimulants acetylcholine and carbachol at a concentration of $10^{-5}$ M increased the activities of protein methylase I and decreased the activitiy of protein methylase III compared with control.

  • PDF

Correlation between Protein Methylation and Hepatotoxicity (단백질메칠화 반응과 간독성간의 상관관계)

  • 김재현;박창원;이주한;백윤기;문화회;홍성렬;이향우
    • Biomolecules & Therapeutics
    • /
    • v.2 no.1
    • /
    • pp.47-53
    • /
    • 1994
  • The methylation response as well as the level of methyl donor substance, 5-adenosyl-L-methionine (SAM) has been suggested to be related to hepatotoxicity including hepatocarcinogenesis. But direct correlation between protein methylation and hepatotoxicity has not been established to the present. To observe relationship between protein methylation and short-term hepatotoxicity induced by chemical substances, the activities of protein methylase I and II (PM I, PM II) were examined in cytosolic fraction of SD rat treated orally with acetaminophen(AA), $\alpha$-naphtyl-isothiocyanate (ANIT) and tetracycline (TC) that was known to produce necrosis, cholestasis and steatosis respectively. To evaluate the degree of hepatotoxicity induced by each chemicals, we observed the serum levels of indicative parameters and histopathological alteration. In AA treated group, the activities of PM I were increased at 6, 12 hours after administration, prior to the appearance of the hepatotoxicity by clinical parameters. It was suggested that the levels of PM I were related with the initial stage of hepatotoxic mechanism induced by AA. In ANIT treated group, though most of clinical parameters were significantly increased at 24, 48 hours after administration, the activity of PM I was not changed, indicating that ANIT induced hepatotoxicity was not coupled to protein methylation.

  • PDF

Inhibition of Sma I, Ava I, Nae I, and Xma I endonuclease activities by the methylation of DNA with Hpa II methylase (제한효소 Sma I, Xma I, AVa I, Nae I의 DNA절단반응에 있어서 Hpa II methylation의 억제효과)

  • 최우성;강선철;서정선;유욱준
    • Korean Journal of Microbiology
    • /
    • v.24 no.2
    • /
    • pp.86-90
    • /
    • 1986
  • The DNA methylated by Hpa II methylase was not cleaved by Sma, I, Ava I and Nae I endonucleases. This experimental data could be interpreted as strong evidences that Sma I, Ava I and Nae I methylases which yet to be isolated would methylate on the inmost cytosine nucleotide within their hexameric recognition sequences. The facts that Sma I, Ava I and Nae I endonucleases can not cleave the DNA methylated by Hpa II methylase are the valuable informations for protecting DNAs upon cleavage reactions by Sma I, Ava I and NAe I endonucleases especially for cDNA insertion experiments into vector DNAs using Sma I, Ava I and Nae I oligonucleotide linkers. In the case of Xma I endonuclease, partially cleaved DNA fragments were observed although the reaction rate was greatly decreased. This result implies that the methylation site of Xma I methylase which yet to be isolated would not be the same as that of Hpa II methylase in Xma I sequence.

  • PDF