Increased lysine N-methylation of a 23-kDa protein during hepatic regeneration
Experimental & Molecular Medicine
; : 155-160, 2005.
Article
в En
| WPRIM
| ID: wpr-201948
Ответственная библиотека:
WPRO
ABSTRACT
The methylation of a 23-kDa nuclear protein increased after partial hepatectomy and methylation returned to basal levels after the initial stage of regeneration. The methylating enzyme was partially purified from rat liver by ammonium sulfate precipitation, DEAE-anion exchange chromatography and Butyl-Sepharose chromatography. The 23-kDa protein was purified from a nuclear fraction of liver tissue with SP-Sepharose. When the 23-kDa protein was methylated with the partially purified methyltransferase and analyzed on C18 high performance liquid chromatography (HPLC), the methylated acceptor amino acid was monomethyl lysine (MML). Previously, only arginine N-methylation of specific substrate proteins has been reported during liver regeneration. However, in this report, we found that lysine N-methylation increased during early hepatic regeneration, suggesting that lysine N-methylation of the 23-kDa nuclear protein may play a functional role in hepatic regeneration. The methyltransferase did not methylate other proteins such as histones, hnRNPA1, or cytochrome C, suggesting the enzyme is a 23-kDa nuclear protein- specific lysine N-methyltransferase.
Key words
Полный текст:
1
База данных:
WPRIM
Основная тема:
Histones
/
Proteins
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Histone-Lysine N-Methyltransferase
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Rats, Sprague-Dawley
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DNA Helicases
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Cytochromes c
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Hepatectomy
/
Liver
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Liver Regeneration
/
Lysine
Пределы темы:
Animals
Язык:
En
Журнал:
Experimental & Molecular Medicine
Год:
2005
Тип:
Article