Abstract
Arginine methylation has been implicated in the signal transduction pathway leading to cell growth. Here we show that a regenerating rat liver following partial hepatectomy exhibited elevated methyltransferase activity as shown by increased methylation of a subset of endogenous proteins in vitro. The 20-kDa protein was shown to be a major cytosolic protein undergoing methylation in regenerating hepatocytes. Methylation of the 20-kDa protein peaked at 1 d following partial hepatectomy, which gradually declined to a basal level within the next 14 d. Likewise, methylation of exogenously added bulk histones followed the similar time kinetics as the 20-kDa protein, reflecting time-dependent changes in methyltransferase activity in regenerating hepatocytes. Presence of exogenously added bulk histone in the in vitro methylation assay resulted in dose-dependent inhibition of methylation of the 20-kDa protein. All the histone subtypes tested, histone 1, 2A, 2B, 3 or 4, were able to inhibit methylation of the 20-kDa protein while addition of cytochrome C, α-lactalbumin, carbonic anhydrase, bovine serum albumin, and γ globulin minimally affected methylation of the 20-kDa protein. Since methylation of the 20-kDa protein preceded proliferation of hepatocytes upon partial hepatectomy, it is tempting to speculate that the methylated 20-kDa protein by activated histone-specific methyltransferase may be involved in an early signal critical for liver regeneration.
| Original language | English |
|---|---|
| Pages (from-to) | 85-92 |
| Number of pages | 8 |
| Journal | Experimental and Molecular Medicine |
| Volume | 36 |
| Issue number | 1 |
| Publication status | Published - 2004 Feb 29 |
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Keywords
- Arginine N-methylation
- Cytosolic 20-kDa protein
- Histone
- Regenerating rat liver
ASJC Scopus subject areas
- Biochemistry
- Genetics
Cite this
Increased methylation of the cytosolic 20-kD protein is accompanied by liver regeneration in a hepatectomized rat. / Kwon, Soon Young; Kim, Sohee; Lee, Kyounghwa; Kim, Tae Jin; Lee, Seung Hoon; Lee, Kyung-Mi; Park, Gil-Hong.
In: Experimental and Molecular Medicine, Vol. 36, No. 1, 29.02.2004, p. 85-92.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Increased methylation of the cytosolic 20-kD protein is accompanied by liver regeneration in a hepatectomized rat
AU - Kwon, Soon Young
AU - Kim, Sohee
AU - Lee, Kyounghwa
AU - Kim, Tae Jin
AU - Lee, Seung Hoon
AU - Lee, Kyung-Mi
AU - Park, Gil-Hong
PY - 2004/2/29
Y1 - 2004/2/29
N2 - Arginine methylation has been implicated in the signal transduction pathway leading to cell growth. Here we show that a regenerating rat liver following partial hepatectomy exhibited elevated methyltransferase activity as shown by increased methylation of a subset of endogenous proteins in vitro. The 20-kDa protein was shown to be a major cytosolic protein undergoing methylation in regenerating hepatocytes. Methylation of the 20-kDa protein peaked at 1 d following partial hepatectomy, which gradually declined to a basal level within the next 14 d. Likewise, methylation of exogenously added bulk histones followed the similar time kinetics as the 20-kDa protein, reflecting time-dependent changes in methyltransferase activity in regenerating hepatocytes. Presence of exogenously added bulk histone in the in vitro methylation assay resulted in dose-dependent inhibition of methylation of the 20-kDa protein. All the histone subtypes tested, histone 1, 2A, 2B, 3 or 4, were able to inhibit methylation of the 20-kDa protein while addition of cytochrome C, α-lactalbumin, carbonic anhydrase, bovine serum albumin, and γ globulin minimally affected methylation of the 20-kDa protein. Since methylation of the 20-kDa protein preceded proliferation of hepatocytes upon partial hepatectomy, it is tempting to speculate that the methylated 20-kDa protein by activated histone-specific methyltransferase may be involved in an early signal critical for liver regeneration.
AB - Arginine methylation has been implicated in the signal transduction pathway leading to cell growth. Here we show that a regenerating rat liver following partial hepatectomy exhibited elevated methyltransferase activity as shown by increased methylation of a subset of endogenous proteins in vitro. The 20-kDa protein was shown to be a major cytosolic protein undergoing methylation in regenerating hepatocytes. Methylation of the 20-kDa protein peaked at 1 d following partial hepatectomy, which gradually declined to a basal level within the next 14 d. Likewise, methylation of exogenously added bulk histones followed the similar time kinetics as the 20-kDa protein, reflecting time-dependent changes in methyltransferase activity in regenerating hepatocytes. Presence of exogenously added bulk histone in the in vitro methylation assay resulted in dose-dependent inhibition of methylation of the 20-kDa protein. All the histone subtypes tested, histone 1, 2A, 2B, 3 or 4, were able to inhibit methylation of the 20-kDa protein while addition of cytochrome C, α-lactalbumin, carbonic anhydrase, bovine serum albumin, and γ globulin minimally affected methylation of the 20-kDa protein. Since methylation of the 20-kDa protein preceded proliferation of hepatocytes upon partial hepatectomy, it is tempting to speculate that the methylated 20-kDa protein by activated histone-specific methyltransferase may be involved in an early signal critical for liver regeneration.
KW - Arginine N-methylation
KW - Cytosolic 20-kDa protein
KW - Histone
KW - Regenerating rat liver
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UR - http://www.scopus.com/inward/citedby.url?scp=1642368160&partnerID=8YFLogxK
M3 - Article
C2 - 15031676
AN - SCOPUS:1642368160
VL - 36
SP - 85
EP - 92
JO - Experimental and Molecular Medicine
JF - Experimental and Molecular Medicine
SN - 1226-3613
IS - 1
ER -