Increased methylation of the cytosolic 20-kD protein is accompanied by liver regeneration in a hepatectomized rat

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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.

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Kwon, S. Y., Kim, S., Lee, K., Kim, T. J., Lee, S. H., Lee, K. M., & Park, G. H. (2004). Increased methylation of the cytosolic 20-kD protein is accompanied by liver regeneration in a hepatectomized rat. Experimental and Molecular Medicine, 36(1), 85–92. https://doi.org/10.1038/emm.2004.12

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