Nonhistone protein reorganization in normal and hepatoma cells.
Previously we described (Dong et al., 1990) a nuclear protein (mol. wt. 112 kD) which is expressed abundantly in hepatoma cells and also in hepatocyte cells committed to carcinogenesis. In this report, we further characterize its chemical properties and cellular localization in normal and hepatoma cells. 112 kD hepatoma-associate nonhistone protein is not a cytokeratin-related protein as described by Fukuda et al. (1991). Protein purification experiments revealed that 112 kD protein is a dimer of 56 kD polypeptide present in normal rat liver nuclei. Intranuclear distribution pattern indicated that 112 kD nonhistone protein localizes exclusively in hepatoma nuclear matrix. The data from this study suggest that dimerization of 56 kD nonhistone protein is involved in nuclear matrix reorganization during neoplastic transformation.
Krajewska
W M
WM
Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405, USA.
Chen
H
H
Xie
R
R
Chiu
J F
JF
D000818:Animals; D002471:Cell Transformation, Neoplastic; D005260:Female; D006657:Histones / Q000378:metabolism; D015151:Immunoblotting; D007633:Keratins / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000378:metabolism*; D015530:Nuclear Matrix / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism*; D051381:Rats; D011915:Rats, Inbred BUF
D006657:Histones; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D007633:Keratins