Nuclear matrix protein profiles of malignant cells vary from their normal c
ounterparts. By two-dimensional gel electrophoresis, we analyzed nuclear ma
trix proteins in 11 hepatocellular carcinomas and compared them with corres
ponding non-neoplastic liver tissue, Although the compositions were mostly
similar, several peptides were noted predominantly in the former, The most
prominent one was an acidic protein of apparent M-r 62,000, which was ident
ified to be calreticulin upon NH2-terminal amino acid sequencing, By immuno
blotting, calreticulin was confirmed to be present abundantly in the nuclea
r matrix fraction of carcinomas but not in that of the nonmalignant liver t
issue. Interestingly, the total content of calreticulin was similar between
them. By immunofluorescence microscopy, evident nuclear immunostaining was
detected in carcinomas. Cal-reticulin was also found to be in the nuclear
matrices of various carcinoma cell lines. We conclude that calreticulin Is
a component of the nuclear matrix. The formation and/or expansion of the ca
lreticulin-nuclear matrix may be related to the activated cell growth.