Nuclear matrix of calreticulin in hepatocellular carcinoma.
Nuclear matrix protein profiles of malignant cells vary from their normal counterparts. By two-dimensional gel electrophoresis, we analyzed nuclear matrix proteins in 11 hepatocellular carcinomas and compared them with corresponding 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 Mr 62,000, which was identified to be calreticulin upon NH2-terminal amino acid sequencing. By immunoblotting, calreticulin was confirmed to be present abundantly in the nuclear matrix fraction of carcinomas but not in that of the nonmalignant liver tissue. Interestingly, the total content of calreticulin was similar between them. By immunofluorescence microscopy, evident nuclear immunostaining was detected in carcinomas. Calreticulin 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 calreticulin-nuclear matrix may be related to the activated cell growth.
Yoon
G S
GS
Department of Pathology, University of Ulsan College of Medicine and Asan Institute for Life Sciences, Seoul, Korea.
Lee
H
H
Jung
Y
Y
Yu
E
E
Moon
H B
HB
Song
K
K
Lee
I
I
D000328:Adult; D000368:Aged; D002135:Calcium-Binding Proteins / Q000032:analysis*; D037282:Calreticulin; D006528:Carcinoma, Hepatocellular / Q000737:chemistry*; D006801:Humans; D008113:Liver Neoplasms / Q000737:chemistry*; D008856:Microscopy, Fluorescence; D008875:Middle Aged; D015530:Nuclear Matrix / Q000737:chemistry*; D012261:Ribonucleoproteins / Q000032:analysis*
D002135:Calcium-Binding Proteins; D037282:Calreticulin; D012261:Ribonucleoproteins