This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Burrus, G. R. Articles by Briggs, R. C. Search for Related Content PubMed PubMed Citation Articles by Burrus, G. R. Articles by Briggs, R. C.

Lectin-binding Proteins in Nuclear Preparations from Rat Liver and Malignant Tumors¹

Departments of Pathology [G. R. B, W. N. S., L. S. H., and R. C.B.] and Biochemistry [W. N. S., J. A. B., L. S. H., and R. C. B.], the A. B. Hancock, Jr., Memorial Laboratory of the Vanderbilt University Cancer Center, and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

Lectin binding [concanavalin A, biotinylated ricinus communis agglutinin, and biotinylated succinylated wheat germ agglutinin (B-SWGA)] was used to detect the glycosylated proteins associated with a residual protein fraction [insoluble in 4% sodium dodecyl sulfate and termed the nuclear residual fraction (NRF)] or with nuclear matrix preparations from normal rat liver, azo dye (3'-MeDAB)-induced rat hepatoma, and Walker 256 transplantable carcinosarcoma. One- and two-dimensional gel electrophoresis were used with lectins, polyclonal antisera, and monoclonal antibody binding to characterize some of the glycoconjugates. Two polypeptide bands with approximate molecular weights of 95,000 and 55,000, shown previously to be present only in the induced tumor cells and the Walker 256 tumor, were reactive with lectins. In addition, a M_r 62,000 protein reacted only with B-SWGA in the nuclear matrix fractions from normal rat liver and the induced hepatoma. A polypeptide band (approximate molecular weight, 213,000) in the Walker 256 NRF reacted with concanavalin A and biotinylated ricinus communis agglutinin. One polypeptide band (approximate molecular weight, 182,000) reacted with concanavalin A in all three tissues, with biotinylated ricinus communis agglutinin and B-SWGA in the Walker NRF, and with B-SWGA in the hepatoma NRF. Another polypeptide band (approximate molecular weight, 138,000), reactive with all three lectins, was present in all three tissues. Our findings are consistent with previous reports of lectin binding proteins in the eukaryotic cell nucleus and indicate that certain glycoproteins isolated in nuclear preparations are found specifically in 3'-MeDAB-induced hepatoma and Walker 256 transplantable carcinosarcoma.

¹ Supported by National Cancer Institute Grant CA 26412.

² To whom requests for reprints should be addressed, at Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232.

Received 4/17/87. Revised 8/20/87. Accepted 10/23/87.