Lectins and Cancer by N. Sharon (auth.), Priv.-Doz. Dr. Hans Joachim Gabius, Dr.

By N. Sharon (auth.), Priv.-Doz. Dr. Hans Joachim Gabius, Dr. Sigrun Gabius (eds.)

Molecular popularity certainly governs any point of mobile interplay. to appreciate tumor mobilephone progress legislation and unfold, analysisof protein carbohydrate interactions can give a contribution to guide to the institution of rational equipment for analysis and remedy. Chemically and biochemically optimized guidance of sufficient instruments, their program for localization of receptor (tissue lectin) and ligand (cellular glycoconjugate) pairs in tumor cells and tumor sections and the usefulness of a lectin from a plant extract as effective immunomodulator point out the possibility for a spot of such suggestions in pathology and oncology.

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After washing, anti-digoxigenin/peroxidase was added and the immunocomplexes were detected and quantified by adding the substrate o-phenylene diamine (containing hydrogen peroxide); after 4 min the reaction was stopped and the optical density determined at 490 nm. The EUSA test was used to determine the amount of gpl20 in the supernatant of HIV-l infected CEM cells at various periods of time after virus infection. As summarized in Table 5, 3 days p. i. RT activity could be measured in the culture supernatant indicating the release of virus particles into the medium.

2, lane c) and also other mannosylated proteins, for example HIV-gp-120 (Fig. 2, lane d). Therefore, La protein represents a self binding nuclear lectin-like protein. The sugar residues reside in the 29 kD fragment of the 43 kD- La prote in, wh i ch i s formed dur i ng a proteolytic degradation process of La protein (not shown). Analyzing the cDNA sequence of La prote in, pub 1i shed independent ly by severa 1 groups, one potential N-glycosylation site exists in this 29-kD region. Acknowledgements This work was supported by grants from the Bundesgesundheitsamt (AI 02 11032-87), the Bundesministerium für Forschung und Technologie (under the coordinat ion of the Kernforschungsan lage Jü 1ich; no.

3). On the basis of all this one could conclude that the lectins reveal complex tumor cell surface heterogeneity, reflecting their heterogenous functions and specialization. Several lectins were found to be reactive with tumors cell cytoplasm rather than with the cell membranes, although some reacted with both. Lectins that react with cytoplasm of tumor cells often reveal internal structural disorganization (Fig. 4). In better differentiated tumors the same lectin may, however, react exclusively with the Golgi apparatus.

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