Author
Joo, E.J.; Hui, Y.; Park, Y.; Park, N.Y.; Toida, T.; Linhardt, Robert J.; Kim, Y.S.
Other Contributors
Date Issued
2010
Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Degree
Terms of Use
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Full Citation
Induction of nucleolin translocation by acharan sulfate in A549 cells, E. J. Joo, Y. Hui, Y. Park, N. Y. Park, T. Toida, R. J. Linhardt, Y.S. Kim, Journal of Cellular Biochemistry, 110, 1272–1278, 2010.
Abstract
Acharan sulfate (AS), isolated from the giant African snail Achatina fulica, is a novel glycosaminoglycan, consisting primarily of the repeating disaccharide structure α-D-N-acetylglucosaminyl (1 → 4) 2-sulfoiduronic acid. AS shows anti-tumor activity in vitro and in vivo. Despite this activity, AS is only weakly cytotoxic towards cancer cells. We examine the interactions between AS and cell-surface proteins in an effort to explain this anti-tumor activity. Using flow cytometry and affinity column chromatography, we confirm that AS has strong affinity to specific cell-surface proteins including nucleolin (NL) in A549 human lung adenocarcinomas. Surprisingly, we found the translocation of NL from nucleus to cytoplasm under the stimulation of AS (100 µg/ml) in vitro. Also, as NL exits the nucleus, the levels of growth factors such as bFGF and signaling cascade proteins, such as p38, p53, and pERK, are altered. These results suggest that the communication between AS and NL plays a critical role on signal transduction in tumor inhibition.;
Description
Journal of Cellular Biochemistry, 110, 1272–1278; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
Relationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;
Access
https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1002/jcb.22643;