Lactose-Functionalized Dendrimers Arbitrate the Interaction of Galectin-3/MUC1 Mediated Cancer Cellular Aggregation
| Autor: | Anna K. Michel, Avrahamx Raz, Mary J. Cloninger, Pratima Nangia-Makker |
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| Rok vydání: | 2014 |
| Předmět: |
Dendrimers
Galectin 3 Lactose Plasma protein binding Biochemistry Article Cell Line Tumor Neoplasms Dendrimer Protein Interaction Mapping medicine Humans Antigens Tumor-Associated Carbohydrate Protein Interaction Maps Molecular Biology MUC1 Chemistry Ligand Mucin-1 Organic Chemistry Cancer Carbohydrate medicine.disease Cell culture Cancer cell Molecular Medicine Protein Binding |
| Zdroj: | ChemBioChem. 15:2106-2112 |
| ISSN: | 1439-4227 |
| DOI: | 10.1002/cbic.201402134 |
| Popis: | By using lactose-functionalized poly(amidoamine) dendrimers as a tunable multivalent platform, we studied cancer cell aggregation in three different cell lines (A549, DU-145, and HT-1080) with galectin-3. We found that small lactose-functionalized G(2)-dendrimer 1 inhibited galectin-3-induced aggregation of the cancer cells. In contrast, dendrimer 4 (a larger, generation 6 dendrimer with 100 carbohydrate end groups) caused cancer cells to aggregate through a galectin-3 pathway. This study indicates that inhibition of cellular aggregation occurred because 1 provided competitive binding sites for galectin-3 (compared to its putative cancer cell ligand, TF-antigen on MUC1). Dendrimer 4, in contrast, provided an excess of ligands for galectin-3 binding; this caused crosslinking and aggregation of cells to be increased. |
| Databáze: | OpenAIRE |
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