Roles of glycosaminoglycans and glycanmimetics in tumor progression and metastasis

Basappa and Rangappa, K. S. and Sugahara, K. (2014) Roles of glycosaminoglycans and glycanmimetics in tumor progression and metastasis. Glycoconjugate Journal, 31 (6). pp. 461-467. ISSN 0282-0080

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Abstract

Various tumor cells exhibit structural alterations in the sulfated modifications to glycosaminoglycans (GAGs). The altered expression of chondroitin sulfate (CS) and heparan sulfate (HS) on the surfaces of tumor cells is known to play a key role in malignant transformation and tumor metastasis. The receptor molecule for the CS chains containing Edisaccharide units (CS-E) expressed on Lewis lung carcinoma (LLC) cells was recently revealed to be Receptor for Advanced Glycation End-products (RAGE). RAGE is also involved in the development of various pathological conditions including aging, infection, pulmonary fibrosis, diabetes, and Alzheimer's disease, by binding to a wide range of ligands. RAGE binds strongly not only to CS-E, but also to HS-expressing LLC cells. Recombinant RAGE bound CS-E and HS with high affinity. Furthermore, in a mouse model, the colonization of the lungs by LLC cells was inhibited by intravenously injected CS-E, an anti-CS-E antibody, or an anti-RAGE antibody. These findings demonstrated that RAGE is at least one of the critical receptors for CS and HS chains expressed on the tumor cell surface and is involved in experimental lung metastasis, and also that CS/HS and RAGE are potential molecular targets for the treatment of pulmonary metastasis. We, hence, reviewed these findings and also several chemically synthesized small GAGmimetics that exhibit potent anti-metastatic and/or anti-tumor activities. © Springer Science+Business Media New York 2014.

Item Type:	Article
Uncontrolled Keywords:	animal model, antiangiogenic activity, antineoplastic activity, antineoplastic agent, Article, controlled study, drug synthesis, mouse, nonhuman, unclassified drug, animal cell, 7, ligand binding, metabolism, pathology, protein expression, tumor growth, priority journal, drug design, enzyme activity, 5, neoplasm, binding affinity, cell proliferation, surface plasmon resonance, amino acid sequence, protein function, signal transduction, polysaccharide, molecular mimicry, Neoplasms, Disease Progression, protein binding, chondroitin sulfate, binding site, oxazine derivative, disease course, tumor cell, liver metastasis, Molecular Mimicry, vasculotropin, Polysaccharides, 2 2, 2 3 nitro 4 phenylthiobenzoylbenzoic acid, 2 butyl 5 chloro 3 4 nitro benzyl 3h imidazole 4 carbaldehyde, 3oxazine, 5 3 4 chlorophenyl 4, 5 dihydroisoxazol 5 yl methyl 5h dibenzo b, 6, 6 difluorophenyl 4a, 8, 8a hexahydro 4a 4 methoxyphenyl 4h benzoe1, advanced glycation end product receptor, dermatan sulfate, dibenzazepine derivative, disaccharide, f azepine, fibroblast growth factor 2, glycanmimetic, glycosaminoglycan, Glycosaminoglycans, heparan sulfate, heparanase, heparin binding epidermal growth factor, imidazole, Lewis lung carcinoma cell, lung metastasis, malignant transformation, metastasis, metastasis potential, Neoplasm Metastasis, protein modification
Subjects:	C Chemical Science > Chemistry
Divisions:	Department of > Chemistry
Depositing User:	Arshiya Kousar Library Assistant
Date Deposited:	15 Jun 2019 09:57
Last Modified:	15 Jun 2019 09:57
URI:	http://eprints.uni-mysore.ac.in/id/eprint/3055

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