A Tn antigen binding lectin from Myrsine coriacea displays toxicity in human cancer cell lines.

Abstract : The Tn antigen (GalNAc-O-Ser/Thr) is one of the most specific human cancer-associated structures. In the present study we characterize the biochemical and functional properties of the Myrsine coriacea lectin (McL). We show that McL is an unusual high molecular weight highly glycosylated protein, which displays a strong Tn binding activity. The lectin exhibits in vitro inhibition of proliferation in the six cancer cell lines evaluated, in a dose-dependent manner (the strongest activity being against HT-29 and HeLa cells), whereas it does not exhibit toxicity against normal lymphocytes. McL could be exploited in the design of potential new tools for the diagnosis or treatment of cancer.
Document type :
Journal articles
Complete list of metadatas

Cited literature [46 references]  Display  Hide  Download

https://hal-riip.archives-ouvertes.fr/pasteur-00839289
Contributor : Mariella Botta <>
Submitted on : Thursday, June 27, 2013 - 4:10:07 PM
Last modification on : Friday, February 22, 2019 - 11:16:44 AM
Long-term archiving on : Wednesday, April 5, 2017 - 4:26:15 AM

File

 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document

Identifiers

Collections

Citation

Andrea Medeiros, Nora Berois, Marcelo Incerti, Sylvie Bay, Laura Franco Fraguas, et al.. A Tn antigen binding lectin from Myrsine coriacea displays toxicity in human cancer cell lines.. Journal of Natural Medicines, Springer Verlag, 2013, 67 (2), pp.247-54. ⟨10.1007/s11418-012-0671-x⟩. ⟨pasteur-00839289⟩

Share

Metrics

Record views

174