Structural analysis of Dioclea lasiocarpa lectin: A C6 cells apoptosis-inducing protein.

Autor: Nascimento KS; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil., Santiago MQ; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil., Pinto-Junior VR; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil., Osterne VJS; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil., Martins FWV; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil., Nascimento APM; Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil., Wolin IAV; Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil., Heinrich IA; Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil., Martins MGQ; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil., Silva MTL; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil., Lossio CF; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil., Rocha CRC; Universidade Federal de Pernambuco (UFPE), Recife, Pernambuco, Brazil., Leal RB; Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil. Electronic address: rbleal@gmail.com., Cavada BS; Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil. Electronic address: bscavada@ufc.br.
Jazyk: angličtina
Zdroj: The international journal of biochemistry & cell biology [Int J Biochem Cell Biol] 2017 Nov; Vol. 92, pp. 79-89. Date of Electronic Publication: 2017 Sep 20.
DOI: 10.1016/j.biocel.2017.09.014
Abstrakt: Lectins are multidomain proteins that specifically recognize various carbohydrates. The structural characterization of these molecules is crucial in understanding their function and activity in systems and organisms. Most cancer cells exhibit changes in glycosylation patterns, and lectins may be able to recognize these changes. In this work, Dioclea lasiocarpa seed lectin (DLL) was structurally characterized. The lectin presented a high degree of similarity with other lectins isolated from legumes, presenting a jelly roll motif and a metal-binding site stabilizing the carbohydrate-recognition domain. DLL demonstrated differential interactions with carbohydrates, depending on type of glycosidic linkage present in ligands. As observed by the reduction of cell viability in C6 cells, DLL showed strong antiglioma activity by mechanisms involving activation of caspase 3.
(Copyright © 2017 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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