TY - JOUR
T1 - Structural characterization of two isolectins from the marine red alga Solieria filiformis (Kützing) P.W. Gabrielson and their anticancer effect on MCF-7 breast cancer cells
AU - Chaves, Renata Pinheiro
AU - Silva, Suzete Roberta da
AU - Nascimento Neto, Luiz Gonzaga
AU - Carneiro, Romulo Farias
AU - Silva, André Luis Coelho da
AU - Sampaio, Alexandre Holanda
AU - Sousa, Bruno Lopes de
AU - Cabral, Maria Guadalupe
AU - Videira, Paula Alexandra
AU - Teixeira, Edson Holanda
AU - Nagano, Celso Shiniti
PY - 2018/2
Y1 - 2018/2
N2 - As described in the literature, Solieria filiformis lectin (SfL) from the marine red alga S. filiformis was found to have antinociceptive and anti-inflammatory effects. In this study, we characterized two SfL variants, SfL-1 and SfL-2, with molecular mass of 27,552Da and 27,985Da, respectively. The primary structures of SfL-1 and SfL-2 consist of four tandem-repeat protein domains with 67 amino acids each. SfL-1 and -2 showed high similarity to OAAH-family lectins. 3D structure prediction revealed that SfL-1 and -2 are composed of two β-barrel-like domains formed by five antiparallel β-strands, which are connected by a short peptide linker. Furthermore, the mixture of isoforms (SfLs) showed anticancer effect against MCF-7 cells. Specifically, SfLs inhibited 50% of viability in MCF-7 cells after treatment at 125μg.mL-1, while the inhibition of Human Dermal Fibroblasts (HDF) was 34% with the same treatment. Finally, 24h after treatment, 25% of MCF-7 cells were in early apoptosis and 35% in late apoptosis. Evaluation of pro- and anti-apoptotic gene expression of MCF-7 cells revealed that SfLs induced caspase-dependent apoptosis within 24h.
AB - As described in the literature, Solieria filiformis lectin (SfL) from the marine red alga S. filiformis was found to have antinociceptive and anti-inflammatory effects. In this study, we characterized two SfL variants, SfL-1 and SfL-2, with molecular mass of 27,552Da and 27,985Da, respectively. The primary structures of SfL-1 and SfL-2 consist of four tandem-repeat protein domains with 67 amino acids each. SfL-1 and -2 showed high similarity to OAAH-family lectins. 3D structure prediction revealed that SfL-1 and -2 are composed of two β-barrel-like domains formed by five antiparallel β-strands, which are connected by a short peptide linker. Furthermore, the mixture of isoforms (SfLs) showed anticancer effect against MCF-7 cells. Specifically, SfLs inhibited 50% of viability in MCF-7 cells after treatment at 125μg.mL-1, while the inhibition of Human Dermal Fibroblasts (HDF) was 34% with the same treatment. Finally, 24h after treatment, 25% of MCF-7 cells were in early apoptosis and 35% in late apoptosis. Evaluation of pro- and anti-apoptotic gene expression of MCF-7 cells revealed that SfLs induced caspase-dependent apoptosis within 24h.
KW - Anticancer effect
KW - Lectin
KW - Marine alga
UR - http://www.scopus.com/inward/record.url?scp=85030668513&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2017.09.116
DO - 10.1016/j.ijbiomac.2017.09.116
M3 - Article
C2 - 28970169
AN - SCOPUS:85030668513
VL - 107
SP - 1320
EP - 1329
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
ER -