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Ulva pertusa lectin 1 delivery through adenovirus vector affects multiple signaling pathways in cancer cells

Li, Gongchu ; Zhao, Zhenzhen ; Wu, Bingbing ; Su, Qunshu ; Wu, Liqin ; Yang, Xinyan ; Chen, Jing

Glycoconjugate journal, 2017-08, Vol.34 (4), p.489-498 [Periódico revisado por pares]

New York: Springer US

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Título:
Ulva pertusa lectin 1 delivery through adenovirus vector affects multiple signaling pathways in cancer cells
Autor: Li, Gongchu ; Zhao, Zhenzhen ; Wu, Bingbing ; Su, Qunshu ; Wu, Liqin ; Yang, Xinyan ; Chen, Jing
Assuntos: 1-Phosphatidylinositol 3-kinase ; Actin ; Adenoviridae - genetics ; Adenoviruses ; AKT protein ; Algae ; Arginine ; Autophagy - drug effects ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Cancer ; Cell Line, Tumor ; Cell Proliferation ; Cell survival ; Cells ; Cytoskeleton ; Cytotoxicity ; Enzyme inhibitors ; Expression vectors ; Extracellular signal-regulated kinase ; Genetic Vectors - metabolism ; Glucosamine ; Hepatocytes ; Humans ; Inhibition ; Inhibitors ; Intracellular signalling ; Intracellular Space - metabolism ; Kinases ; Lectins ; Lectins - metabolism ; Life Sciences ; Liver ; Liver cancer ; MAP kinase ; Mitogen-Activated Protein Kinase Kinases - metabolism ; Molecular weight ; N-Acetylglucosamine ; Original Article ; p38 Mitogen-Activated Protein Kinases - metabolism ; Pathology ; Phagocytosis ; Phosphatidylinositol 3-Kinases - metabolism ; Phosphorylation ; Protein arginine methyltransferase ; Protein kinase ; Proteins ; ras Proteins - metabolism ; Signal Transduction ; Starvation ; Subcellular Fractions - metabolism ; Survival ; Tubulin - metabolism ; Tumor cell lines ; Ulva - metabolism
É parte de: Glycoconjugate journal, 2017-08, Vol.34 (4), p.489-498
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: Ulva pertusa lectin 1 (UPL1) is a N -acetyl-D-glucosamine (GlcNAc) binding lectin in marine green alga Ulva pertusa . Exogenous UPL1 colocalized with protein arginine methyltransferase 5 (PRMT5), methylosome protein 50 (MEP50), β-actin and β-tubulin, indicating the interaction of UPL1 with the methylosome and cytoskeleton. UPL1 delivery through adenovirus vector (Ad-UPL1) dramatically induced extracellularly regulated protein kinases 1/2 (ERK1/2) phosphorylation in liver cancer cell lines BEL-7404 and Huh7. Signaling pathways including p38 mitogen-activated protein kinase (MAPK), and Akt were also affected by Ad-UPL1 in a cell type dependent manner. MEK1/2 inhibitor U0126, as well as to a lesser extent p38 MAPK inhibitor SB203580 and phosphoinositide 3-kinase (PI3K) inhibitor LY294002, completely eliminated a higher molecular weight isoform of β-tubulin induced by Ad-UPL1, and significantly enhanced the cytotoxicity of Ad-UPL1 in Huh7 cells, suggesting that the inhibition of MEK1/2, p38 MAPK, and PI3K enhanced antiproliferative effect of Ad-UPL1 possibly through regulating the modification of β-tubulin. Ad-UPL1 completely inhibited the expression of autophagy-related factor Beclin1, but induced LC3-II expression in Huh7 cells. In addition, Ad-UPL1 significantly enhanced starvation induced survival suppression in Huh7 cells. Our data elucidated intracellular signaling pathways affected by exogenous UPL1, and may provide insights into a novel way of UPL1 delivery through adenovirus vectors combined with survival signaling inhibitors for cancer treatment.
Editor: New York: Springer US
Idioma: Inglês

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Ulva pertusa lectin 1 delivery through adenovirus vector affects multiple signaling pathways in cancer cells

Li, Gongchu ; Zhao, Zhenzhen ; Wu, Bingbing ; Su, Qunshu ; Wu, Liqin ; Yang, Xinyan ; Chen, Jing

New York: Springer US

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