title: Anguilla japonica lectin 1 delivery through adenovirus vector induces apoptotic cancer cell death through interaction with PRMT5.
abstract: BACKGROUND
  Our previous studies have demonstrated that, through adenovirus mediated gene delivery, various exogenously expressed lectins elicited cytotoxicity to cancer cells, utilizing protein arginine methyltransferase 5 (PRMT5) as a common binding target.
  
  
  METHODS
  In the present study, a FLAG tagged Anguilla japonica lectin 1 (AJL1) expression cassette was genetically harbored in a replication-defective adenovirus genome, forming Ad.FLAG-AJL1. The exogenous AJL1-induced cytotoxicity and the underlying mechanisms were analyzed.
  
  
  RESULTS
  The exogenous AJL1 suppressed the proliferation of a variety of human cancer cells by inducing apoptosis. Caspase 9, Bcl-2, X-linked inhibitor of apoptosis protein, mitogen-activated protein kinase kinase 1/2-extracellular signal-regulated kinase and p38 mitogen-activated protein kinase were found to be responsible for the exogenous AJL1-induced cytotoxicity. AJL1 was further suggested to regulate PRMT5-E2F-1 pathway, a pathway shared by previously reported marine lectins Dicentrarchus labrax fucose binding lectin and Strongylocentrotus purpuratus rhamnose binding lectin. A localization study revealed that exogenous AJL1 widely distributed in the cell membrane and cytoplasm.
  
  
  CONCLUSIONS
  The results of the present study suggest that the PRMT5-E2F-1 pathway may act as a common target for exogenous lectins including AJL1, and the cellular response to exogenous AJL1 may suggest a novel agent for cancer gene therapy. Copyright © 2016 John Wiley & Sons, Ltd.
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou, Zhejiang, China.
authors.forename: Gongchu
authors.initials: G
authors.lastname: Li
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou, Zhejiang, China.
authors.forename: Yajun
authors.initials: Y
authors.lastname: Gao
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou, Zhejiang, China.
authors.forename: Lianzhen
authors.initials: L
authors.lastname: Cui
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou, Zhejiang, China.
authors.forename: Liqin
authors.initials: L
authors.lastname: Wu
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou, Zhejiang, China.
authors.forename: Xinyan
authors.initials: X
authors.lastname: Yang
authors.affiliation: Institute of Life Sciences, College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, China.
authors.forename: Jing
authors.initials: J
authors.lastname: Chen
mesh_terms: D000072283:A549 Cells; D000256:Adenoviridae / Q000235:genetics; D000811:Anguilla / Q000378:metabolism; D000818:Animals; D017209:Apoptosis / Q000235:genetics*; D051017:Apoptosis Regulatory Proteins / Q000378:metabolism; D045744:Cell Line, Tumor; D002470:Cell Survival / Q000235:genetics; D050687:E2F1 Transcription Factor / Q000235:genetics / Q000378:metabolism; D029941:Fish Proteins / Q000235:genetics* / Q000378:metabolism; D018014:Gene Transfer Techniques; D006801:Humans; D037102:Lectins / Q000235:genetics* / Q000378:metabolism; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D011485:Protein Binding; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics* / Q000378:metabolism; D015398:Signal Transduction / Q000235:genetics
chemical_list: D051017:Apoptosis Regulatory Proteins; D050687:E2F1 Transcription Factor; C493753:E2F1 protein, human; D029941:Fish Proteins; D037102:Lectins; C400529:PRMT5 protein, human; D011484:Protein-Arginine N-Methyltransferases; D020928:Mitogen-Activated Protein Kinases
keywords: Anguilla japonica lectin 1; E2F-1; PRMT5; apoptosis; cancer