{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7"],"submitter":["Luo C"],"pubmed_abstract":["Pertuzumab is an antihuman HER2 antibody developed for HER2 positive breast cancer. Glycosylation profiles are always the important issue for antibody based therapy. Previous findings have suggested the impact of glycosylation profiles on the function of antibodies, like pharmacodynamics, antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC). However, the roles of fucose and sialic acid in the function of therapeutic antibodies still need further investigation, especially the role of sialic acid in nonfucosylated antibodies. This study focused on the pharmacokinetic and pharmacodynamic properties of pertuzumab after glycoengineering. Herein, nonfucosylated pertuzumab was produced in CHO<sup>FUT8-/-</sup> cells, and desialylated pertuzumab was generated"],"journal":["Scientific reports"],"pagination":["46347"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5387714"],"repository":["biostudies-literature"],"pubmed_title":["Glycoengineering of pertuzumab and its impact on the pharmacokinetic/pharmacodynamic properties."],"pmcid":["PMC5387714"],"pubmed_authors":["Xu N","Li YC","Wang C","Tian H","Gao XD","Zhao W","Sai WB","Hu XJ","Luo C","Chen S","Yao WB"],"additional_accession":[]},"is_claimable":false,"name":"Glycoengineering of pertuzumab and its impact on the pharmacokinetic/pharmacodynamic properties.","description":"Pertuzumab is an antihuman HER2 antibody developed for HER2 positive breast cancer. Glycosylation profiles are always the important issue for antibody based therapy. Previous findings have suggested the impact of glycosylation profiles on the function of antibodies, like pharmacodynamics, antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC). However, the roles of fucose and sialic acid in the function of therapeutic antibodies still need further investigation, especially the role of sialic acid in nonfucosylated antibodies. This study focused on the pharmacokinetic and pharmacodynamic properties of pertuzumab after glycoengineering. Herein, nonfucosylated pertuzumab was produced in CHO<sup>FUT8-/-</sup> cells, and desialylated pertuzumab was generated","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Apr","modification":"2025-04-05T12:12:59.832Z","creation":"2019-03-27T02:41:01Z"},"accession":"S-EPMC5387714","cross_references":{"pubmed":["28397880"],"doi":["10.1038/srep46347"]}}