{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xiong N"],"funding":["the project of \"Dengfeng plan\" from Foshan Hospital of Traditional Chinese Medicine","Beijing Xisike Clinical Oncology Research Foundation","National Natural Science Foundation of China","Beijing Bethune Charitable Foundation","National Natural Science Foundation of Chongqing","Beijing Natural Science Foundation","National Key Research and Development of China"],"pagination":["e2411740"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11831497"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(7)"],"pubmed_abstract":["Liver metastasis is the primary factor contributing to unfavorable prognosis in colorectal cancer (CRC). Although N-glycosylation is implicated in metastasis, there is a notable paucity of comprehensive studies addressing the N-glycosylation proteomics associated with liver metastasis in CRC. In this study, N-glycosylated proteins and N-glycosylation sites of differential expression between primary lesions and paired liver metastatic lesions are identified. Cathepsin D (CTSD) is further screened as a potentially pivotal N-glycosylated protein in CRC liver metastasis. Glycosyltransferases complex DDOST and STT3B can regulate N-glycosylation modification at residue 263 of CTSD (a protease), thereby affecting CTSD protease to lyse ACADM. ACADM can regulate ferroptosis-related proteins (ACSL4,"],"journal":["Advanced science (Weinheim, Baden-Wurttemberg, Germany)"],"pubmed_title":["N-glycosylation Modification of CTSD Affects Liver Metastases in Colorectal Cancer."],"pmcid":["PMC11831497"],"funding_grant_id":["Y-bayer202001-0122","2022YFC3400801","2159000087","Z220014","7182171","82272841","62072435","202000205","92478117","82170801","CSTB2023NSCQ-MSX0131"],"pubmed_authors":["Huang C","Yan Q","Xiong N","Wang C","Zhang H","Du Y","Ye Y","Yang C","Li Y","Zhao L","Shen Z","Sun Q","Wang S","Gao Z","Zhan J"],"additional_accession":[]},"is_claimable":false,"name":"N-glycosylation Modification of CTSD Affects Liver Metastases in Colorectal Cancer.","description":"Liver metastasis is the primary factor contributing to unfavorable prognosis in colorectal cancer (CRC). Although N-glycosylation is implicated in metastasis, there is a notable paucity of comprehensive studies addressing the N-glycosylation proteomics associated with liver metastasis in CRC. In this study, N-glycosylated proteins and N-glycosylation sites of differential expression between primary lesions and paired liver metastatic lesions are identified. Cathepsin D (CTSD) is further screened as a potentially pivotal N-glycosylated protein in CRC liver metastasis. Glycosyltransferases complex DDOST and STT3B can regulate N-glycosylation modification at residue 263 of CTSD (a protease), thereby affecting CTSD protease to lyse ACADM. ACADM can regulate ferroptosis-related proteins (ACSL4,","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2025-04-04T01:24:17.26Z","creation":"2025-04-04T01:24:17.26Z"},"accession":"S-EPMC11831497","cross_references":{"pubmed":["39716927"],"doi":["10.1002/advs.202411740"]}}