<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Xiong N</submitter><funding>the project of "Dengfeng plan" from Foshan Hospital of Traditional Chinese Medicine</funding><funding>Beijing Xisike Clinical Oncology Research Foundation</funding><funding>National Natural Science Foundation of China</funding><funding>Beijing Bethune Charitable Foundation</funding><funding>National Natural Science Foundation of Chongqing</funding><funding>Beijing Natural Science Foundation</funding><funding>National Key Research and Development of China</funding><pagination>e2411740</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11831497</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>12(7)</volume><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,</pubmed_abstract><journal>Advanced science (Weinheim, Baden-Wurttemberg, Germany)</journal><pubmed_title>N-glycosylation Modification of CTSD Affects Liver Metastases in Colorectal Cancer.</pubmed_title><pmcid>PMC11831497</pmcid><funding_grant_id>Y-bayer202001-0122</funding_grant_id><funding_grant_id>2022YFC3400801</funding_grant_id><funding_grant_id>2159000087</funding_grant_id><funding_grant_id>Z220014</funding_grant_id><funding_grant_id>7182171</funding_grant_id><funding_grant_id>82272841</funding_grant_id><funding_grant_id>62072435</funding_grant_id><funding_grant_id>202000205</funding_grant_id><funding_grant_id>92478117</funding_grant_id><funding_grant_id>82170801</funding_grant_id><funding_grant_id>CSTB2023NSCQ-MSX0131</funding_grant_id><pubmed_authors>Huang C</pubmed_authors><pubmed_authors>Yan Q</pubmed_authors><pubmed_authors>Xiong N</pubmed_authors><pubmed_authors>Wang C</pubmed_authors><pubmed_authors>Zhang H</pubmed_authors><pubmed_authors>Du Y</pubmed_authors><pubmed_authors>Ye Y</pubmed_authors><pubmed_authors>Yang C</pubmed_authors><pubmed_authors>Li Y</pubmed_authors><pubmed_authors>Zhao L</pubmed_authors><pubmed_authors>Shen Z</pubmed_authors><pubmed_authors>Sun Q</pubmed_authors><pubmed_authors>Wang S</pubmed_authors><pubmed_authors>Gao Z</pubmed_authors><pubmed_authors>Zhan J</pubmed_authors></additional><is_claimable>false</is_claimable><name>N-glycosylation Modification of CTSD Affects Liver Metastases in Colorectal Cancer.</name><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,</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Feb</publication><modification>2025-04-04T01:24:17.26Z</modification><creation>2025-04-04T01:24:17.26Z</creation></dates><accession>S-EPMC11831497</accession><cross_references><pubmed>39716927</pubmed><doi>10.1002/advs.202411740</doi></cross_references></HashMap>