{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Shisheng Sun"],"species":["Mus Musculus"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0009722000"],"submitter_email":["suns@nwu.edu.cn"],"submitter_affiliation":["Northwest University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["Ovarian aging typically precedes the decline of other organ systems, yet its molecular mechanisms remain poorly understood. Glycosylation as one of the most important protein modifications has been especially unexplored in this context. Here, we present the first high-resolution glycoproteomic landscape of aging mouse ovaries, uncovering site-specific N-glycan signatures across subcellular components such as high proportions of complex glycans, core fucosylation, and LacdiNAc branches at the zone pellucida. We report three major glycosylation alterations in aged ovaries: the frequently changed core-fucosylation associated with cell adhesion and immune responses, the decreased LacdiNAc glycans on zona pellucida (ZP) responsible for fertility decline, and the increased sialylated glycans modified by Neu5Ac and Neu5Gc playing different roles in immune activation and responses. Integrated multi-omic analyses further highlight the unique role of glycosylation, distinct from phosphorylation, in regulating key signaling pathways, antigen processing and presentation, complement coagulation cascades, ROS biosynthetic and metabolic processes, as well as cell death. This study offers a novel glycobiological perspective on ovarian aging, broadening our understanding of its molecular mechanisms beyond traditional multi-omic approaches."],"pubmed_title":["A high-resolution N-glycoproteome landscape of aging mouse ovary."],"pubmed_authors":["Wu Yongqi Y, Zhang Zhida Z, Xu Yongchao Y, Zhang Yingjie Y, Chen Lin L, Zhang Yiwen Y, Hou Ke K, Yang Muyao M, Jin Zhehui Z, Cai Yinli Y, Zhao Jiayu J, Sun Shisheng S"],"name_synonyms":["gonad of female reproductive system, determination, Laboratory, gonada of reproductive system of female organism, gonad of female organism reproductive system, gonada of female reproductive system, Mus domesticus, number, mouse, genitalia of female organism gonada., presence, House Mouse, gonada of female organism genitalia, count in organism, gonad of genitalia of female organism, House, Mus, Ovaries, chemical analysis, Mus musculus domesticus, Mice, female reproductive system gonad, Mus musculus, ovaries, female organism reproductive system gonada, gonada of female organism reproductive system, animal ovary, gonada of genitalia of female organism, Swiss, mice, genitalia of female organism gonad, ovum-producing ovary, Swiss Mouse, female gonad, ovarium, gonad of reproductive system of female organism, female organism reproductive system gonad, House Mice, Swiss Mice, gonad of female organism genitalia, domesticus, Laboratory Mice, reproductive system of female organism gonada, female organism genitalia gonada, reproductive system of female organism gonad, ovary - animal, ovary, Mouse, assay, house mouse, female organism genitalia gonad, Laboratory Mouse, female reproductive system gonada, Elderly"],"pubmed_abstract_synonyms":["Panomics, vitelline envelope, Metabolic Process, O-linked Glycosylations, Laboratory, Galactosylation, Mus domesticus, Metabolic Concepts, Galactosylations, Progress Reports, Aging, House Mouse, phosphorylation, element, gonada of female organism genitalia, 2-acetamido-4-O-(2-acetamido-2-deoxygalactopyranosyl)-2-deoxyglucopyranose, World Fertility Survey, Fertility Preferences, Readability, Neu5Ac, Roles, Biological, Below Replacement, Summary Report, Concepts, N'-diacetyllactosediamine, Metabolism Concept, Phenomenon, Summary Reports, Fertility Surveys, IKKg, KEY, Key, genitalia of female organism gonada, organ, Senescence, Fertility Incentives, Immune Processes, Immune Responses, Glycans, Progress Report, Natural, N, ovum-producing ovary, N-Acetylglucosaminylation, female organism reproductive system gonad, Swiss Mice, Sialylation, c-ros-1, Progress, Biological Aging, Adhesions, Immune, reproductive system of female organism gonada, Field Reports, O-linked, Adhesion, Glycan, Role Concepts, Fertility Determinant, Fertility Preference, GalNAc-1-4-GlcNAc, necrosis, house mouse, CG5232, Catabolism, Differential Fertility, N-Acetylglucosaminylations, single organism signaling, antigen presentation, Process, gonada of reproductive system of female organism, gonad of female organism reproductive system, World Fertility Surveys, mouse, Glycosylations, antigen processing, Fucosylations, DmIKKgamma, Role Concept, Investigative Report, Phosphoglycosylations, Ovaries, dIKK, Kenny, Role, female reproductive system gonad, region, activation, Integrative Omics., Mus musculus, DmelCG5232, Multi Omics, clotting, striated membrane, gonada of genitalia of female organism, Complement, mice, N linked Glycosylation, Swiss Mouse, Field, IKK-gamma, gonad of reproductive system of female organism, Integrative, Sialylations, m. vitellina, Preferences, domesticus, Fertility Determinants, pellucid zone, Report, DmelCG16910, MCF3, female organism genitalia gonada, N Acetylglucosaminylation, Surveys, Complement System, Mouse, Fecundability, Elderly, Marital Fertility, Subfecundity, GlcNAcylation, Processes, yolk sac membrane, Fertility, N-linked Glycosylations, Metabolic Processes, Complement Protein, dIKK-gamma, Multi-Omics, N-linked, O-linked Glycosylation, gonad of genitalia of female organism, Determinant, Investigative, glycosylation, Glycosylation, House, Metabolism, DmIKK-gamma, Mus musculus domesticus, Survey, single organism cell adhesion, Preference, World Fertility, dmIKKgamma, IKK[[gamma]], Mice, Metabolism Phenomena, Polysaccharide, Fecundity, lacdiNAc, study, gonada of female organism reproductive system, Protein Glycosylations, Swiss, genitalia of female organism gonad, cell adhesion molecule activity, Metabolic Concept, Omics, Immune Response, IKK, reproductive system of female organism gonad, anatomical unit, Phosphoglycosylation, Below Replacement Fertility, body organ, accidental cell death, ovary - animal, ovary, site, Pan-Omics, Hemolytic, zona pellucida - vitelline membrane, Fertility Incentive, Fucosylation, Investigative Reports, female organism genitalia gonad, Immune Process, female reproductive system gonada, N-linked Glycosylation, Integrative-Omics, gonad of female reproductive system, Protein Glycosylation, World, DmSAS, gonada of female reproductive system, Proteins, zona radiata, Phosphorylations, vitelline membrane, oolemma, Integrative Omics, Cell, Concept, Metabolic Phenomena, O linked Glycosylation, IKKgamma, Metabolism Concepts, Mus, Protein, Research Reports, Phenomena, Multi-Omic, core, Natural Fertility, Pan Omics, GlcNAcylations, zona pellucida, Hemolytic Complement, ROS, Determinants, Death, Metabolic Phenomenon, ovaries, female organism reproductive system gonada, SAS, animal ovary, Metabolic, Dmikkgamma, female gonad, ovarium, House Mice, gonad of female organism genitalia, Cell Adhesions, Understanding, CG16910, Laboratory Mice, Complement Proteins, Differential, sas, signalling process, Reports, Marital, Response, zona striata, Summary, Laboratory Mouse, Field Report, Fertility Survey, Anabolism"],"pubmed_title_synonyms":["gonad of female reproductive system, Laboratory, gonada of reproductive system of female organism, gonad of female organism reproductive system, gonada of female reproductive system, Mus domesticus, mouse, Aging, genitalia of female organism gonada., House Mouse, gonada of female organism genitalia, gonad of genitalia of female organism, House, Mus, Biological, Ovaries, Mus musculus domesticus, Mice, female reproductive system gonad, Senescence, Mus musculus, ovaries, female organism reproductive system gonada, gonada of female organism reproductive system, animal ovary, gonada of genitalia of female organism, Swiss, mice, genitalia of female organism gonad, ovum-producing ovary, Swiss Mouse, female gonad, ovarium, gonad of reproductive system of female organism, female organism reproductive system gonad, House Mice, Swiss Mice, gonad of female organism genitalia, domesticus, Laboratory Mice, Biological Aging, reproductive system of female organism gonada, female organism genitalia gonada, reproductive system of female organism gonad, ovary - animal, ovary, Mouse, house mouse, female organism genitalia gonad, Laboratory Mouse, female reproductive system gonada"],"description_synonyms":["joint, biological signaling, joints, O-linked Glycosylations, GlcNAcylation, Protein Glycosylation, determination, Laboratory, Galactosylation, Mus domesticus, mouse, FBN, Galactosylations, Glycosylations, N-linked Glycosylations, House Mouse, Fucosylations, Mdu, CG11121, ACMICD, O linked Glycosylation, N-linked, TPSG1, S-adenosyl-L-methionine:thiol S-methyltransferase activity, O-linked Glycosylation, old, glycosylation, Glycosylation, Phosphoglycosylations, DmelCG11121, House, Mus, mda, ECTOL1, Joint, Protein, Mus musculus domesticus, GlcNAcylations, MFS1, Mice, region, ami, WMS, WMS2, Mus musculus, covalent modifier, somda, articulation, Protein Glycosylations, Swiss, med, mice, N linked Glycosylation, Swiss Mouse, Tissue, N-Acetylglucosaminylation, Sialylations, chemical analysis., House Mice, Swiss Mice, labeling, MASS, SO, Sialylation, signalling, domesticus, Laboratory Mice, OCTD, signalling process, N Acetylglucosaminylation, Phosphoglycosylation, O-linked, signaling process, SSKS, PRSS31, articular joint, site, Mouse, assay, house mouse, Fucosylation, GPHYSD2, TMT, Laboratory Mouse, TAG, N-Acetylglucosaminylations, So, N-linked Glycosylation, Elderly, thiol methyltransferase activity, SGS, single organism signaling, Drl"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative glycoproteomic, proteomic, and phosphoproteomic analysis of aged mouse ovary","description":"In this work, we investigate the differences of site-specific N-glycosylation between young (2-month-old) and middle-aged (12-month-old) mouse ovarian tissues by integrating N-glycoproteomics and proteomic approaches with tandem mass tag (TMT) labeling.To identify signalling pathways associated with glycosylation, we integrated the phosphoproteome for joint analysis.","dates":{"publication":"Sat Sep 14 00:00:00 GMT+01:00 2024"},"accession":"PXD056126","cross_references":{"TAXONOMY":["10090"],"pubmed":["40073759"]}}