{"database":"JPOST Repository","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["https://storage.jpostdb.org/JPST000988/files/mouse-intestine_in-solution_HILIC_result.xlsx"],"Raw":["https://storage.jpostdb.org/JPST000988/files/mouse-intestine_in-solution_HILIC_1.raw","https://storage.jpostdb.org/JPST000988/files/mouse-intestine_in-solution_HILIC_2.raw","https://storage.jpostdb.org/JPST000988/files/mouse-intestine_in-solution_HILIC_4.raw","https://storage.jpostdb.org/JPST000988/files/mouse-intestine_in-solution_HILIC_3.raw","https://storage.jpostdb.org/JPST000988/files/mouse-intestine_in-solution_HILIC_6.raw","https://storage.jpostdb.org/JPST000988/files/mouse-intestine_in-solution_HILIC_5.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Tetsuya Okajima"],"species":["Mus Musculus (mouse)"],"full_dataset_link":["https://repository.jpostdb.org/entry/JPST000988"],"submitter_affiliation":["Nagoya University Graduate School of Medicine"],"sample_protocol":[""],"repository":["jPOST"],"data_protocol":[""],"pubmed_abstract":["The modification of galactose with α1,2-fucose is involved in symbiosis with intestinal bacteria and elimination of pathogenic bacteria. It is postulated that α1,2-fucosylated mucin secreted from goblet cells is involved in defending an organism against infections, but the detailed molecular mechanisms are yet to be elucidated. It was previously reported that Paneth cells of the small intestine were positive for UEA-1 lectin staining. However, glycoproteins in Paneth cells carrying α1,2-fucose have not yet been identified. Glycoproteomic analysis of ileal lysates identified 3212 O-linked and 2962 N-linked glycopeptides. In particular, cryptdin-related sequence 1 (CRS1) expressed in Paneth cells was found to be α1,2-fucosylated. Unlike other antimicrobial α-defensin proteins, CRS1 contains unique Thr residues, which are modified with O-glycans, with 3HexNAc2Hex1Fuc1NeuAc being the main glycoform. Identification of α1,2-fucose on the O-glycans of CRS1 expressed in Paneth cells will pave the way for a mechanistic understanding of α1,2-fucose-dependent symbiosis with intestinal bacteria and elimination of pathogenic bacteria in the intestine."],"pubmed_title":["Glycoproteomic analysis identifies cryptdin-related sequence 1 as O-glycosylated protein modified with α1,2-fucose in the small intestine."],"pubmed_authors":["Hashiguchi Hiroki H, Tsukamoto Yohei Y, Ogawa Mitsutaka M, Tashima Yuko Y, Takeuchi Hideyuki H, Nakamura Masanao M, Kawashima Hiroki H, Fujishiro Mitsuhiro M, Okajima Tetsuya T"],"pubmed_abstract_synonyms":["glicoproteinas, SCS, O-Glycosylated, multi-cellular organism, parasitism, C-Glycosylated, determination, antibiotique, antimicrobials, D Galactose, Histological Labelings, Paneth Cell, Infestations and Infections, mug17, glycans, antimicrobial agents, Gene, commensalism, Glykan, eubacteria, symbiotic process, Small, polisacarido, Readability, microbicides, Glycoprotein, glycoproteins, Cryptdin, symbiotic interaction between species, Gene Products, Histological, encompassing mutualism through parasitism, Carrying, symbiosis, Bacteriobiota, glycoproteine, animal, small intestine, C-Glycosylated Proteins, antibiotics, Polysaccharide, glicoproteina, antimicrobial, Glykoprotein, Deoxygalactose, mid intestine, N-Glycosylated, symbiotic interaction between host and organism, Eubacteria, Staining, Glycans, Antibiotika, glycoproteines, Glycane, Fuc, Intestine, Monera, O-Glycosylated Proteins, D-Galactose, THR, Thr, Bacteria Woese et al. 2024, DmelCG5785, Commensalism, Bacteria (ex Cavalier-Smith 1987), Intestines, Infestation and Infection, 6-Deoxygalactose, anterior intestine, Galaktose, Bacteria <bacteria>, bowel, Prokaryotae, Glycan, Mucin, bHLHa38, fungi, Procaryotae, species, Infections and Infestations, Glycosylated Protein, Histological Labeling, Small Intestine, Glykoproteine, Neoglycoproteins, Antibiotikum, anch, antibiotic, a glycoprotein, bacteria, symbiotic interaction between organisms, body, Proteins, cryptdin-1, whole body, Labeling and Staining, Stainings, Labeling, Cell, Glykane, organism, frag1, Protein, Glycosylated Proteins, chemical analysis, Infection, sequence, Gal, prokaryotes, microbicide, Defensin, polisacaridos, intestinal tract., CRS, whole organism, alpha Fucose, Galactopyranoside, N-Glycosylated Proteins, symbiotic interaction, Mutualism, Glycosylated, TWIST, Small Intestines, Infection and Infestation, Glycopeptide, CG5785, ana, Understanding, small bowel, Galactopyranose, primary structure of sequence macromolecule, CSO, host-pathogen interaction, Goblet Cell, Protein Gene Products, polysaccharides, intestinum tenue, Gene Proteins, intestinal defensin, Labelings, alpha-Fucose, prokaryote, Cells, Koerper, BPES3, BPES2, Paneth, CRS1, Goblet, Endosymbiosis, assay, ACS3, Prokaryota"],"name_synonyms":["Deoxygalactose, mid intestine, determination, alpha Fucose, alpha Fucose., Proteins, cryptdin-1, Gene, Small Intestines, Fuc, small bowel, primary structure of sequence macromolecule, Protein Gene Products, intestinum tenue, Gene Proteins, Intestines, Small, 6-Deoxygalactose, anterior intestine, intestinal defensin, alpha-Fucose, Cryptdin, chemical analysis, Protein, Gene Products, sequence, assay, small intestine, Small Intestine"],"description_synonyms":["glicoproteinas, SCS, O-Glycosylated, multi-cellular organism, parasitism, C-Glycosylated, determination, antibiotique, antimicrobials, D Galactose, Histological Labelings, Paneth Cell, Infestations and Infections, mug17, glycans, antimicrobial agents, Gene, commensalism, Glykan, eubacteria, symbiotic process, Small, polisacarido, Readability, microbicides, Glycoprotein, glycoproteins, Cryptdin, symbiotic interaction between species, Gene Products, Histological, encompassing mutualism through parasitism, Carrying, symbiosis, Bacteriobiota, glycoproteine, animal, small intestine, C-Glycosylated Proteins, antibiotics, Polysaccharide, glicoproteina, antimicrobial, Glykoprotein, Deoxygalactose, mid intestine, N-Glycosylated, symbiotic interaction between host and organism, Eubacteria, Staining, Glycans, Antibiotika, glycoproteines, Glycane, Fuc, Intestine, Monera, O-Glycosylated Proteins, D-Galactose, THR, Thr, Bacteria Woese et al. 2024, DmelCG5785, Commensalism, Bacteria (ex Cavalier-Smith 1987), Intestines, Infestation and Infection, 6-Deoxygalactose, anterior intestine, Galaktose, Bacteria <bacteria>, bowel, Prokaryotae, Glycan, Mucin, bHLHa38, fungi, Procaryotae, species, Infections and Infestations, Glycosylated Protein, Histological Labeling, Small Intestine, Glykoproteine, Neoglycoproteins, Antibiotikum, anch, antibiotic, a glycoprotein, bacteria, symbiotic interaction between organisms, body, Proteins, cryptdin-1, whole body, Labeling and Staining, Stainings, Labeling, Cell, Glykane, organism, frag1, Protein, Glycosylated Proteins, chemical analysis, Infection, sequence, Gal, prokaryotes, microbicide, Defensin, polisacaridos, intestinal tract., CRS, whole organism, alpha Fucose, Galactopyranoside, N-Glycosylated Proteins, symbiotic interaction, Mutualism, Glycosylated, TWIST, Small Intestines, Infection and Infestation, Glycopeptide, CG5785, ana, Understanding, small bowel, Galactopyranose, primary structure of sequence macromolecule, CSO, host-pathogen interaction, Goblet Cell, Protein Gene Products, polysaccharides, intestinum tenue, Gene Proteins, intestinal defensin, Labelings, alpha-Fucose, prokaryote, Cells, Koerper, BPES3, BPES2, Paneth, CRS1, Goblet, Endosymbiosis, assay, ACS3, Prokaryota"],"pubmed_title_synonyms":["Deoxygalactose, mid intestine, determination, alpha Fucose, protein complex, Proteins, cryptdin-1, Gene, Small Intestines, Fuc, protein, protein-containing complex, small bowel, primary structure of sequence macromolecule, Protein Gene Products, intestinum tenue, Gene Proteins, Intestines, Small, 6-Deoxygalactose, anterior intestine, intestinal defensin, native protein, Small Intestine., alpha-Fucose, Cryptdin, chemical analysis, Protein, Gene Products, sequence, assay, protein aggregate, small intestine"],"additional_accession":[]},"is_claimable":false,"name":"Glycoproteomic analysis of fucose-containing proteins in small intestine identified cryptdin-related sequence 1 as O-glycosylated proteins modified with α1,2-fucose","description":"The modification of galactose with α1,2-fucose is involved in symbiosis with intestinal bacteria and elimination of pathogenic bacteria. It is postulated that α1,2-fucosylated mucin secreted from goblet cells is involved in defending an organism against infections, but the detailed molecular mechanisms are yet to be elucidated. It was previously reported that Paneth cells of the small intestine were positive for UEA-1 lectin staining. However, glycoproteins in Paneth cells carrying α1,2-fucose have not yet been identified. Glycoproteomic analysis of ileal lysates identified 3212 O-linked and 2962 N-linked glycopeptides. In particular, cryptdin-related sequence 1 (CRS1) expressed in Paneth cells was found to be α1,2-fucosylated. Unlike other antimicrobial α-defensin proteins, CRS1 contains unique Thr residues, which are modified with O-glycans, with 3HexNAc2Hex1Fuc1NeuAc being the main glycoform. Identification of α1,2-fucose on the O-glycans of CRS1 expressed in Paneth cells will pave the way for a mechanistic understanding of α1,2-fucose-dependent symbiosis with intestinal bacteria and elimination of pathogenic bacteria in the intestine.","dates":{"publication":"Thu Nov 05 00:00:00 GMT 2020"},"accession":"PXD022132","cross_references":{"TAXONOMY":["10090"],"pubmed":["33127381"]}}