JPOST Repositoryapplication/xmlhttps://storage.jpostdb.org/JPST002027/files/Breast%20Cancer_578_glycopeptide_Byonic_Quan.xlsxhttps://storage.jpostdb.org/JPST002027/files/Breast%20Normal_578Bst_membrane_glycopeptide_1.rawhttps://storage.jpostdb.org/JPST002027/files/Breast%20Normal_578Bst_membrane_glycopeptide_2.rawhttps://storage.jpostdb.org/JPST002027/files/Breast%20Normal_578Bst_membrane_glycopeptide_3.rawhttps://storage.jpostdb.org/JPST002027/files/Breast%20Cancer_578T_membrane_glycopeptide_2.rawhttps://storage.jpostdb.org/JPST002027/files/Breast%20Cancer_578T_membrane_glycopeptide_1.rawhttps://storage.jpostdb.org/JPST002027/files/Breast%20Cancer_578T_membrane_glycopeptide_3.rawprimaryOK200ProteomicsDaisuke TakakuraHomo Sapiens (human)https://repository.jpostdb.org/entry/JPST002027Yokohama City UniversityjPOSTAberrant glycosylation of membrane proteins is a hallmark of cancer and a useful molecular marker for the diagnosis of breast cancer (BC). However, the molecular mechanisms by which altered glycosylation affects the malignant transformations associated with BC are poorly understood. Accordingly, we performed comparative membrane <i>N</i>-glycoproteomics using the human BC cell line pair, Hs578T, and its syngeneic normal cell line, Hs578Bst. A total of 359 <i>N</i>-glycoforms derived from 113 proteins were identified in both cell lines, of which 27 were found only in Hs578T cells. Significant changes in <i>N</i>-glycosylation were found in the lysosome-associated membrane protein 1 (LAMP1), the integrin family, and laminin. Confocal immunofluorescence microscopy images revealed the accumulation of lysosomes in the perinuclear space in cancer cells, which could be associated with marked changes in LAMP1 glycosylation, such as a decreased level of polylactosamine chains. Overall, the alterations in glycosylation may be involved in changes in the adhesion and degradation of BC cells.Comprehensive Membrane <i>N</i>-Glycoproteomics Using Human Breast Cancer Cell Line Pairs.Takakura Daisuke D, Yoshida Haruka H, Ohashi Shoko S, Kawasaki Nana Naverage, Taf[[II]]250, Controlling, Taf200, dTAF[[II]]230, TAF[[II]]250, d230, preventive therapy, dTAF[[II]]250, TAF[[II]]230, reference sample, TFIID TAF250, cel, cell, prophylaxis, TAF200, l(3)84Ab, dTAFII250, Taf1p, TAF[II]250, BG:DS00004.13, TAFII-250, CG17603, TAF250/230, TAF[[II]], EfW1, Cell, prevention, dTAF230, preventive measures, dTAF250, dmTAF[[II]]230, TAFII250, DmelCG17603, TAF1., Taf250, control, dmTAF1, SR3-5, Taf230, p230, TAF[[II]]250/230, TFIID, TAF, prevention and control, TAF230, Controlled, TAF250biochemical pathways, Integral Membrane Proteins, Networks, malignant tumor of the breast, Antemortem Diagnosis, O-linked Glycosylations, Kinship, alphaPS2, Galactosylation, Surface Proteins, mammary 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sapiens, Hs 578T, Tissues, integral component of membrane, Modern Man, Modern, region of membrane, whole membrane, membrane region, Tissue, integral to membrane, Membrane, Man, breast carcinoma cell line, humanfalseN-glycoproteomics on BC and normal control cell linesComprehensive membrane N-glycoproteomics using human breast cancer cell line pairs, Hs578T and Hs578Bst.Fri Feb 16 00:00:00 GMT 2024PXD040130960637250596