Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression
Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Chen, Xixi [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2021 |
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| Schlagwörter: |
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| Anmerkung: |
© University of Navarra 2021 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of physiology and biochemistry - Pamplona : Univ. de Navarra, 2000, 78(2021), 1 vom: 31. Aug., Seite 73-83 |
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| Übergeordnetes Werk: |
volume:78 ; year:2021 ; number:1 ; day:31 ; month:08 ; pages:73-83 |
| Links: |
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| DOI / URN: |
10.1007/s13105-021-00840-x |
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SPR04633212X |
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| 100 | 1 | |a Chen, Xixi |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression |
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| 520 | |a Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. | ||
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10.1007/s13105-021-00840-x doi (DE-627)SPR04633212X (SPR)s13105-021-00840-x-e DE-627 ger DE-627 rakwb eng Chen, Xixi verfasserin aut Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © University of Navarra 2021 Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. Caveolin-1 (dpeaa)DE-He213 -glycan (dpeaa)DE-He213 Glycosylation (dpeaa)DE-He213 Sialyltransferase (dpeaa)DE-He213 Wang, Liping aut Wu, Yinshuang aut Zhang, Hongshuo aut Dong, Weijie aut Yu, Xiao aut Huang, Chuncui aut Li, Yan aut Wang, Shujing aut Zhang, Jianing (orcid)0000-0002-4514-9197 aut Enthalten in Journal of physiology and biochemistry Pamplona : Univ. de Navarra, 2000 78(2021), 1 vom: 31. Aug., Seite 73-83 (DE-627)494830220 (DE-600)2196783-0 1877-8755 nnns volume:78 year:2021 number:1 day:31 month:08 pages:73-83 https://dx.doi.org/10.1007/s13105-021-00840-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 78 2021 1 31 08 73-83 |
| spelling |
10.1007/s13105-021-00840-x doi (DE-627)SPR04633212X (SPR)s13105-021-00840-x-e DE-627 ger DE-627 rakwb eng Chen, Xixi verfasserin aut Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © University of Navarra 2021 Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. Caveolin-1 (dpeaa)DE-He213 -glycan (dpeaa)DE-He213 Glycosylation (dpeaa)DE-He213 Sialyltransferase (dpeaa)DE-He213 Wang, Liping aut Wu, Yinshuang aut Zhang, Hongshuo aut Dong, Weijie aut Yu, Xiao aut Huang, Chuncui aut Li, Yan aut Wang, Shujing aut Zhang, Jianing (orcid)0000-0002-4514-9197 aut Enthalten in Journal of physiology and biochemistry Pamplona : Univ. de Navarra, 2000 78(2021), 1 vom: 31. Aug., Seite 73-83 (DE-627)494830220 (DE-600)2196783-0 1877-8755 nnns volume:78 year:2021 number:1 day:31 month:08 pages:73-83 https://dx.doi.org/10.1007/s13105-021-00840-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 78 2021 1 31 08 73-83 |
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10.1007/s13105-021-00840-x doi (DE-627)SPR04633212X (SPR)s13105-021-00840-x-e DE-627 ger DE-627 rakwb eng Chen, Xixi verfasserin aut Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © University of Navarra 2021 Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. Caveolin-1 (dpeaa)DE-He213 -glycan (dpeaa)DE-He213 Glycosylation (dpeaa)DE-He213 Sialyltransferase (dpeaa)DE-He213 Wang, Liping aut Wu, Yinshuang aut Zhang, Hongshuo aut Dong, Weijie aut Yu, Xiao aut Huang, Chuncui aut Li, Yan aut Wang, Shujing aut Zhang, Jianing (orcid)0000-0002-4514-9197 aut Enthalten in Journal of physiology and biochemistry Pamplona : Univ. de Navarra, 2000 78(2021), 1 vom: 31. Aug., Seite 73-83 (DE-627)494830220 (DE-600)2196783-0 1877-8755 nnns volume:78 year:2021 number:1 day:31 month:08 pages:73-83 https://dx.doi.org/10.1007/s13105-021-00840-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 78 2021 1 31 08 73-83 |
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10.1007/s13105-021-00840-x doi (DE-627)SPR04633212X (SPR)s13105-021-00840-x-e DE-627 ger DE-627 rakwb eng Chen, Xixi verfasserin aut Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © University of Navarra 2021 Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. Caveolin-1 (dpeaa)DE-He213 -glycan (dpeaa)DE-He213 Glycosylation (dpeaa)DE-He213 Sialyltransferase (dpeaa)DE-He213 Wang, Liping aut Wu, Yinshuang aut Zhang, Hongshuo aut Dong, Weijie aut Yu, Xiao aut Huang, Chuncui aut Li, Yan aut Wang, Shujing aut Zhang, Jianing (orcid)0000-0002-4514-9197 aut Enthalten in Journal of physiology and biochemistry Pamplona : Univ. de Navarra, 2000 78(2021), 1 vom: 31. Aug., Seite 73-83 (DE-627)494830220 (DE-600)2196783-0 1877-8755 nnns volume:78 year:2021 number:1 day:31 month:08 pages:73-83 https://dx.doi.org/10.1007/s13105-021-00840-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 78 2021 1 31 08 73-83 |
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10.1007/s13105-021-00840-x doi (DE-627)SPR04633212X (SPR)s13105-021-00840-x-e DE-627 ger DE-627 rakwb eng Chen, Xixi verfasserin aut Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © University of Navarra 2021 Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. Caveolin-1 (dpeaa)DE-He213 -glycan (dpeaa)DE-He213 Glycosylation (dpeaa)DE-He213 Sialyltransferase (dpeaa)DE-He213 Wang, Liping aut Wu, Yinshuang aut Zhang, Hongshuo aut Dong, Weijie aut Yu, Xiao aut Huang, Chuncui aut Li, Yan aut Wang, Shujing aut Zhang, Jianing (orcid)0000-0002-4514-9197 aut Enthalten in Journal of physiology and biochemistry Pamplona : Univ. de Navarra, 2000 78(2021), 1 vom: 31. Aug., Seite 73-83 (DE-627)494830220 (DE-600)2196783-0 1877-8755 nnns volume:78 year:2021 number:1 day:31 month:08 pages:73-83 https://dx.doi.org/10.1007/s13105-021-00840-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 78 2021 1 31 08 73-83 |
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Enthalten in Journal of physiology and biochemistry 78(2021), 1 vom: 31. Aug., Seite 73-83 volume:78 year:2021 number:1 day:31 month:08 pages:73-83 |
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Enthalten in Journal of physiology and biochemistry 78(2021), 1 vom: 31. Aug., Seite 73-83 volume:78 year:2021 number:1 day:31 month:08 pages:73-83 |
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Chen, Xixi @@aut@@ Wang, Liping @@aut@@ Wu, Yinshuang @@aut@@ Zhang, Hongshuo @@aut@@ Dong, Weijie @@aut@@ Yu, Xiao @@aut@@ Huang, Chuncui @@aut@@ Li, Yan @@aut@@ Wang, Shujing @@aut@@ Zhang, Jianing @@aut@@ |
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Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. 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|
| author |
Chen, Xixi |
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Chen, Xixi misc Caveolin-1 misc -glycan misc Glycosylation misc Sialyltransferase Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression |
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Chen, Xixi |
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1877-8755 |
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Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression Caveolin-1 (dpeaa)DE-He213 -glycan (dpeaa)DE-He213 Glycosylation (dpeaa)DE-He213 Sialyltransferase (dpeaa)DE-He213 |
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misc Caveolin-1 misc -glycan misc Glycosylation misc Sialyltransferase |
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misc Caveolin-1 misc -glycan misc Glycosylation misc Sialyltransferase |
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misc Caveolin-1 misc -glycan misc Glycosylation misc Sialyltransferase |
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Journal of physiology and biochemistry |
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Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression |
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Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression |
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Chen, Xixi |
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Journal of physiology and biochemistry |
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Journal of physiology and biochemistry |
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Chen, Xixi Wang, Liping Wu, Yinshuang Zhang, Hongshuo Dong, Weijie Yu, Xiao Huang, Chuncui Li, Yan Wang, Shujing Zhang, Jianing |
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Chen, Xixi |
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caveolin-1 knockout mice have altered serum n-glycan profile and sialyltransferase tissue expression |
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Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression |
| abstract |
Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. © University of Navarra 2021 |
| abstractGer |
Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. © University of Navarra 2021 |
| abstract_unstemmed |
Abstract Caveolin-1 (Cav-1) is a constitutive protein within caveolar membranes. Previous studies from our group and others indicated that Cav-1 could mediate N-glycosylation, α2,6-sialylation, and fucosylation in mouse hepatocarcinoma cells in vitro. However, little is known about the effect of Cav-1 expression on glycosylation modifications in vivo. In this study, the N-glycan profiles in serum from Cav-1−/− mice were investigated by lectin microarray and mass spectrometric analysis approaches. The results showed that levels of multi-antennary branched, α2,6-sialylated, and galactosylated N-glycans increased, while high-mannose typed and fucosylated N-glycans decreased in the serum of Cav-1−/− mice, compared with that of wild-type mice. Furthermore, the real-time quantitative PCR analysis indicated that α2,6-sialyltransferase gene expression decreased significantly in Cav-1−/− mouse organ tissues, but α2,3- and α2,8-sialyltransferase did not. Of them, both mRNA and protein expression levels of the β-galactoside α2,6-sialyltransferase 1 (ST6Gal-I) had dramatically reduced in Cav-1−/− mice organ tissues, which was consistent with the α2,6-sialyl Gal/GalNAc level reduced significantly in tissues instead of serum from Cav-1−/− mice. These results provide for the first time the N-glycans profile of Cav-1−/− mice serum, which will facilitate understanding the function of Cav-1 from the perspective of glycosylation. © University of Navarra 2021 |
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| container_issue |
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| title_short |
Caveolin-1 knockout mice have altered serum N-glycan profile and sialyltransferase tissue expression |
| url |
https://dx.doi.org/10.1007/s13105-021-00840-x |
| remote_bool |
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| author2 |
Wang, Liping Wu, Yinshuang Zhang, Hongshuo Dong, Weijie Yu, Xiao Huang, Chuncui Li, Yan Wang, Shujing Zhang, Jianing |
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Wang, Liping Wu, Yinshuang Zhang, Hongshuo Dong, Weijie Yu, Xiao Huang, Chuncui Li, Yan Wang, Shujing Zhang, Jianing |
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| doi_str |
10.1007/s13105-021-00840-x |
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2024-07-03T21:53:13.261Z |
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| score |
7.4011335 |