Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A review
Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Sanji, Ashwini S. [verfasserIn] J., Manasa [verfasserIn] Gurav, Maruti J. [verfasserIn] Batra, Surinder K. [verfasserIn] Chachadi, Vishwanath B. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2024 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: International journal of biological macromolecules - New York, NY [u.a.] : Elsevier, 1979, 260 |
|---|---|
| Übergeordnetes Werk: |
volume:260 |
| DOI / URN: |
10.1016/j.ijbiomac.2024.129318 |
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| Katalog-ID: |
ELV067191479 |
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| 245 | 1 | 0 | |a Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A review |
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| 520 | |a Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. | ||
| 650 | 4 | |a O-glycans | |
| 650 | 4 | |a Cancer | |
| 650 | 4 | |a Lewis antigens | |
| 650 | 4 | |a Glycopathology | |
| 650 | 4 | |a Biosynthesis | |
| 700 | 1 | |a J., Manasa |e verfasserin |4 aut | |
| 700 | 1 | |a Gurav, Maruti J. |e verfasserin |4 aut | |
| 700 | 1 | |a Batra, Surinder K. |e verfasserin |4 aut | |
| 700 | 1 | |a Chachadi, Vishwanath B. |e verfasserin |0 (orcid)0000-0002-4488-419X |4 aut | |
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10.1016/j.ijbiomac.2024.129318 doi (DE-627)ELV067191479 (ELSEVIER)S0141-8130(24)00121-1 DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Sanji, Ashwini S. verfasserin aut Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A review 2024 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. O-glycans Cancer Lewis antigens Glycopathology Biosynthesis J., Manasa verfasserin aut Gurav, Maruti J. verfasserin aut Batra, Surinder K. verfasserin aut Chachadi, Vishwanath B. verfasserin (orcid)0000-0002-4488-419X aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 260 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:260 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 260 |
| spelling |
10.1016/j.ijbiomac.2024.129318 doi (DE-627)ELV067191479 (ELSEVIER)S0141-8130(24)00121-1 DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Sanji, Ashwini S. verfasserin aut Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A review 2024 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. O-glycans Cancer Lewis antigens Glycopathology Biosynthesis J., Manasa verfasserin aut Gurav, Maruti J. verfasserin aut Batra, Surinder K. verfasserin aut Chachadi, Vishwanath B. verfasserin (orcid)0000-0002-4488-419X aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 260 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:260 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 260 |
| allfields_unstemmed |
10.1016/j.ijbiomac.2024.129318 doi (DE-627)ELV067191479 (ELSEVIER)S0141-8130(24)00121-1 DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Sanji, Ashwini S. verfasserin aut Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A review 2024 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. O-glycans Cancer Lewis antigens Glycopathology Biosynthesis J., Manasa verfasserin aut Gurav, Maruti J. verfasserin aut Batra, Surinder K. verfasserin aut Chachadi, Vishwanath B. verfasserin (orcid)0000-0002-4488-419X aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 260 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:260 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 260 |
| allfieldsGer |
10.1016/j.ijbiomac.2024.129318 doi (DE-627)ELV067191479 (ELSEVIER)S0141-8130(24)00121-1 DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Sanji, Ashwini S. verfasserin aut Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A review 2024 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. O-glycans Cancer Lewis antigens Glycopathology Biosynthesis J., Manasa verfasserin aut Gurav, Maruti J. verfasserin aut Batra, Surinder K. verfasserin aut Chachadi, Vishwanath B. verfasserin (orcid)0000-0002-4488-419X aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 260 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:260 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 260 |
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10.1016/j.ijbiomac.2024.129318 doi (DE-627)ELV067191479 (ELSEVIER)S0141-8130(24)00121-1 DE-627 ger DE-627 rda eng 540 570 VZ BIODIV DE-30 fid 35.80 bkl 58.30 bkl Sanji, Ashwini S. verfasserin aut Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A review 2024 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. O-glycans Cancer Lewis antigens Glycopathology Biosynthesis J., Manasa verfasserin aut Gurav, Maruti J. verfasserin aut Batra, Surinder K. verfasserin aut Chachadi, Vishwanath B. verfasserin (orcid)0000-0002-4488-419X aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 260 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:260 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.80 Makromolekulare Chemie VZ 58.30 Biotechnologie VZ AR 260 |
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cancer snap-shots: biochemistry and glycopathology of o-glycans: a review |
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Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A review |
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Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. |
| abstractGer |
Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. |
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Cancer pathogenesis is strongly linked to the qualitative and quantitative alteration of the cell surface glycans, that are glycosidically linked to proteins and lipids. Glycans that are covalently linked to the polypeptide backbone of a protein through nitrogen or oxygen, are known as N-glycans or O-glycans, respectively. Although the role of glycans in the expression, physiology, and communication of cells is well documented, the function of these glycans in tumor biology is not fully elucidated. In this context, current review summarizes biosynthesis, modifications and pathological implications of O-glycans The review also highlights illustrative examples of cancer types modulated by aberrant O-glycosylation. Related O-glycans like Thomsen-nouveau (Tn), Thomsen-Friedenreich (TF), Lewisa/x, Lewisb/y, sialyl Lewisa/x and some other O-glycans are discussed in detail. Since, the overexpression of O-glycans are attributed to the aggressiveness and metastatic behavior of cancer cells, the current review attempts to understand the relation between metastasis and O-glycans. |
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