Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL)
Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type <i<O</i<-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell...
Ausführliche Beschreibung
Autor*in: |
Chiara Napoletano [verfasserIn] Catharina Steentoff [verfasserIn] Federico Battisti [verfasserIn] Zilu Ye [verfasserIn] Hassan Rahimi [verfasserIn] Ilaria Grazia Zizzari [verfasserIn] Marco Dionisi [verfasserIn] Bruna Cerbelli [verfasserIn] Federica Tomao [verfasserIn] Deborah French [verfasserIn] Giulia d’Amati [verfasserIn] Pierluigi Benedetti Panici [verfasserIn] Sergey Vakhrushev [verfasserIn] Henrik Clausen [verfasserIn] Marianna Nuti [verfasserIn] Aurelia Rughetti [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2020 |
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Übergeordnetes Werk: |
In: Cancers - MDPI AG, 2010, 12(2020), 10, p 2841 |
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Übergeordnetes Werk: |
volume:12 ; year:2020 ; number:10, p 2841 |
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DOI / URN: |
10.3390/cancers12102841 |
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Katalog-ID: |
DOAJ039249506 |
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520 | |a Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type <i<O</i<-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface, which profoundly impact anti-tumor immune recognition. The tumor-associated glycan pattern may thus be regarded as a biomarker of immune modulation. In epithelial ovarian cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnosis and develop novel therapeutic interventions. The aim of this study was to investigate the ovarian cancer <i<O</i<-glycoproteome and identify tumor-associated glycoproteins relevant in tumor–dendritic cell (DC) interactions, mediated by macrophage galactose-like C type lectin (MGL), which recognizes the tumor-associated Tn <i<O</i<-glycan. Lectin weak affinity chromatography (LWAC) was employed to probe the <i<O</i<-glycopeptidome by MGL and <i<Vicia villosa</i< agglutinin (VVA) lectin using glycoengineered ovarian cancer cell lines and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis gave information on the glycan arrangement recognized by MGL in tumor cells. The potential MGL binders identified were located, as expected, at the cell membrane, but also within the intracellular compartment and the matrisome, suggesting that MGL in vivo may play a complex role in sensing microenvironmental cues. The tumor glycoproteins binders for MGL may become relevant to characterize the interaction between the immune system and tumor progression and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions. | ||
650 | 4 | |a Epithelial ovarian cancer | |
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10.3390/cancers12102841 doi (DE-627)DOAJ039249506 (DE-599)DOAJ8e8b4a9558fe4d1587e2e2e8cf0464e8 DE-627 ger DE-627 rakwb eng RC254-282 Chiara Napoletano verfasserin aut Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL) 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type <i<O</i<-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface, which profoundly impact anti-tumor immune recognition. The tumor-associated glycan pattern may thus be regarded as a biomarker of immune modulation. In epithelial ovarian cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnosis and develop novel therapeutic interventions. The aim of this study was to investigate the ovarian cancer <i<O</i<-glycoproteome and identify tumor-associated glycoproteins relevant in tumor–dendritic cell (DC) interactions, mediated by macrophage galactose-like C type lectin (MGL), which recognizes the tumor-associated Tn <i<O</i<-glycan. Lectin weak affinity chromatography (LWAC) was employed to probe the <i<O</i<-glycopeptidome by MGL and <i<Vicia villosa</i< agglutinin (VVA) lectin using glycoengineered ovarian cancer cell lines and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis gave information on the glycan arrangement recognized by MGL in tumor cells. The potential MGL binders identified were located, as expected, at the cell membrane, but also within the intracellular compartment and the matrisome, suggesting that MGL in vivo may play a complex role in sensing microenvironmental cues. The tumor glycoproteins binders for MGL may become relevant to characterize the interaction between the immune system and tumor progression and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions. Epithelial ovarian cancer MGL/CLEC10A/CD301 <i<O</i<-glycosylation Tn antigen cancer immunotherapy DCs Neoplasms. Tumors. Oncology. Including cancer and carcinogens Catharina Steentoff verfasserin aut Federico Battisti verfasserin aut Zilu Ye verfasserin aut Hassan Rahimi verfasserin aut Ilaria Grazia Zizzari verfasserin aut Marco Dionisi verfasserin aut Bruna Cerbelli verfasserin aut Federica Tomao verfasserin aut Deborah French verfasserin aut Giulia d’Amati verfasserin aut Pierluigi Benedetti Panici verfasserin aut Sergey Vakhrushev verfasserin aut Henrik Clausen verfasserin aut Marianna Nuti verfasserin aut Aurelia Rughetti verfasserin aut In Cancers MDPI AG, 2010 12(2020), 10, p 2841 (DE-627)614095670 (DE-600)2527080-1 20726694 nnns volume:12 year:2020 number:10, p 2841 https://doi.org/10.3390/cancers12102841 kostenfrei https://doaj.org/article/8e8b4a9558fe4d1587e2e2e8cf0464e8 kostenfrei https://www.mdpi.com/2072-6694/12/10/2841 kostenfrei https://doaj.org/toc/2072-6694 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2020 10, p 2841 |
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10.3390/cancers12102841 doi (DE-627)DOAJ039249506 (DE-599)DOAJ8e8b4a9558fe4d1587e2e2e8cf0464e8 DE-627 ger DE-627 rakwb eng RC254-282 Chiara Napoletano verfasserin aut Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL) 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type <i<O</i<-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface, which profoundly impact anti-tumor immune recognition. The tumor-associated glycan pattern may thus be regarded as a biomarker of immune modulation. In epithelial ovarian cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnosis and develop novel therapeutic interventions. The aim of this study was to investigate the ovarian cancer <i<O</i<-glycoproteome and identify tumor-associated glycoproteins relevant in tumor–dendritic cell (DC) interactions, mediated by macrophage galactose-like C type lectin (MGL), which recognizes the tumor-associated Tn <i<O</i<-glycan. Lectin weak affinity chromatography (LWAC) was employed to probe the <i<O</i<-glycopeptidome by MGL and <i<Vicia villosa</i< agglutinin (VVA) lectin using glycoengineered ovarian cancer cell lines and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis gave information on the glycan arrangement recognized by MGL in tumor cells. The potential MGL binders identified were located, as expected, at the cell membrane, but also within the intracellular compartment and the matrisome, suggesting that MGL in vivo may play a complex role in sensing microenvironmental cues. The tumor glycoproteins binders for MGL may become relevant to characterize the interaction between the immune system and tumor progression and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions. Epithelial ovarian cancer MGL/CLEC10A/CD301 <i<O</i<-glycosylation Tn antigen cancer immunotherapy DCs Neoplasms. Tumors. Oncology. Including cancer and carcinogens Catharina Steentoff verfasserin aut Federico Battisti verfasserin aut Zilu Ye verfasserin aut Hassan Rahimi verfasserin aut Ilaria Grazia Zizzari verfasserin aut Marco Dionisi verfasserin aut Bruna Cerbelli verfasserin aut Federica Tomao verfasserin aut Deborah French verfasserin aut Giulia d’Amati verfasserin aut Pierluigi Benedetti Panici verfasserin aut Sergey Vakhrushev verfasserin aut Henrik Clausen verfasserin aut Marianna Nuti verfasserin aut Aurelia Rughetti verfasserin aut In Cancers MDPI AG, 2010 12(2020), 10, p 2841 (DE-627)614095670 (DE-600)2527080-1 20726694 nnns volume:12 year:2020 number:10, p 2841 https://doi.org/10.3390/cancers12102841 kostenfrei https://doaj.org/article/8e8b4a9558fe4d1587e2e2e8cf0464e8 kostenfrei https://www.mdpi.com/2072-6694/12/10/2841 kostenfrei https://doaj.org/toc/2072-6694 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2020 10, p 2841 |
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10.3390/cancers12102841 doi (DE-627)DOAJ039249506 (DE-599)DOAJ8e8b4a9558fe4d1587e2e2e8cf0464e8 DE-627 ger DE-627 rakwb eng RC254-282 Chiara Napoletano verfasserin aut Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL) 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type <i<O</i<-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface, which profoundly impact anti-tumor immune recognition. The tumor-associated glycan pattern may thus be regarded as a biomarker of immune modulation. In epithelial ovarian cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnosis and develop novel therapeutic interventions. The aim of this study was to investigate the ovarian cancer <i<O</i<-glycoproteome and identify tumor-associated glycoproteins relevant in tumor–dendritic cell (DC) interactions, mediated by macrophage galactose-like C type lectin (MGL), which recognizes the tumor-associated Tn <i<O</i<-glycan. Lectin weak affinity chromatography (LWAC) was employed to probe the <i<O</i<-glycopeptidome by MGL and <i<Vicia villosa</i< agglutinin (VVA) lectin using glycoengineered ovarian cancer cell lines and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis gave information on the glycan arrangement recognized by MGL in tumor cells. The potential MGL binders identified were located, as expected, at the cell membrane, but also within the intracellular compartment and the matrisome, suggesting that MGL in vivo may play a complex role in sensing microenvironmental cues. The tumor glycoproteins binders for MGL may become relevant to characterize the interaction between the immune system and tumor progression and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions. Epithelial ovarian cancer MGL/CLEC10A/CD301 <i<O</i<-glycosylation Tn antigen cancer immunotherapy DCs Neoplasms. Tumors. Oncology. Including cancer and carcinogens Catharina Steentoff verfasserin aut Federico Battisti verfasserin aut Zilu Ye verfasserin aut Hassan Rahimi verfasserin aut Ilaria Grazia Zizzari verfasserin aut Marco Dionisi verfasserin aut Bruna Cerbelli verfasserin aut Federica Tomao verfasserin aut Deborah French verfasserin aut Giulia d’Amati verfasserin aut Pierluigi Benedetti Panici verfasserin aut Sergey Vakhrushev verfasserin aut Henrik Clausen verfasserin aut Marianna Nuti verfasserin aut Aurelia Rughetti verfasserin aut In Cancers MDPI AG, 2010 12(2020), 10, p 2841 (DE-627)614095670 (DE-600)2527080-1 20726694 nnns volume:12 year:2020 number:10, p 2841 https://doi.org/10.3390/cancers12102841 kostenfrei https://doaj.org/article/8e8b4a9558fe4d1587e2e2e8cf0464e8 kostenfrei https://www.mdpi.com/2072-6694/12/10/2841 kostenfrei https://doaj.org/toc/2072-6694 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2020 10, p 2841 |
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Chiara Napoletano @@aut@@ Catharina Steentoff @@aut@@ Federico Battisti @@aut@@ Zilu Ye @@aut@@ Hassan Rahimi @@aut@@ Ilaria Grazia Zizzari @@aut@@ Marco Dionisi @@aut@@ Bruna Cerbelli @@aut@@ Federica Tomao @@aut@@ Deborah French @@aut@@ Giulia d’Amati @@aut@@ Pierluigi Benedetti Panici @@aut@@ Sergey Vakhrushev @@aut@@ Henrik Clausen @@aut@@ Marianna Nuti @@aut@@ Aurelia Rughetti @@aut@@ |
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RC254-282 Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL) Epithelial ovarian cancer MGL/CLEC10A/CD301 <i<O</i<-glycosylation Tn antigen cancer immunotherapy DCs |
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Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL) |
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Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL) |
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Chiara Napoletano |
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Chiara Napoletano Catharina Steentoff Federico Battisti Zilu Ye Hassan Rahimi Ilaria Grazia Zizzari Marco Dionisi Bruna Cerbelli Federica Tomao Deborah French Giulia d’Amati Pierluigi Benedetti Panici Sergey Vakhrushev Henrik Clausen Marianna Nuti Aurelia Rughetti |
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investigating patterns of immune interaction in ovarian cancer: probing the o-glycoproteome by the macrophage galactose-like c-type lectin (mgl) |
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Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL) |
abstract |
Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type <i<O</i<-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface, which profoundly impact anti-tumor immune recognition. The tumor-associated glycan pattern may thus be regarded as a biomarker of immune modulation. In epithelial ovarian cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnosis and develop novel therapeutic interventions. The aim of this study was to investigate the ovarian cancer <i<O</i<-glycoproteome and identify tumor-associated glycoproteins relevant in tumor–dendritic cell (DC) interactions, mediated by macrophage galactose-like C type lectin (MGL), which recognizes the tumor-associated Tn <i<O</i<-glycan. Lectin weak affinity chromatography (LWAC) was employed to probe the <i<O</i<-glycopeptidome by MGL and <i<Vicia villosa</i< agglutinin (VVA) lectin using glycoengineered ovarian cancer cell lines and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis gave information on the glycan arrangement recognized by MGL in tumor cells. The potential MGL binders identified were located, as expected, at the cell membrane, but also within the intracellular compartment and the matrisome, suggesting that MGL in vivo may play a complex role in sensing microenvironmental cues. The tumor glycoproteins binders for MGL may become relevant to characterize the interaction between the immune system and tumor progression and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions. |
abstractGer |
Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type <i<O</i<-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface, which profoundly impact anti-tumor immune recognition. The tumor-associated glycan pattern may thus be regarded as a biomarker of immune modulation. In epithelial ovarian cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnosis and develop novel therapeutic interventions. The aim of this study was to investigate the ovarian cancer <i<O</i<-glycoproteome and identify tumor-associated glycoproteins relevant in tumor–dendritic cell (DC) interactions, mediated by macrophage galactose-like C type lectin (MGL), which recognizes the tumor-associated Tn <i<O</i<-glycan. Lectin weak affinity chromatography (LWAC) was employed to probe the <i<O</i<-glycopeptidome by MGL and <i<Vicia villosa</i< agglutinin (VVA) lectin using glycoengineered ovarian cancer cell lines and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis gave information on the glycan arrangement recognized by MGL in tumor cells. The potential MGL binders identified were located, as expected, at the cell membrane, but also within the intracellular compartment and the matrisome, suggesting that MGL in vivo may play a complex role in sensing microenvironmental cues. The tumor glycoproteins binders for MGL may become relevant to characterize the interaction between the immune system and tumor progression and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions. |
abstract_unstemmed |
Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type <i<O</i<-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface, which profoundly impact anti-tumor immune recognition. The tumor-associated glycan pattern may thus be regarded as a biomarker of immune modulation. In epithelial ovarian cancer (EOC) there is a particular lack of specific biomarkers and molecular targets to aid early diagnosis and develop novel therapeutic interventions. The aim of this study was to investigate the ovarian cancer <i<O</i<-glycoproteome and identify tumor-associated glycoproteins relevant in tumor–dendritic cell (DC) interactions, mediated by macrophage galactose-like C type lectin (MGL), which recognizes the tumor-associated Tn <i<O</i<-glycan. Lectin weak affinity chromatography (LWAC) was employed to probe the <i<O</i<-glycopeptidome by MGL and <i<Vicia villosa</i< agglutinin (VVA) lectin using glycoengineered ovarian cancer cell lines and ovarian cancer tissues as input material. Biochemical and bioinformatics analysis gave information on the glycan arrangement recognized by MGL in tumor cells. The potential MGL binders identified were located, as expected, at the cell membrane, but also within the intracellular compartment and the matrisome, suggesting that MGL in vivo may play a complex role in sensing microenvironmental cues. The tumor glycoproteins binders for MGL may become relevant to characterize the interaction between the immune system and tumor progression and contribute to the design of glycan targeting-based strategies for EOC immunotherapeutic interventions. |
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Investigating Patterns of Immune Interaction in Ovarian Cancer: Probing the O-glycoproteome by the Macrophage Galactose-Like C-Type Lectin (MGL) |
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