Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells

High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Ahadova, Aysel - 1988- [verfasserIn] Gebert, Johannes [verfasserIn] Knebel Doeberitz, Magnus von [verfasserIn] Kopitz, Jürgen [verfasserIn] Kloor, Matthias - 1972- [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	9 April 2015

Schlagwörter:	cellular glucose metabolism glycobiology membrane proteins

Anmerkung:	Gesehen am TT.MM.JJJ
Umfang:	9

Übergeordnetes Werk:	Enthalten in: IUBMB life - International Union of Biochemistry and Molecular Biology, Weinheim [u.a.] : Wiley-VCH, 1999, 67(2015), 3, Seite 218-226
Übergeordnetes Werk:	volume:67 ; year:2015 ; number:3 ; pages:218-226 ; extent:9

Links:	Volltext Volltext

DOI / URN:	10.1002/iub.1364

Katalog-ID:	1563793873

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245	1	0	\|a Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells \|c Aysel Ahadova, Johannes Gebert, Magnus von Knebel Doeberitz, Juergen Kopitz, Matthias Kloor
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520			\|a High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015
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author_variant	a a aa j g jg d m v k dmv dmvk j k jk m k mk
matchkey_str	article:15216551:2015----::oeeednefco2exdlcsogyortimno
oclc_num	1340979641
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publishDate	2015
allfields	10.1002/iub.1364 doi (DE-627)1563793873 (DE-576)493793879 (DE-599)BSZ493793879 (OCoLC)1340979641 DE-627 ger DE-627 rda eng Ahadova, Aysel 1988- verfasserin (DE-588)106835268X (DE-627)820167118 (DE-576)427724783 aut Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells Aysel Ahadova, Johannes Gebert, Magnus von Knebel Doeberitz, Juergen Kopitz, Matthias Kloor 9 April 2015 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am TT.MM.JJJ High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 cellular glucose metabolism glycobiology membrane proteins Gebert, Johannes verfasserin (DE-588)1033923567 (DE-627)743674731 (DE-576)381600688 aut Knebel Doeberitz, Magnus von verfasserin (DE-588)1022165291 (DE-627)71693289X (DE-576)364934239 aut Kopitz, Jürgen verfasserin (DE-588)1033923397 (DE-627)743674472 (DE-576)16530393X aut Kloor, Matthias 1972- verfasserin (DE-588)124552803 (DE-627)363416609 (DE-576)294228616 aut Enthalten in International Union of Biochemistry and Molecular Biology IUBMB life Weinheim [u.a.] : Wiley-VCH, 1999 67(2015), 3, Seite 218-226 Online-Ressource (DE-627)31368040X (DE-600)2009952-6 (DE-576)27387831X 1521-6551 nnns volume:67 year:2015 number:3 pages:218-226 extent:9 http://dx.doi.org/10.1002/iub.1364 Verlag Resolving-System kostenfrei Volltext http://onlinelibrary.wiley.com/doi/10.1002/iub.1364/abstract Verlag kostenfrei Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 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_2018 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_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 GBV_ILN_2403 GBV_ILN_2403 ISIL_DE-LFER AR 67 2015 3 218-226 9 2013 01 DE-16-250 2981429426 00 --%%-- --%%-- --%%-- --%%-- l01 25-09-17 2403 01 DE-LFER 298371876X 00 --%%-- --%%-- n --%%-- l01 10-10-17 2403 01 DE-LFER http://dx.doi.org/10.1002/iub.1364 2013 01 DE-16-250 00 s hd2015 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_9 2013 01 DE-16-250 04 p (DE-627)1503432874 Ahadova, Aysel 2013 01 DE-16-250 04 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_1 2013 01 DE-16-250 05 p (DE-627)1451604718 Gebert, Johannes 2013 01 DE-16-250 05 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_2 2013 01 DE-16-250 06 p (DE-627)1435319745 Knebel Doeberitz, Magnus von 2013 01 DE-16-250 06 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 06 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 06 s pos_3 2013 01 DE-16-250 07 p (DE-627)1451604467 Kopitz, Jürgen 2013 01 DE-16-250 07 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 07 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 07 s pos_4 2013 01 DE-16-250 08 p (DE-627)1434888363 Kloor, Matthias 2013 01 DE-16-250 08 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 08 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 08 s pos_5
spelling	10.1002/iub.1364 doi (DE-627)1563793873 (DE-576)493793879 (DE-599)BSZ493793879 (OCoLC)1340979641 DE-627 ger DE-627 rda eng Ahadova, Aysel 1988- verfasserin (DE-588)106835268X (DE-627)820167118 (DE-576)427724783 aut Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells Aysel Ahadova, Johannes Gebert, Magnus von Knebel Doeberitz, Juergen Kopitz, Matthias Kloor 9 April 2015 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am TT.MM.JJJ High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 cellular glucose metabolism glycobiology membrane proteins Gebert, Johannes verfasserin (DE-588)1033923567 (DE-627)743674731 (DE-576)381600688 aut Knebel Doeberitz, Magnus von verfasserin (DE-588)1022165291 (DE-627)71693289X (DE-576)364934239 aut Kopitz, Jürgen verfasserin (DE-588)1033923397 (DE-627)743674472 (DE-576)16530393X aut Kloor, Matthias 1972- verfasserin (DE-588)124552803 (DE-627)363416609 (DE-576)294228616 aut Enthalten in International Union of Biochemistry and Molecular Biology IUBMB life Weinheim [u.a.] : Wiley-VCH, 1999 67(2015), 3, Seite 218-226 Online-Ressource (DE-627)31368040X (DE-600)2009952-6 (DE-576)27387831X 1521-6551 nnns volume:67 year:2015 number:3 pages:218-226 extent:9 http://dx.doi.org/10.1002/iub.1364 Verlag Resolving-System kostenfrei Volltext http://onlinelibrary.wiley.com/doi/10.1002/iub.1364/abstract Verlag kostenfrei Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 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_2018 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_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 GBV_ILN_2403 GBV_ILN_2403 ISIL_DE-LFER AR 67 2015 3 218-226 9 2013 01 DE-16-250 2981429426 00 --%%-- --%%-- --%%-- --%%-- l01 25-09-17 2403 01 DE-LFER 298371876X 00 --%%-- --%%-- n --%%-- l01 10-10-17 2403 01 DE-LFER http://dx.doi.org/10.1002/iub.1364 2013 01 DE-16-250 00 s hd2015 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_9 2013 01 DE-16-250 04 p (DE-627)1503432874 Ahadova, Aysel 2013 01 DE-16-250 04 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_1 2013 01 DE-16-250 05 p (DE-627)1451604718 Gebert, Johannes 2013 01 DE-16-250 05 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_2 2013 01 DE-16-250 06 p (DE-627)1435319745 Knebel Doeberitz, Magnus von 2013 01 DE-16-250 06 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 06 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 06 s pos_3 2013 01 DE-16-250 07 p (DE-627)1451604467 Kopitz, Jürgen 2013 01 DE-16-250 07 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 07 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 07 s pos_4 2013 01 DE-16-250 08 p (DE-627)1434888363 Kloor, Matthias 2013 01 DE-16-250 08 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 08 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 08 s pos_5
allfields_unstemmed	10.1002/iub.1364 doi (DE-627)1563793873 (DE-576)493793879 (DE-599)BSZ493793879 (OCoLC)1340979641 DE-627 ger DE-627 rda eng Ahadova, Aysel 1988- verfasserin (DE-588)106835268X (DE-627)820167118 (DE-576)427724783 aut Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells Aysel Ahadova, Johannes Gebert, Magnus von Knebel Doeberitz, Juergen Kopitz, Matthias Kloor 9 April 2015 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am TT.MM.JJJ High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 cellular glucose metabolism glycobiology membrane proteins Gebert, Johannes verfasserin (DE-588)1033923567 (DE-627)743674731 (DE-576)381600688 aut Knebel Doeberitz, Magnus von verfasserin (DE-588)1022165291 (DE-627)71693289X (DE-576)364934239 aut Kopitz, Jürgen verfasserin (DE-588)1033923397 (DE-627)743674472 (DE-576)16530393X aut Kloor, Matthias 1972- verfasserin (DE-588)124552803 (DE-627)363416609 (DE-576)294228616 aut Enthalten in International Union of Biochemistry and Molecular Biology IUBMB life Weinheim [u.a.] : Wiley-VCH, 1999 67(2015), 3, Seite 218-226 Online-Ressource (DE-627)31368040X (DE-600)2009952-6 (DE-576)27387831X 1521-6551 nnns volume:67 year:2015 number:3 pages:218-226 extent:9 http://dx.doi.org/10.1002/iub.1364 Verlag Resolving-System kostenfrei Volltext http://onlinelibrary.wiley.com/doi/10.1002/iub.1364/abstract Verlag kostenfrei Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 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_2018 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_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 GBV_ILN_2403 GBV_ILN_2403 ISIL_DE-LFER AR 67 2015 3 218-226 9 2013 01 DE-16-250 2981429426 00 --%%-- --%%-- --%%-- --%%-- l01 25-09-17 2403 01 DE-LFER 298371876X 00 --%%-- --%%-- n --%%-- l01 10-10-17 2403 01 DE-LFER http://dx.doi.org/10.1002/iub.1364 2013 01 DE-16-250 00 s hd2015 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_9 2013 01 DE-16-250 04 p (DE-627)1503432874 Ahadova, Aysel 2013 01 DE-16-250 04 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_1 2013 01 DE-16-250 05 p (DE-627)1451604718 Gebert, Johannes 2013 01 DE-16-250 05 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_2 2013 01 DE-16-250 06 p (DE-627)1435319745 Knebel Doeberitz, Magnus von 2013 01 DE-16-250 06 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 06 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 06 s pos_3 2013 01 DE-16-250 07 p (DE-627)1451604467 Kopitz, Jürgen 2013 01 DE-16-250 07 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 07 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 07 s pos_4 2013 01 DE-16-250 08 p (DE-627)1434888363 Kloor, Matthias 2013 01 DE-16-250 08 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 08 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 08 s pos_5
allfieldsGer	10.1002/iub.1364 doi (DE-627)1563793873 (DE-576)493793879 (DE-599)BSZ493793879 (OCoLC)1340979641 DE-627 ger DE-627 rda eng Ahadova, Aysel 1988- verfasserin (DE-588)106835268X (DE-627)820167118 (DE-576)427724783 aut Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells Aysel Ahadova, Johannes Gebert, Magnus von Knebel Doeberitz, Juergen Kopitz, Matthias Kloor 9 April 2015 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am TT.MM.JJJ High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 cellular glucose metabolism glycobiology membrane proteins Gebert, Johannes verfasserin (DE-588)1033923567 (DE-627)743674731 (DE-576)381600688 aut Knebel Doeberitz, Magnus von verfasserin (DE-588)1022165291 (DE-627)71693289X (DE-576)364934239 aut Kopitz, Jürgen verfasserin (DE-588)1033923397 (DE-627)743674472 (DE-576)16530393X aut Kloor, Matthias 1972- verfasserin (DE-588)124552803 (DE-627)363416609 (DE-576)294228616 aut Enthalten in International Union of Biochemistry and Molecular Biology IUBMB life Weinheim [u.a.] : Wiley-VCH, 1999 67(2015), 3, Seite 218-226 Online-Ressource (DE-627)31368040X (DE-600)2009952-6 (DE-576)27387831X 1521-6551 nnns volume:67 year:2015 number:3 pages:218-226 extent:9 http://dx.doi.org/10.1002/iub.1364 Verlag Resolving-System kostenfrei Volltext http://onlinelibrary.wiley.com/doi/10.1002/iub.1364/abstract Verlag kostenfrei Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 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_2018 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_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 GBV_ILN_2403 GBV_ILN_2403 ISIL_DE-LFER AR 67 2015 3 218-226 9 2013 01 DE-16-250 2981429426 00 --%%-- --%%-- --%%-- --%%-- l01 25-09-17 2403 01 DE-LFER 298371876X 00 --%%-- --%%-- n --%%-- l01 10-10-17 2403 01 DE-LFER http://dx.doi.org/10.1002/iub.1364 2013 01 DE-16-250 00 s hd2015 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_9 2013 01 DE-16-250 04 p (DE-627)1503432874 Ahadova, Aysel 2013 01 DE-16-250 04 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_1 2013 01 DE-16-250 05 p (DE-627)1451604718 Gebert, Johannes 2013 01 DE-16-250 05 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_2 2013 01 DE-16-250 06 p (DE-627)1435319745 Knebel Doeberitz, Magnus von 2013 01 DE-16-250 06 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 06 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 06 s pos_3 2013 01 DE-16-250 07 p (DE-627)1451604467 Kopitz, Jürgen 2013 01 DE-16-250 07 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 07 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 07 s pos_4 2013 01 DE-16-250 08 p (DE-627)1434888363 Kloor, Matthias 2013 01 DE-16-250 08 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 08 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 08 s pos_5
allfieldsSound	10.1002/iub.1364 doi (DE-627)1563793873 (DE-576)493793879 (DE-599)BSZ493793879 (OCoLC)1340979641 DE-627 ger DE-627 rda eng Ahadova, Aysel 1988- verfasserin (DE-588)106835268X (DE-627)820167118 (DE-576)427724783 aut Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells Aysel Ahadova, Johannes Gebert, Magnus von Knebel Doeberitz, Juergen Kopitz, Matthias Kloor 9 April 2015 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am TT.MM.JJJ High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 cellular glucose metabolism glycobiology membrane proteins Gebert, Johannes verfasserin (DE-588)1033923567 (DE-627)743674731 (DE-576)381600688 aut Knebel Doeberitz, Magnus von verfasserin (DE-588)1022165291 (DE-627)71693289X (DE-576)364934239 aut Kopitz, Jürgen verfasserin (DE-588)1033923397 (DE-627)743674472 (DE-576)16530393X aut Kloor, Matthias 1972- verfasserin (DE-588)124552803 (DE-627)363416609 (DE-576)294228616 aut Enthalten in International Union of Biochemistry and Molecular Biology IUBMB life Weinheim [u.a.] : Wiley-VCH, 1999 67(2015), 3, Seite 218-226 Online-Ressource (DE-627)31368040X (DE-600)2009952-6 (DE-576)27387831X 1521-6551 nnns volume:67 year:2015 number:3 pages:218-226 extent:9 http://dx.doi.org/10.1002/iub.1364 Verlag Resolving-System kostenfrei Volltext http://onlinelibrary.wiley.com/doi/10.1002/iub.1364/abstract Verlag kostenfrei Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 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_2018 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_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 GBV_ILN_2403 GBV_ILN_2403 ISIL_DE-LFER AR 67 2015 3 218-226 9 2013 01 DE-16-250 2981429426 00 --%%-- --%%-- --%%-- --%%-- l01 25-09-17 2403 01 DE-LFER 298371876X 00 --%%-- --%%-- n --%%-- l01 10-10-17 2403 01 DE-LFER http://dx.doi.org/10.1002/iub.1364 2013 01 DE-16-250 00 s hd2015 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_9 2013 01 DE-16-250 04 p (DE-627)1503432874 Ahadova, Aysel 2013 01 DE-16-250 04 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_1 2013 01 DE-16-250 05 p (DE-627)1451604718 Gebert, Johannes 2013 01 DE-16-250 05 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_2 2013 01 DE-16-250 06 p (DE-627)1435319745 Knebel Doeberitz, Magnus von 2013 01 DE-16-250 06 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 06 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 06 s pos_3 2013 01 DE-16-250 07 p (DE-627)1451604467 Kopitz, Jürgen 2013 01 DE-16-250 07 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 07 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 07 s pos_4 2013 01 DE-16-250 08 p (DE-627)1434888363 Kloor, Matthias 2013 01 DE-16-250 08 k (DE-627)1416741658 Pathologisches Institut 2013 01 DE-16-250 08 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 08 s pos_5
language	English
source	Enthalten in IUBMB life 67(2015), 3, Seite 218-226 volume:67 year:2015 number:3 pages:218-226 extent:9
sourceStr	Enthalten in IUBMB life 67(2015), 3, Seite 218-226 volume:67 year:2015 number:3 pages:218-226 extent:9
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authorswithroles_txt_mv	Ahadova, Aysel @@aut@@ Gebert, Johannes @@aut@@ Knebel Doeberitz, Magnus von @@aut@@ Kopitz, Jürgen @@aut@@ Kloor, Matthias @@aut@@
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topic	misc cellular glucose metabolism misc glycobiology misc membrane proteins 2013 hd2015 2013 wissenschaftlicher Artikel (Zeitschrift) 2013 per_5 2013 s_9 2013 Ahadova, Aysel 2013 Pathologisches Institut 2013 Verfasser 2013 pos_1 2013 Gebert, Johannes 2013 pos_2 2013 Knebel Doeberitz, Magnus von 2013 pos_3 2013 Kopitz, Jürgen 2013 pos_4 2013 Kloor, Matthias 2013 pos_5
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title	Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells
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title_full	Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells Aysel Ahadova, Johannes Gebert, Magnus von Knebel Doeberitz, Juergen Kopitz, Matthias Kloor
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title_sort	dose-dependent effect of 2-deoxy-d-glucose on glycoprotein mannosylation in cancer cells
title_auth	Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells
abstract	High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 Gesehen am TT.MM.JJJ
abstractGer	High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 Gesehen am TT.MM.JJJ
abstract_unstemmed	High glucose consumption due to Warburg effect is one of the metabolic hallmarks of cancer. Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015 Gesehen am TT.MM.JJJ
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title_short	Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells
url	http://dx.doi.org/10.1002/iub.1364 http://onlinelibrary.wiley.com/doi/10.1002/iub.1364/abstract
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Consequently, glucose antimetabolites, such as 2-deoxy-glucose (2DG), can induce substantial growth inhibition of cancer cells. However, the inhibition of metabolic pathways is not the sole effect of 2DG on cancer cells. As mannose-mimetic molecule, 2DG is believed to interfere with normal glycosylation of proteins in cells. Here, we address how 2DG influences protein glycosylation in cancer cells and discuss possible implications of the consequences of this influence. In detail, six colorectal cancer cell lines were examined for alterations of protein glycosylation by measuring monosaccharide incorporation into cellular glycoproteins and cell surface glycosylation by lectin FACS. A significant increase in mannose incorporation was observed on treatment with 2DG (1 mM for 48 h), which was also reflected by an increased binding of the mannose-binding lectin Concanavalin A in FACS analysis. This phenomenon, which could be reversed by external addition of mannose, was not caused by 2DG-mediated mannosidase inhibition, as shown by pulse-chase experiments, arguing in favor of the hypothesis that 2DG directly influenced the incorporation of mannose. Increased mannose content was generally observed in cellular glycoproteins, including glycoproteins isolated from the plasma membrane fraction. Our results indicate that 2DG at low doses, which have only a limited metabolism-related effect on glycosylation, induces a strong increase in mannose incorporation into cellular glycoproteins. On the other hand, higher 2DG concentrations (10 and 20 mM) led to a significant decrease of absolute mannose incorporation accompanied by a dramatically reduced protein synthesis rate. 2DG-induced alterations of glycosylation may represent a novel mechanism potentially explaining the varied effects of 2DG on cancer cells. Moreover, 2DG treatment may open a path toward novel diagnostic and cancer therapeutic approaches, which specifically target altered glycoantigen structures induced by 2DG. © 2015 IUBMB Life, 67(3):218-226, 2015</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">cellular glucose metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">glycobiology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">membrane proteins</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gebert, Johannes</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(DE-588)1033923567</subfield><subfield code="0">(DE-627)743674731</subfield><subfield code="0">(DE-576)381600688</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Knebel Doeberitz, Magnus von</subfield><subfield code="e">verfasserin</subfield><subfield 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Dose-dependent effect of 2-deoxy-D-glucose on glycoprotein mannosylation in cancer cells

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