Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella)

Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has n...
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Autor*in:	Wang, Congcong [verfasserIn] Han, Chunzhou [verfasserIn] Li, Tao [verfasserIn] Yang, Dehao [verfasserIn] Shen, Xiaojiong [verfasserIn] Fan, Yinxin [verfasserIn] Xu, Yang [verfasserIn] Zheng, Wenli [verfasserIn] Fei, Chenzhong [verfasserIn] Zhang, Lifang [verfasserIn] Xue, Feiqun [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2013

Schlagwörter:	Gapdh mRNA Coccidiosis Glycolytic Activity GAPDH Activity GAPDH Protein

Übergeordnetes Werk:	Enthalten in: Veterinary research - London : BioMed Central, 1993, 44(2013), 1 vom: 07. Mai
Übergeordnetes Werk:	volume:44 ; year:2013 ; number:1 ; day:07 ; month:05

Links:	Volltext

DOI / URN:	10.1186/1297-9716-44-29

Katalog-ID:	SPR031816207

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245	1	0	\|a Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella)
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520			\|a Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group.
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allfields	10.1186/1297-9716-44-29 doi (DE-627)SPR031816207 (SPR)1297-9716-44-29-e DE-627 ger DE-627 rakwb eng 630 640 ASE 46.00 bkl Wang, Congcong verfasserin aut Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella) 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group. Gapdh mRNA (dpeaa)DE-He213 Coccidiosis (dpeaa)DE-He213 Glycolytic Activity (dpeaa)DE-He213 GAPDH Activity (dpeaa)DE-He213 GAPDH Protein (dpeaa)DE-He213 Han, Chunzhou verfasserin aut Li, Tao verfasserin aut Yang, Dehao verfasserin aut Shen, Xiaojiong verfasserin aut Fan, Yinxin verfasserin aut Xu, Yang verfasserin aut Zheng, Wenli verfasserin aut Fei, Chenzhong verfasserin aut Zhang, Lifang verfasserin aut Xue, Feiqun verfasserin aut Enthalten in Veterinary research London : BioMed Central, 1993 44(2013), 1 vom: 07. Mai (DE-627)312853653 (DE-600)2012391-7 1297-9716 nnns volume:44 year:2013 number:1 day:07 month:05 https://dx.doi.org/10.1186/1297-9716-44-29 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 46.00 ASE AR 44 2013 1 07 05
spelling	10.1186/1297-9716-44-29 doi (DE-627)SPR031816207 (SPR)1297-9716-44-29-e DE-627 ger DE-627 rakwb eng 630 640 ASE 46.00 bkl Wang, Congcong verfasserin aut Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella) 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group. Gapdh mRNA (dpeaa)DE-He213 Coccidiosis (dpeaa)DE-He213 Glycolytic Activity (dpeaa)DE-He213 GAPDH Activity (dpeaa)DE-He213 GAPDH Protein (dpeaa)DE-He213 Han, Chunzhou verfasserin aut Li, Tao verfasserin aut Yang, Dehao verfasserin aut Shen, Xiaojiong verfasserin aut Fan, Yinxin verfasserin aut Xu, Yang verfasserin aut Zheng, Wenli verfasserin aut Fei, Chenzhong verfasserin aut Zhang, Lifang verfasserin aut Xue, Feiqun verfasserin aut Enthalten in Veterinary research London : BioMed Central, 1993 44(2013), 1 vom: 07. Mai (DE-627)312853653 (DE-600)2012391-7 1297-9716 nnns volume:44 year:2013 number:1 day:07 month:05 https://dx.doi.org/10.1186/1297-9716-44-29 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 46.00 ASE AR 44 2013 1 07 05
allfields_unstemmed	10.1186/1297-9716-44-29 doi (DE-627)SPR031816207 (SPR)1297-9716-44-29-e DE-627 ger DE-627 rakwb eng 630 640 ASE 46.00 bkl Wang, Congcong verfasserin aut Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella) 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group. Gapdh mRNA (dpeaa)DE-He213 Coccidiosis (dpeaa)DE-He213 Glycolytic Activity (dpeaa)DE-He213 GAPDH Activity (dpeaa)DE-He213 GAPDH Protein (dpeaa)DE-He213 Han, Chunzhou verfasserin aut Li, Tao verfasserin aut Yang, Dehao verfasserin aut Shen, Xiaojiong verfasserin aut Fan, Yinxin verfasserin aut Xu, Yang verfasserin aut Zheng, Wenli verfasserin aut Fei, Chenzhong verfasserin aut Zhang, Lifang verfasserin aut Xue, Feiqun verfasserin aut Enthalten in Veterinary research London : BioMed Central, 1993 44(2013), 1 vom: 07. Mai (DE-627)312853653 (DE-600)2012391-7 1297-9716 nnns volume:44 year:2013 number:1 day:07 month:05 https://dx.doi.org/10.1186/1297-9716-44-29 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 46.00 ASE AR 44 2013 1 07 05
allfieldsGer	10.1186/1297-9716-44-29 doi (DE-627)SPR031816207 (SPR)1297-9716-44-29-e DE-627 ger DE-627 rakwb eng 630 640 ASE 46.00 bkl Wang, Congcong verfasserin aut Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella) 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group. Gapdh mRNA (dpeaa)DE-He213 Coccidiosis (dpeaa)DE-He213 Glycolytic Activity (dpeaa)DE-He213 GAPDH Activity (dpeaa)DE-He213 GAPDH Protein (dpeaa)DE-He213 Han, Chunzhou verfasserin aut Li, Tao verfasserin aut Yang, Dehao verfasserin aut Shen, Xiaojiong verfasserin aut Fan, Yinxin verfasserin aut Xu, Yang verfasserin aut Zheng, Wenli verfasserin aut Fei, Chenzhong verfasserin aut Zhang, Lifang verfasserin aut Xue, Feiqun verfasserin aut Enthalten in Veterinary research London : BioMed Central, 1993 44(2013), 1 vom: 07. Mai (DE-627)312853653 (DE-600)2012391-7 1297-9716 nnns volume:44 year:2013 number:1 day:07 month:05 https://dx.doi.org/10.1186/1297-9716-44-29 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 46.00 ASE AR 44 2013 1 07 05
allfieldsSound	10.1186/1297-9716-44-29 doi (DE-627)SPR031816207 (SPR)1297-9716-44-29-e DE-627 ger DE-627 rakwb eng 630 640 ASE 46.00 bkl Wang, Congcong verfasserin aut Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella) 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group. Gapdh mRNA (dpeaa)DE-He213 Coccidiosis (dpeaa)DE-He213 Glycolytic Activity (dpeaa)DE-He213 GAPDH Activity (dpeaa)DE-He213 GAPDH Protein (dpeaa)DE-He213 Han, Chunzhou verfasserin aut Li, Tao verfasserin aut Yang, Dehao verfasserin aut Shen, Xiaojiong verfasserin aut Fan, Yinxin verfasserin aut Xu, Yang verfasserin aut Zheng, Wenli verfasserin aut Fei, Chenzhong verfasserin aut Zhang, Lifang verfasserin aut Xue, Feiqun verfasserin aut Enthalten in Veterinary research London : BioMed Central, 1993 44(2013), 1 vom: 07. Mai (DE-627)312853653 (DE-600)2012391-7 1297-9716 nnns volume:44 year:2013 number:1 day:07 month:05 https://dx.doi.org/10.1186/1297-9716-44-29 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 46.00 ASE AR 44 2013 1 07 05
language	English
source	Enthalten in Veterinary research 44(2013), 1 vom: 07. Mai volume:44 year:2013 number:1 day:07 month:05
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topic_facet	Gapdh mRNA Coccidiosis Glycolytic Activity GAPDH Activity GAPDH Protein
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authorswithroles_txt_mv	Wang, Congcong @@aut@@ Han, Chunzhou @@aut@@ Li, Tao @@aut@@ Yang, Dehao @@aut@@ Shen, Xiaojiong @@aut@@ Fan, Yinxin @@aut@@ Xu, Yang @@aut@@ Zheng, Wenli @@aut@@ Fei, Chenzhong @@aut@@ Zhang, Lifang @@aut@@ Xue, Feiqun @@aut@@
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author	Wang, Congcong
spellingShingle	Wang, Congcong ddc 630 bkl 46.00 misc Gapdh mRNA misc Coccidiosis misc Glycolytic Activity misc GAPDH Activity misc GAPDH Protein Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella)
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topic_title	630 640 ASE 46.00 bkl Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella) Gapdh mRNA (dpeaa)DE-He213 Coccidiosis (dpeaa)DE-He213 Glycolytic Activity (dpeaa)DE-He213 GAPDH Activity (dpeaa)DE-He213 GAPDH Protein (dpeaa)DE-He213
topic	ddc 630 bkl 46.00 misc Gapdh mRNA misc Coccidiosis misc Glycolytic Activity misc GAPDH Activity misc GAPDH Protein
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title	Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella)
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title_full	Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella)
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author_browse	Wang, Congcong Han, Chunzhou Li, Tao Yang, Dehao Shen, Xiaojiong Fan, Yinxin Xu, Yang Zheng, Wenli Fei, Chenzhong Zhang, Lifang Xue, Feiqun
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title_sort	nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in eimeria tenella (e. tenella)
title_auth	Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella)
abstract	Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group.
abstractGer	Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group.
abstract_unstemmed	Abstract In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. The data show significant increases in caspase-3 and caspase-9 activities in the diclazuril-treated group.
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title_short	Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella)
url	https://dx.doi.org/10.1186/1297-9716-44-29
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author2	Han, Chunzhou Li, Tao Yang, Dehao Shen, Xiaojiong Fan, Yinxin Xu, Yang Zheng, Wenli Fei, Chenzhong Zhang, Lifang Xue, Feiqun
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up_date	2024-07-04T01:22:10.178Z
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However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella). We found that upon treatment of parasites with diclazuril, the expression levels of GAPDH transcript and protein were significantly increased in second-generation merozoites. Then, we examined the subcellular localization of GAPDH by fluorescence microscopy and Western blot analysis. The results show that a considerable amount of GAPDH protein appeared in the nucleus within diclazuril-treated second-generation merozoites; in contrast, the control group had very low levels of GAPDH in the nucleus. The glycolytic activity of GAPDH was kinetically analyzed in different subcellular fractions. A substantial decrease (48.5%) in glycolytic activity of GAPDH in the nucleus was displayed. Moreover, the activities of caspases-3, -9, and −8 were measured in cell extracts using specific caspase substrates. 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Nuclear translocation and accumulation of glyceraldehyde-3-phosphate dehydrogenase involved in diclazuril-induced apoptosis in Eimeria tenella (E. tenella)

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