Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts

Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Hongmei Xu [verfasserIn] Yueyue Li [verfasserIn] Qiao Li [verfasserIn] Zifeng Ma [verfasserIn] Shi Yin [verfasserIn] Honghong He [verfasserIn] Yan Xiong [verfasserIn] Xianrong Xiong [verfasserIn] Daoliang Lan [verfasserIn] Jian Li [verfasserIn] Wei Fu [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	yak fetal fibroblasts ferroptosis Bisphenol S

Übergeordnetes Werk:	In: Animals - MDPI AG, 2011, 13(2023), 24, p 3832
Übergeordnetes Werk:	volume:13 ; year:2023 ; number:24, p 3832

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/ani13243832

Katalog-ID:	DOAJ098922793

Internformat


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520			\|a Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species.
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allfields	10.3390/ani13243832 doi (DE-627)DOAJ098922793 (DE-599)DOAJ833df95838e34f5c814b0f14aa8d2af5 DE-627 ger DE-627 rakwb eng SF600-1100 QL1-991 Hongmei Xu verfasserin aut Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species. yak <i<DHODH</i< gene fetal fibroblasts ferroptosis Bisphenol S Veterinary medicine Zoology Yueyue Li verfasserin aut Qiao Li verfasserin aut Zifeng Ma verfasserin aut Shi Yin verfasserin aut Honghong He verfasserin aut Yan Xiong verfasserin aut Xianrong Xiong verfasserin aut Daoliang Lan verfasserin aut Jian Li verfasserin aut Wei Fu verfasserin aut In Animals MDPI AG, 2011 13(2023), 24, p 3832 (DE-627)657589306 (DE-600)2606558-7 20762615 nnns volume:13 year:2023 number:24, p 3832 https://doi.org/10.3390/ani13243832 kostenfrei https://doaj.org/article/833df95838e34f5c814b0f14aa8d2af5 kostenfrei https://www.mdpi.com/2076-2615/13/24/3832 kostenfrei https://doaj.org/toc/2076-2615 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 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 13 2023 24, p 3832
spelling	10.3390/ani13243832 doi (DE-627)DOAJ098922793 (DE-599)DOAJ833df95838e34f5c814b0f14aa8d2af5 DE-627 ger DE-627 rakwb eng SF600-1100 QL1-991 Hongmei Xu verfasserin aut Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species. yak <i<DHODH</i< gene fetal fibroblasts ferroptosis Bisphenol S Veterinary medicine Zoology Yueyue Li verfasserin aut Qiao Li verfasserin aut Zifeng Ma verfasserin aut Shi Yin verfasserin aut Honghong He verfasserin aut Yan Xiong verfasserin aut Xianrong Xiong verfasserin aut Daoliang Lan verfasserin aut Jian Li verfasserin aut Wei Fu verfasserin aut In Animals MDPI AG, 2011 13(2023), 24, p 3832 (DE-627)657589306 (DE-600)2606558-7 20762615 nnns volume:13 year:2023 number:24, p 3832 https://doi.org/10.3390/ani13243832 kostenfrei https://doaj.org/article/833df95838e34f5c814b0f14aa8d2af5 kostenfrei https://www.mdpi.com/2076-2615/13/24/3832 kostenfrei https://doaj.org/toc/2076-2615 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 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 13 2023 24, p 3832
allfields_unstemmed	10.3390/ani13243832 doi (DE-627)DOAJ098922793 (DE-599)DOAJ833df95838e34f5c814b0f14aa8d2af5 DE-627 ger DE-627 rakwb eng SF600-1100 QL1-991 Hongmei Xu verfasserin aut Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species. yak <i<DHODH</i< gene fetal fibroblasts ferroptosis Bisphenol S Veterinary medicine Zoology Yueyue Li verfasserin aut Qiao Li verfasserin aut Zifeng Ma verfasserin aut Shi Yin verfasserin aut Honghong He verfasserin aut Yan Xiong verfasserin aut Xianrong Xiong verfasserin aut Daoliang Lan verfasserin aut Jian Li verfasserin aut Wei Fu verfasserin aut In Animals MDPI AG, 2011 13(2023), 24, p 3832 (DE-627)657589306 (DE-600)2606558-7 20762615 nnns volume:13 year:2023 number:24, p 3832 https://doi.org/10.3390/ani13243832 kostenfrei https://doaj.org/article/833df95838e34f5c814b0f14aa8d2af5 kostenfrei https://www.mdpi.com/2076-2615/13/24/3832 kostenfrei https://doaj.org/toc/2076-2615 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 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 13 2023 24, p 3832
allfieldsGer	10.3390/ani13243832 doi (DE-627)DOAJ098922793 (DE-599)DOAJ833df95838e34f5c814b0f14aa8d2af5 DE-627 ger DE-627 rakwb eng SF600-1100 QL1-991 Hongmei Xu verfasserin aut Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species. yak <i<DHODH</i< gene fetal fibroblasts ferroptosis Bisphenol S Veterinary medicine Zoology Yueyue Li verfasserin aut Qiao Li verfasserin aut Zifeng Ma verfasserin aut Shi Yin verfasserin aut Honghong He verfasserin aut Yan Xiong verfasserin aut Xianrong Xiong verfasserin aut Daoliang Lan verfasserin aut Jian Li verfasserin aut Wei Fu verfasserin aut In Animals MDPI AG, 2011 13(2023), 24, p 3832 (DE-627)657589306 (DE-600)2606558-7 20762615 nnns volume:13 year:2023 number:24, p 3832 https://doi.org/10.3390/ani13243832 kostenfrei https://doaj.org/article/833df95838e34f5c814b0f14aa8d2af5 kostenfrei https://www.mdpi.com/2076-2615/13/24/3832 kostenfrei https://doaj.org/toc/2076-2615 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 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 13 2023 24, p 3832
allfieldsSound	10.3390/ani13243832 doi (DE-627)DOAJ098922793 (DE-599)DOAJ833df95838e34f5c814b0f14aa8d2af5 DE-627 ger DE-627 rakwb eng SF600-1100 QL1-991 Hongmei Xu verfasserin aut Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species. yak <i<DHODH</i< gene fetal fibroblasts ferroptosis Bisphenol S Veterinary medicine Zoology Yueyue Li verfasserin aut Qiao Li verfasserin aut Zifeng Ma verfasserin aut Shi Yin verfasserin aut Honghong He verfasserin aut Yan Xiong verfasserin aut Xianrong Xiong verfasserin aut Daoliang Lan verfasserin aut Jian Li verfasserin aut Wei Fu verfasserin aut In Animals MDPI AG, 2011 13(2023), 24, p 3832 (DE-627)657589306 (DE-600)2606558-7 20762615 nnns volume:13 year:2023 number:24, p 3832 https://doi.org/10.3390/ani13243832 kostenfrei https://doaj.org/article/833df95838e34f5c814b0f14aa8d2af5 kostenfrei https://www.mdpi.com/2076-2615/13/24/3832 kostenfrei https://doaj.org/toc/2076-2615 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 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 13 2023 24, p 3832
language	English
source	In Animals 13(2023), 24, p 3832 volume:13 year:2023 number:24, p 3832
sourceStr	In Animals 13(2023), 24, p 3832 volume:13 year:2023 number:24, p 3832
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	yak <i<DHODH</i< gene fetal fibroblasts ferroptosis Bisphenol S Veterinary medicine Zoology
isfreeaccess_bool	true
container_title	Animals
authorswithroles_txt_mv	Hongmei Xu @@aut@@ Yueyue Li @@aut@@ Qiao Li @@aut@@ Zifeng Ma @@aut@@ Shi Yin @@aut@@ Honghong He @@aut@@ Yan Xiong @@aut@@ Xianrong Xiong @@aut@@ Daoliang Lan @@aut@@ Jian Li @@aut@@ Wei Fu @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	657589306
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Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. 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callnumber-first	S - Agriculture
author	Hongmei Xu
spellingShingle	Hongmei Xu misc SF600-1100 misc QL1-991 misc yak misc <i<DHODH</i< gene misc fetal fibroblasts misc ferroptosis misc Bisphenol S misc Veterinary medicine misc Zoology Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts
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topic_title	SF600-1100 QL1-991 Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts yak <i<DHODH</i< gene fetal fibroblasts ferroptosis Bisphenol S
topic	misc SF600-1100 misc QL1-991 misc yak misc <i<DHODH</i< gene misc fetal fibroblasts misc ferroptosis misc Bisphenol S misc Veterinary medicine misc Zoology
topic_unstemmed	misc SF600-1100 misc QL1-991 misc yak misc <i<DHODH</i< gene misc fetal fibroblasts misc ferroptosis misc Bisphenol S misc Veterinary medicine misc Zoology
topic_browse	misc SF600-1100 misc QL1-991 misc yak misc <i<DHODH</i< gene misc fetal fibroblasts misc ferroptosis misc Bisphenol S misc Veterinary medicine misc Zoology
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title	Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts
ctrlnum	(DE-627)DOAJ098922793 (DE-599)DOAJ833df95838e34f5c814b0f14aa8d2af5
title_full	Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts
author_sort	Hongmei Xu
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author_browse	Hongmei Xu Yueyue Li Qiao Li Zifeng Ma Shi Yin Honghong He Yan Xiong Xianrong Xiong Daoliang Lan Jian Li Wei Fu
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class	SF600-1100 QL1-991
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author-letter	Hongmei Xu
doi_str_mv	10.3390/ani13243832
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title_sort	cloning and characterization of yak <i<dhodh</i< gene and its functional studies in a bisphenol s-induced ferroptosis model of fetal fibroblasts
callnumber	SF600-1100
title_auth	Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts
abstract	Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species.
abstractGer	Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species.
abstract_unstemmed	Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme of <i<de novo</i< biosynthesis of pyrimidine. Although the involvement of DHODH in resisting ferroptosis has been successively reported in recent years, which greatly advanced the understanding of the mechanism of programmed cell death (PCD), the genetic sequence of the yak <i<DHODH</i< gene and its roles in ferroptosis are still unknown. For this purpose, we firstly cloned the coding region sequence of <i<DHODH</i< (1188 bp) from yak liver and conducted a characterization analysis of its predictive protein that consists of 395 amino acids. We found that the coding region of the yak <i<DHODH</i< gene presented high conservation among species. Second, the expression profile of the <i<DHODH</i< gene in various yak tissues was investigated using RT-qPCR. The results demonstrated that <i<DHODH</i< was widely expressed in different yak tissues, with particularly high levels in the spleen, heart, and liver. Third, to investigate the involvement of <i<DHODH</i< in regulating ferroptosis in cells, yak skin fibroblasts (YSFs) were isolated from fetuses. And then, bisphenol S (BPS) was used to induce the <i<in vitro</i< ferroptosis model of YSFs. We observed that BPS decreased the cell viability (CCK8) and membrane potential (JC-1) of YSFs in a dose-dependent manner and induced oxidative stress by elevating reactive oxygen species (ROS). Simultaneously, it was evident that BPS effectively augmented the indicators associated with ferroptosis (MDA and BODIPY staining) and reduced GSH levels. Importantly, the co-administration of Ferrostatin-1 (Fer), a potent inhibitor of ferroptosis, significantly alleviated the aforementioned markers, thereby confirming the successful induction of ferroptosis in YSFs by BPS. Finally, overexpression plasmids and siRNAs of the yak <i<DHODH</i< gene were designed and transfected respectively into BPS-cultured YSFs to modulate <i<DHODH</i< expression. The findings revealed that <i<DHODH</i< overexpression alleviated the occurrence of BPS-induced ferroptosis, while interference of <i<DHODH</i< intensified the ferroptosis process in YSFs. In summary, we successfully cloned the coding region of the yak <i<DHODH</i< gene, demonstrating its remarkable conservation across species. Moreover, using BPS-induced ferroptosis in YSFs as the model, the study confirmed the role of the <i<DHODH</i< gene in resisting ferroptosis in yaks. These results offer valuable theoretical foundations for future investigations into the functionality of the yak <i<DHODH</i< gene and the underlying mechanisms of ferroptosis in this species.
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container_issue	24, p 3832
title_short	Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts
url	https://doi.org/10.3390/ani13243832 https://doaj.org/article/833df95838e34f5c814b0f14aa8d2af5 https://www.mdpi.com/2076-2615/13/24/3832 https://doaj.org/toc/2076-2615
remote_bool	true
author2	Yueyue Li Qiao Li Zifeng Ma Shi Yin Honghong He Yan Xiong Xianrong Xiong Daoliang Lan Jian Li Wei Fu
author2Str	Yueyue Li Qiao Li Zifeng Ma Shi Yin Honghong He Yan Xiong Xianrong Xiong Daoliang Lan Jian Li Wei Fu
ppnlink	657589306
callnumber-subject	SF - Animal Culture
mediatype_str_mv	c
isOA_txt	true
hochschulschrift_bool	false
doi_str	10.3390/ani13243832
callnumber-a	SF600-1100
up_date	2024-07-03T20:00:45.047Z
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Cloning and Characterization of Yak <i<DHODH</i< Gene and Its Functional Studies in a Bisphenol S-Induced Ferroptosis Model of Fetal Fibroblasts

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