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3.2对仔猪淋巴细胞HSP70mRNA定量的分析实验结果表明,仔猪在一10~一4oC冷暴露0.5h,淋巴细胞内HSP70mRNA转录量明显升高(P<0.05),说明机体淋...
3.2 对仔猪淋巴细胞HSP70 mRNA定量的分析
实验结果表明,仔猪在一10~一4 oC冷暴露0.5 h,淋巴细胞内HSP70 mRNA转录量明显升高(P<0.05),说明机体淋巴细胞对应激源的反应速度较快,这有利于动物在遭受冷应激时及时启动保护系统,增强对外界病毒、细菌的抵抗力,减少发病率和死亡率.HSP70 mRNA的表达产物HSP70可作为抗原分子载体,由抗原或病原体激活巨噬细胞及淋巴细胞进行免疫应答时产生的各种免疫细胞因子,也可诱导HSP的产生并协同参与抗原加工、提呈,并利用其抗原特异性为T细胞免疫识别导航.脾脏和淋巴细胞中HSP70的增多可能与其免疫功能相关 [6].周舫[7]等 对冷库作业工人的血液淋巴细中HSP70与李士泽[8]等对冷应激仔猪组织中HSP70的研究都表明:0 oC组与对照组(常温)相比,HSP70表达差异显著,这与本实验结果一致.随后,转录量虽有下降,但应激3 h和6 h的转录量与基础量相比具有显著差异(P<0.05).随着应激时间的延长,在动物逐渐产生冷适应的过程中HSP70 mRNA的转录量也呈现不断下降趋势.当仔猪由冷环境转移到正常饲养温度时,HSP70 mRNA转录量又呈逐渐上升趋势,至应激恢复24 h后,由于动物逐渐适应环境,mRNA降解速度加快,其转录量下降并趋近于基础水平.在4~1O℃冷应激前后,淋巴细胞HSP70mRNA转录量无明显变化.
由此可见,冷暴露温度越低,淋巴细胞中HSP70 mRNA转录越迅速.在一1O~一4℃冷暴露12 h和24 h时,HSP70 mR—NA转录量与对照组比较差异不明显,可能与mRNA降解速度加快,寒冷对组织细胞功能造成损害,从而使HSP70 mRNA转录功能受损,或与动物对寒冷产生适应等因素有关.结束冷暴露进入室温环境,等于在初步建立的冷适应的基础上施加了新的热刺激,所以,HSP70 mRNA转录会再次增强,但由于在一1O~一4℃冷暴露时对细胞功能的损害,使得HSP70 mRNA的转录不能迅速做出反应.
通过mRNA的检测可在一定程度上反映HSP70的表达情况,HSP70的升高,有利于提高动物的自我保护机能,增强对外界不良刺激的抵抗力[9]。.冷应激时组织细胞易受损伤,蛋白折叠发生错误,导致蛋白质功能受损.HSP70可以阻止非天然肽多肽链内部或相互间的非正确折叠,或者说它们给处于折叠中间肽的多肽链提供了最多的正确折叠机会[10,11] .有人通过四膜虫细胞热休克的研究发现,有些HSP具有促进细胞内糖原异生和糖原生成的作用,使细胞内糖原贮存量增多,从而提高耐受能力[12],这与肝脏内HSP70 mRNA较快的增加有一定联系[11],因为肝脏是糖原合成代谢的场所.Ishiyama等[13](1996)也发现存在于细胞内的HSP主要起保护细胞的作用,可以抵抗不同信号通路引起的细胞凋亡.吕裕强等[14](1996)在对家兔淋巴细胞的试验中发现,尽管高温能使热耐受细胞发生形态改变,但要轻得多,甚至没有改变. 展开
实验结果表明,仔猪在一10~一4 oC冷暴露0.5 h,淋巴细胞内HSP70 mRNA转录量明显升高(P<0.05),说明机体淋巴细胞对应激源的反应速度较快,这有利于动物在遭受冷应激时及时启动保护系统,增强对外界病毒、细菌的抵抗力,减少发病率和死亡率.HSP70 mRNA的表达产物HSP70可作为抗原分子载体,由抗原或病原体激活巨噬细胞及淋巴细胞进行免疫应答时产生的各种免疫细胞因子,也可诱导HSP的产生并协同参与抗原加工、提呈,并利用其抗原特异性为T细胞免疫识别导航.脾脏和淋巴细胞中HSP70的增多可能与其免疫功能相关 [6].周舫[7]等 对冷库作业工人的血液淋巴细中HSP70与李士泽[8]等对冷应激仔猪组织中HSP70的研究都表明:0 oC组与对照组(常温)相比,HSP70表达差异显著,这与本实验结果一致.随后,转录量虽有下降,但应激3 h和6 h的转录量与基础量相比具有显著差异(P<0.05).随着应激时间的延长,在动物逐渐产生冷适应的过程中HSP70 mRNA的转录量也呈现不断下降趋势.当仔猪由冷环境转移到正常饲养温度时,HSP70 mRNA转录量又呈逐渐上升趋势,至应激恢复24 h后,由于动物逐渐适应环境,mRNA降解速度加快,其转录量下降并趋近于基础水平.在4~1O℃冷应激前后,淋巴细胞HSP70mRNA转录量无明显变化.
由此可见,冷暴露温度越低,淋巴细胞中HSP70 mRNA转录越迅速.在一1O~一4℃冷暴露12 h和24 h时,HSP70 mR—NA转录量与对照组比较差异不明显,可能与mRNA降解速度加快,寒冷对组织细胞功能造成损害,从而使HSP70 mRNA转录功能受损,或与动物对寒冷产生适应等因素有关.结束冷暴露进入室温环境,等于在初步建立的冷适应的基础上施加了新的热刺激,所以,HSP70 mRNA转录会再次增强,但由于在一1O~一4℃冷暴露时对细胞功能的损害,使得HSP70 mRNA的转录不能迅速做出反应.
通过mRNA的检测可在一定程度上反映HSP70的表达情况,HSP70的升高,有利于提高动物的自我保护机能,增强对外界不良刺激的抵抗力[9]。.冷应激时组织细胞易受损伤,蛋白折叠发生错误,导致蛋白质功能受损.HSP70可以阻止非天然肽多肽链内部或相互间的非正确折叠,或者说它们给处于折叠中间肽的多肽链提供了最多的正确折叠机会[10,11] .有人通过四膜虫细胞热休克的研究发现,有些HSP具有促进细胞内糖原异生和糖原生成的作用,使细胞内糖原贮存量增多,从而提高耐受能力[12],这与肝脏内HSP70 mRNA较快的增加有一定联系[11],因为肝脏是糖原合成代谢的场所.Ishiyama等[13](1996)也发现存在于细胞内的HSP主要起保护细胞的作用,可以抵抗不同信号通路引起的细胞凋亡.吕裕强等[14](1996)在对家兔淋巴细胞的试验中发现,尽管高温能使热耐受细胞发生形态改变,但要轻得多,甚至没有改变. 展开
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3.2 pairs of piglets lymphocytes Quantitative analysis of HSP70 mRNA
The experimental results show that piglets in a 10 ~ a 4 oC exposed to cold 0.5 h, lymphocytes within the HSP70 mRNA transcription increased significantly (P <0.05), indicate the source of the body cells of the stress response faster This is conducive to animals subjected to cold stress protection system in time to start to enhance the outside world viruses, bacteria resistance, reduce morbidity and mortality. HSP70 mRNA expression product of HSP70 antigen molecules can be used as the carrier, by the antigen or pathogen-activated macrophages and lymphocytes when the immune response to various immune cytokines, HSP can be induced to participate in the selection and coordination antigen processing, presentation, and use of its antigen-specific T cell immune recognition for navigation. Lymphocytes in the spleen and an increase in HSP70 may be related to immune function [6]. Zhou Fang [7] and other workers of the cold storage of blood in small lymphatic HSP70 and Lee士泽[8], such as cold stress on piglet tissue HSP70 studies have shown that: 0 oC group and the control group (room temperature) compared to, HSP70 expression difference significantly, which agreed with the experimental results. Subsequently, although the decline in the amount of transcription, but the stress-3 h and 6 h the amount of transcription compared with the amount based on significant differences (P <0.05). With the stress time, resulting in a gradual cooling of animals to adapt to the process of transcription of HSP70 mRNA also showed a downward trend continued. When the piglets from the transfer of cold to the normal rearing temperature, HSP70 mRNA transcription volume also showed a gradual upward trend, to the restoration of 24 h after stress, due to gradually adapt to the environment of animals, mRNA degradation faster decline in their transcription and near the basis of level. 4 ~ 1O ℃ in cold stress before and after transcription HSP70mRNA lymphocytes no significant changes in volume.
It can be seen that the lower the temperature of cold exposure, HSP70 mRNA transcription in cells more quickly. 1O ~ one in a 4 ℃ cold exposure of 12 h and 24 h when, HSP70 mR-NA transcription volume compared with the control group the difference was not obvious, may be associated with accelerated degradation of mRNA, the cold cell function of damage, so that HSP70 mRNA transcription impaired, or with animals have to adapt to the cold and other factors. The end of cold exposure at room temperature into the environment, equal to the initial establishment of the cold adaptation based on the imposition of a new thermal stimulation, so, HSP70 mRNA transcription to strengthen again, but because in a 1O ~ a 4 ℃ when exposed to cold damage to cell function , the HSP70 mRNA transcription can not respond quickly.
Detection of mRNA can be adopted to some extent reflect the HSP70 expression, HSP70 increased and will be beneficial to animals, self-protection function, increase resistance to external adverse stimuli [9]. . Cold stress vulnerable to injury when the cells, protein folding error, resulting in impaired protein function. HSP70 can prevent the non-natural peptide polypeptide chain between internal or non-correctly folded, or fold them in the middle of the polypeptide chain of the peptide to provide the most opportunity for the correct folding [10,11]. It was through Tetrahymena heat shock cells, studies have found that some cells HSP promote gluconeogenesis and glycogenesis role, so that an increase in intracellular glycogen storage capacity, thereby enhancing the tolerance [12], which is the liver HSP70 mRNA in rapid increase in the number of links [11], because the liver is the metabolism of glycogen synthase sites. Ishiyama, etc. [13] (1996) also found in cells from HSP major role in the protection of cells, different signaling pathway can cause resistance to apoptosis.吕裕strong [14] (1996) on rabbit lymphocytes in the trial found that, despite the high temperature heat resistant cells can change shape, but much lighter, and even has not changed.
The experimental results show that piglets in a 10 ~ a 4 oC exposed to cold 0.5 h, lymphocytes within the HSP70 mRNA transcription increased significantly (P <0.05), indicate the source of the body cells of the stress response faster This is conducive to animals subjected to cold stress protection system in time to start to enhance the outside world viruses, bacteria resistance, reduce morbidity and mortality. HSP70 mRNA expression product of HSP70 antigen molecules can be used as the carrier, by the antigen or pathogen-activated macrophages and lymphocytes when the immune response to various immune cytokines, HSP can be induced to participate in the selection and coordination antigen processing, presentation, and use of its antigen-specific T cell immune recognition for navigation. Lymphocytes in the spleen and an increase in HSP70 may be related to immune function [6]. Zhou Fang [7] and other workers of the cold storage of blood in small lymphatic HSP70 and Lee士泽[8], such as cold stress on piglet tissue HSP70 studies have shown that: 0 oC group and the control group (room temperature) compared to, HSP70 expression difference significantly, which agreed with the experimental results. Subsequently, although the decline in the amount of transcription, but the stress-3 h and 6 h the amount of transcription compared with the amount based on significant differences (P <0.05). With the stress time, resulting in a gradual cooling of animals to adapt to the process of transcription of HSP70 mRNA also showed a downward trend continued. When the piglets from the transfer of cold to the normal rearing temperature, HSP70 mRNA transcription volume also showed a gradual upward trend, to the restoration of 24 h after stress, due to gradually adapt to the environment of animals, mRNA degradation faster decline in their transcription and near the basis of level. 4 ~ 1O ℃ in cold stress before and after transcription HSP70mRNA lymphocytes no significant changes in volume.
It can be seen that the lower the temperature of cold exposure, HSP70 mRNA transcription in cells more quickly. 1O ~ one in a 4 ℃ cold exposure of 12 h and 24 h when, HSP70 mR-NA transcription volume compared with the control group the difference was not obvious, may be associated with accelerated degradation of mRNA, the cold cell function of damage, so that HSP70 mRNA transcription impaired, or with animals have to adapt to the cold and other factors. The end of cold exposure at room temperature into the environment, equal to the initial establishment of the cold adaptation based on the imposition of a new thermal stimulation, so, HSP70 mRNA transcription to strengthen again, but because in a 1O ~ a 4 ℃ when exposed to cold damage to cell function , the HSP70 mRNA transcription can not respond quickly.
Detection of mRNA can be adopted to some extent reflect the HSP70 expression, HSP70 increased and will be beneficial to animals, self-protection function, increase resistance to external adverse stimuli [9]. . Cold stress vulnerable to injury when the cells, protein folding error, resulting in impaired protein function. HSP70 can prevent the non-natural peptide polypeptide chain between internal or non-correctly folded, or fold them in the middle of the polypeptide chain of the peptide to provide the most opportunity for the correct folding [10,11]. It was through Tetrahymena heat shock cells, studies have found that some cells HSP promote gluconeogenesis and glycogenesis role, so that an increase in intracellular glycogen storage capacity, thereby enhancing the tolerance [12], which is the liver HSP70 mRNA in rapid increase in the number of links [11], because the liver is the metabolism of glycogen synthase sites. Ishiyama, etc. [13] (1996) also found in cells from HSP major role in the protection of cells, different signaling pathway can cause resistance to apoptosis.吕裕strong [14] (1996) on rabbit lymphocytes in the trial found that, despite the high temperature heat resistant cells can change shape, but much lighter, and even has not changed.
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这是我的理解:
The experimental results show that piglets in a 10 ~ a 4 oC exposed to cold 0.5 h, lymphocytes within the HSP70 mRNA transcription increased significantly (P <0.05), indicate the source of the body cells of the stress response faster This is conducive to animals subjected to cold stress protection system in time to start to enhance the outside world viruses, bacteria resistance, reduce morbidity and mortality. HSP70 mRNA expression product of HSP70 antigen molecules can be used as the carrier, by the antigen or pathogen-activated macrophages and lymphocytes when the immune response to various immune cytokines, HSP can be induced to participate in the selection and coordination antigen processing, presentation, and use of its antigen-specific T cell immune recognition for navigation. Lymphocytes in the spleen and an increase in HSP70 may be related to immune function [6]. Zhou Fang [7] and other workers of the cold storage of blood in small lymphatic HSP70 and Lee士泽[8], such as cold stress on piglet tissue HSP70 studies have shown that: 0 oC group and the control group (room temperature) compared to, HSP70 expression difference significantly, which agreed with the experimental results. Subsequently, although the decline in the amount of transcription, but the stress-3 h and 6 h the amount of transcription compared with the amount based on significant differences (P <0.05). With the stress time, resulting in a gradual cooling of animals to adapt to the process of transcription of HSP70 mRNA also showed a downward trend continued. When the piglets from the transfer of cold to the normal rearing temperature, HSP70 mRNA transcription volume also showed a gradual upward trend, to the restoration of 24 h after stress, due to gradually adapt to the environment of animals, mRNA degradation faster decline in their transcription and near the basis of level. 4 ~ 1O ℃ in cold stress before and after transcription HSP70mRNA lymphocytes no significant changes in volume.
It can be seen that the lower the temperature of cold exposure, HSP70 mRNA transcription in cells more quickly. 1O ~ one in a 4 ℃ cold exposure of 12 h and 24 h when, HSP70 mR-NA transcription volume compared with the control group the difference was not obvious, may be associated with accelerated degradation of mRNA, the cold cell function of damage, so that HSP70 mRNA transcription impaired, or with animals have to adapt to the cold and other factors. The end of cold exposure at room temperature into the environment, equal to the initial establishment of the cold adaptation based on the imposition of a new thermal stimulation, so, HSP70 mRNA transcription to strengthen again, but because in a 1O ~ a 4 ℃ when exposed to cold damage to cell function , the HSP70 mRNA transcription can not respond quickly.
Detection of mRNA can be adopted to some extent reflect the HSP70 expression, HSP70 increased and will be beneficial to animals, self-protection function, increase resistance to external adverse stimuli [9]. . Cold stress vulnerable to injury when the cells, protein folding error, resulting in impaired protein function. HSP70 can prevent the non-natural peptide polypeptide chain between internal or non-correctly folded, or fold them in the middle of the polypeptide chain of the peptide to provide the most opportunity for the correct folding [10,11]. It was through Tetrahymena heat shock cells, studies have found that some cells HSP promote gluconeogenesis and glycogenesis role, so that an increase in intracellular glycogen storage capacity, thereby enhancing the tolerance [12], which is the liver HSP70 mRNA in rapid increase in the number of links [11], because the liver is the metabolism of glycogen synthase sites. Ishiyama, etc. [13] (1996) also found in cells from HSP major role in the protection of cells, different signaling pathway can cause resistance to apoptosis.吕裕strong [14] (1996) on rabbit lymphocytes in the trial found that, despite the high temperature heat resistant cells can change shape, but much lighter, and even has not changed.
The experimental results show that piglets in a 10 ~ a 4 oC exposed to cold 0.5 h, lymphocytes within the HSP70 mRNA transcription increased significantly (P <0.05), indicate the source of the body cells of the stress response faster This is conducive to animals subjected to cold stress protection system in time to start to enhance the outside world viruses, bacteria resistance, reduce morbidity and mortality. HSP70 mRNA expression product of HSP70 antigen molecules can be used as the carrier, by the antigen or pathogen-activated macrophages and lymphocytes when the immune response to various immune cytokines, HSP can be induced to participate in the selection and coordination antigen processing, presentation, and use of its antigen-specific T cell immune recognition for navigation. Lymphocytes in the spleen and an increase in HSP70 may be related to immune function [6]. Zhou Fang [7] and other workers of the cold storage of blood in small lymphatic HSP70 and Lee士泽[8], such as cold stress on piglet tissue HSP70 studies have shown that: 0 oC group and the control group (room temperature) compared to, HSP70 expression difference significantly, which agreed with the experimental results. Subsequently, although the decline in the amount of transcription, but the stress-3 h and 6 h the amount of transcription compared with the amount based on significant differences (P <0.05). With the stress time, resulting in a gradual cooling of animals to adapt to the process of transcription of HSP70 mRNA also showed a downward trend continued. When the piglets from the transfer of cold to the normal rearing temperature, HSP70 mRNA transcription volume also showed a gradual upward trend, to the restoration of 24 h after stress, due to gradually adapt to the environment of animals, mRNA degradation faster decline in their transcription and near the basis of level. 4 ~ 1O ℃ in cold stress before and after transcription HSP70mRNA lymphocytes no significant changes in volume.
It can be seen that the lower the temperature of cold exposure, HSP70 mRNA transcription in cells more quickly. 1O ~ one in a 4 ℃ cold exposure of 12 h and 24 h when, HSP70 mR-NA transcription volume compared with the control group the difference was not obvious, may be associated with accelerated degradation of mRNA, the cold cell function of damage, so that HSP70 mRNA transcription impaired, or with animals have to adapt to the cold and other factors. The end of cold exposure at room temperature into the environment, equal to the initial establishment of the cold adaptation based on the imposition of a new thermal stimulation, so, HSP70 mRNA transcription to strengthen again, but because in a 1O ~ a 4 ℃ when exposed to cold damage to cell function , the HSP70 mRNA transcription can not respond quickly.
Detection of mRNA can be adopted to some extent reflect the HSP70 expression, HSP70 increased and will be beneficial to animals, self-protection function, increase resistance to external adverse stimuli [9]. . Cold stress vulnerable to injury when the cells, protein folding error, resulting in impaired protein function. HSP70 can prevent the non-natural peptide polypeptide chain between internal or non-correctly folded, or fold them in the middle of the polypeptide chain of the peptide to provide the most opportunity for the correct folding [10,11]. It was through Tetrahymena heat shock cells, studies have found that some cells HSP promote gluconeogenesis and glycogenesis role, so that an increase in intracellular glycogen storage capacity, thereby enhancing the tolerance [12], which is the liver HSP70 mRNA in rapid increase in the number of links [11], because the liver is the metabolism of glycogen synthase sites. Ishiyama, etc. [13] (1996) also found in cells from HSP major role in the protection of cells, different signaling pathway can cause resistance to apoptosis.吕裕strong [14] (1996) on rabbit lymphocytes in the trial found that, despite the high temperature heat resistant cells can change shape, but much lighter, and even has not changed.
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