视网膜色素变性T17M视紫红质突变诱导细胞死亡的机制研究
发布时间：2018-07-20 12:49
【摘要】：第一章视紫红质T17M突变体的亚细胞定位 目的：研究视紫红质T17M突变体的亚细胞定位及意义。 方法：构建pCDNA-3.1-T17M rhodopsin-myc质粒和pCDNA-3.1-WT rhodopsin-myc质粒,使用EcoR Ⅰ和BamH Ⅰ双酶切法进行鉴定,基因测序。将构建成功的质粒转染到HEK293细胞,采用Western blot检测视紫红质T17M突变体和野生型的蛋白表达差异。免疫荧光显微镜下观察视紫红质T17M突变体和野生型的亚细胞定位。 结果：经过PCR扩增和双酶切鉴定,获得约1000bp大小的条带,基因测序显示第50位碱基C突变成T,成功构建pCDNA-3.1-T17M rhodopsin-myc质粒和pCDNA-3.1-WT rhodopsin-myc质粒。质粒转染后,Western blot检测到约40KD的条带,转染可高效表达视紫红质T17M突变体和野生型蛋白。荧光显微镜检查发现,视紫红质T17突变体聚集在内质网,与高尔基体不存在共定位；而野生型主要位于细胞膜。 结论：视紫红质T17M突变体异常定位于内质网,与高尔基体不存在共定位。视紫红质野生型主要位于细胞膜。 第二章视紫红质T17M突变体的降解途径 目的：研究视紫红质T17M突变体的降解途径及意义。 方法：使用MTT法检测视紫红质T17M突变体和野生型的降解速度。Western blot检测溶酶体抑制剂CQ和蛋白酶体抑制剂MG132对视紫红质T17M突变体和野生型降解的影响。免疫沉淀检测视紫红质泛素化水平。Western blot检测p97/VCP-QQ(?)Erasin siRNA对视紫红质T17M突变体和野生型的半衰期的影响。 结果：蛋白合成抑制剂CHX处理HEK293细胞和ARPE-19细胞6h后,CHX处理前视紫红质蛋白标化为1, HEK293细胞的视紫红质T17M突变体和野生型蛋白相对值分别为0.219±0.032和0.635±0.072(P0.01), ARPE-19细胞的视紫红质T17M突变体和野生型蛋白相对值分别为0.302±0.041和0.531±0.052(P0.01)。溶酶体抑制剂CQ处理HEK293细胞12h后,视紫红质T17M突变体由1增加到1.023±0.265,视紫红质野生型蛋白相对值由1增加到1.433±0.159(P0.05)。蛋白酶体抑制剂MG132处L理HEK293细胞6h后,视紫红质T17M突变体由1增加到7.213±2.108(P0.01),视紫红质野生型蛋白相对值由1增加到2.011±0.221(P0.05)。免疫沉淀后,泛素化视紫红质T17M突变体由1增加到2.200±0.361(P0.01),野生型蛋白相对值由1增加到1.160±0.162。在ARPE-19细胞中过表达p97/VCP-QQ后,对照组和p97/VCP-QQ组的视紫红质T17M突变体蛋白相对值分别为0.159±0.052和0.558±0.095(P0.01)。Erasin siRNA处理后,视紫红质T17M突变体的对照组Erasin siRNA组的蛋白相对值分别为0.230±0.059和0.602±0.064(P0.01),而视紫红质野生型降解速度没有明显变化。 结论：与视紫红质野生型相比,T17M突变体降解加速。视紫红质T17M突变体只能通过蛋白酶体系统降解,而野生型可以通过自噬溶酶体系统和蛋白酶体系统降解。视紫红质T17M突变体的降解与泛素化的ERAD相关。过表达p97/VCP-QQ和Erasin siRNA干扰可以抑制视紫红质T17M突变体通过ERAD途径降解。 第三章视紫红质T17M突变诱导细胞死亡的机制 目的：研究视紫红质T17M突变诱导细胞死亡的机制。 方法：建立pEGFP-CL1-ARPE-19细胞系,采用Western blot方法检测其蛋白酶体活性。过表达视紫红质蛋白,诱导内质网应激反应,采用Western blot方法检测内质网应激相关蛋白BIP、GRP94、CHOP、 peIF-2a、eIF-2a、active ATF-6a的表达差异,并用PBA处理细胞,观察PBA对以上内质网应激相关蛋白表达的影响。Tunicamycin处理ARPE-19细胞,流式细胞仪检测细胞死亡数目。过表达视紫红质T17M突变体,采用流式细胞仪检测细胞内ROS水平,并使用ROS清除剂NAC和BHA处理,观察细胞死亡变化情况。 结果：pEGFP-CL1-ARPE-19细胞系可稳定表达uGFP,视紫红质T17M突变、野生型的uGFP表达量没有显著变化。T17M突变可使细胞内质网应激蛋白BIP、GRP94、CHOP、peIF-2a、eIF-2a、active ATF-6a表达上调,与视紫红质野生型相比,BIP、CHOP、GRP94、 peIF-2a/eIF-2a、active ATF-6a表达量分别增加2.439±0.363倍(P0.01)、2.433±0.802倍(P0.01)、1.600±0.212倍(P0.05)、1.567±0.153(P0.05)、2.167±0.306倍(P0.01)。与视紫红质野生型相比,CHOP表达量在使用PBA处理前后分别增加了2.600±0.854倍和1.467±0.306倍(P0.05),GRP94表达量处理前后增加1.921±0.557倍和1.203±0.239倍(P0.05),peIF-2a/eIF-2a为1.733±0.154倍和1.167±0.252倍(P0.05),active ATF-6a为2.564±0.406倍和1.349±0.529倍(P0.05)。而使用内质网应激诱导剂‘Tunicamycin前后,空载体、视紫红质野生型和T17M突变体的ARPE-19细胞死亡率分别为4.156%±0.501%和4.814%±0.531%、3.879%±0.413%和5.712%±0.574%、7.021%±0.612%和16.213%±3.419%,视紫红质T17M突变体过表达的细胞死亡率较空载体和野生型明显增加(P0.05)。与空载体组相比,视紫红质野生型和视紫红质T17M突变体ROS的相对比分别为1.136±0.055,1.935±0.088(P0.01)。使用ROS清除剂NAC和BHA后,空载体组、DMSO组、NAC组和BHA组的死亡率分别为3.716%±0.523%、7.322%±1.924%、4.857%±1.369%(相比DMSO组,P0.05)和4.271%±0.988%(相比DMSO组,P0.01)。 结论：视紫红质T17M突变不影响蛋白酶体活性。T17M突变能诱导细胞内质网应激,使内质网应激蛋白BIP、GRP94、CHOP、peIF-2a、 eIF-2a、active ATF-6a表达上调。化学分子伴侣PBA能缓解T17M诱导的内质网应激。视紫红质T17M突变增加细胞对内质网应激诱导剂Tunicamycin的敏感性。突变的T17M视紫红质增加细胞内ROS的水平,ROS清除剂NAC和BHA能抑制视紫红质T17M突变导致的细胞死
[Abstract]:Chapter 1 subcellular localization of rhodopsin T17M mutant
Objective: To study the subcellular localization and significance of rhodopsin T17M mutant.
Methods: pCDNA-3.1-T17M rhodopsin-myc plasmids and pCDNA-3.1-WT rhodopsin-myc plasmids were constructed and identified by EcoR I and BamH I double enzyme digestion and gene sequencing. The constructed plasmids were transfected into HEK293 cells, and Western blot was used to detect the differences in the expression of rhodopsin T17M mutants and wild type proteins. Immunofluorescence microscopy was used. Subcellular localization of rhodopsin T17M mutant and wild type was observed.
Results: after PCR amplification and double enzyme digestion, the 1000bp size bands were obtained. Gene sequencing showed that fiftieth base C was transformed into T, and pCDNA-3.1-T17M rhodopsin-myc plasmids and pCDNA-3.1-WT rhodopsin-myc plasmids were successfully constructed. After plasmid transfection, Western blot detected approximately 40KD bands. The transfection could efficiently express rhodopsin T17M mutation The fluorescence microscope showed that the T17 mutant of rhodopsin was clustered in the endoplasmic reticulum, and there was no co location with the Golgi body, while the wild type was mainly in the cell membrane.
Conclusion: the rhodopsin T17M mutant is located in the endoplasmic reticulum and has no co localization with Golgi apparatus. The rhodopsin type is mainly located in the cell membrane.
The second chapter of degradation pathway of rhodopsin T17M mutant
Objective: To study the degradation pathway and significance of rhodopsin T17M mutant.
Methods: MTT method was used to detect the T17M mutant of rhodopsin and the degradation rate of wild type.Western blot to detect the effect of lysosome inhibitor CQ and proteasome inhibitor MG132 on the degradation of rhodopsin T17M mutants and wild type. Immunoprecipitating detection of.Western blot detection p97/VCP-QQ (?) Erasin siRNA against rhodopsin The half-life of T17M mutant and wild type of purplish red.
Results: after the protein synthesis inhibitor CHX treated the HEK293 cells and ARPE-19 cells 6h, the CHX treated rhodopsin was labeled as 1, the relative values of the rhodopsin T17M mutants and the wild type proteins were 0.219 + 0.032 and 0.635 + 0.072 (P0.01) respectively, and the relative values of the rhodopsin T17M mutants of ARPE-19 cells and the relative values of the wild type proteins in ARPE-19 cells were divided. Don't be 0.302 + 0.041 and 0.531 + 0.052 (P0.01). After the lysosome inhibitor CQ treated HEK293 cell 12h, the T17M mutant of the rhodopsin increased from 1 to 1.023 + 0.265, and the relative value of the rhodopsin wild type protein increased from 1 to 1.433 + 0.159 (P0.05). After the proteasome inhibitor MG132 was L rational HEK293 cell 6h, the T17M mutant of the rhodopsin increased from 1 to 7.21. 3 + 2.108 (P0.01), the relative value of rhodopsin wild type protein increased from 1 to 2.011 + 0.221 (P0.05). After immunoprecipitation, the ubiquitination rhodopsin T17M mutant was increased from 1 to 2.200 + 0.361 (P0.01), and the relative value of wild type protein increased from 1 to 1.160 + 0.162. in ARPE-19 cells, and the control group and p97/VCP-QQ group of rhodopsin The relative values of the qualitative T17M mutant proteins were 0.159 + 0.052 and 0.558 + 0.095 (P0.01).Erasin siRNA respectively. The relative values of the Erasin siRNA group of the control group of the rhodopsin T17M mutant were 0.230 + 0.059 and 0.602 + 0.064 (P0.01), respectively, while the degradation rate of the rhodopsin wild type was not significantly changed.
Conclusion: compared with the wild type of rhodopsin, the degradation of T17M mutant is accelerated. The T17M mutant of rhodopsin can be degraded only through the proteasome system, while the wild type can be degraded by autophagosome system and proteasome system. The degradation of the T17M mutant of the rhodopsin is related to the ERAD of the ubiquitination. P97/VCP-QQ and Erasin siRNA are overexpressed by over expression of the mutant of the rhodopsin. Disturbance can inhibit the degradation of rhodopsin T17M mutant via ERAD pathway.
The third chapter is about the mechanism of cell death induced by T17M mutation of rhodopsin.
Objective: To study the mechanism of cell death induced by T17M mutation of rhodopsin.
Methods: the pEGFP-CL1-ARPE-19 cell line was established and the activity of proteasome was detected by Western blot. Overexpression of rhodopsin, induced endoplasmic reticulum stress reaction, and Western blot method was used to detect the expression difference of endoplasmic reticulum stress related protein BIP, GRP94, CHOP, peIF-2a, eIF-2a, active ATF-6a. The expression of stress related protein in the endoplasmic reticulum was affected by.Tunicamycin treatment of ARPE-19 cells, the number of cell deaths was detected by flow cytometry. The T17M mutant of rhodopsin was overexpressed. The level of intracellular ROS was detected by flow cytometry, and the ROS scavenger NAC and BHA were used to observe the change of cell death.
Results: pEGFP-CL1-ARPE-19 cell lines can express uGFP, T17M mutation of rhodopsin, and there is no significant change in the expression of uGFP in the wild type,.T17M mutation can make the cell endoplasmic reticulum stress protein BIP, GRP94, CHOP, peIF-2a, eIF-2a, active ATF-6a, compared with the wild type of rhodopsin The amount increased by 2.439 + 0.363 times (P0.01), 2.433 + 0.802 times (P0.01), 1.600 + 0.212 times (P0.05), 1.567 + 0.153 (P0.05), 2.167 + 0.306 times (P0.01). Compared with the wild type of rhodopsin, the expression of CHOP increased by 2.600 + 0.854 times and 1.467 + 1.600 times (P0.05) before and after PBA treatment, and the GRP94 expression was increased before and after the treatment. It was 1.203 + 0.239 times (P0.05), peIF-2a/eIF-2a was 1.733 + 0.154 times and 1.167 + 0.252 times (P0.05), active ATF-6a was 2.564 + 0.406 times and 1.349 + 0.529 times (P0.05). And the ARPE-19 cell death rate was 4.156% + 0.501% and 4.8 by using endoplasmic reticulum stress inducer before and after Tunicamycin. 14% + 0.531%, 3.879% + 0.413% and 5.712% + 0.574%, 7.021% + 0.612% and 16.213% + 3.419%, the overexpressed cell mortality of the rhodopsin T17M mutant was significantly higher than that of the empty vector and the wild type (P0.05). Compared with the no-load group, the relative ratio of the rhodopsin wild type and the rhodopsin T17M mutant ROS was respectively (P0.01) + 0.088 (P0.01). After the use of ROS scavenger NAC and BHA, the mortality of the unloaded body group, the DMSO group, the NAC group and the BHA group were 3.716% + 0.523%, 7.322% + 1.924%, 4.857% + 1.369% (compared to the DMSO group, P0.05) and 4.271% + 0.988% (compared to the DMSO group, P0.01).
Conclusion: T17M mutation of rhodopsin does not affect the.T17M mutation of proteasome activity can induce endoplasmic reticulum stress and up-regulated expression of BIP, GRP94, CHOP, peIF-2a, eIF-2a, active ATF-6a expression of endoplasmic reticulum stress protein. Chemical chaperone PBA can alleviate the T17M induced endoplasmic reticulum stress. Rhodopsin T17M mutation increases the induction of endoplasmic reticulum stress induced by the rhodopsin T17M mutation The sensitivity of the agent Tunicamycin. Mutant T17M rhodopsin increased the level of ROS in cells. ROS scavenger NAC and BHA could inhibit cell death caused by T17M mutation of rhodopsin.
【学位授予单位】：中南大学
【学位级别】：博士
【学位授予年份】：2014
【分类号】：R774.13
本文编号：2133565
[Abstract]:Chapter 1 subcellular localization of rhodopsin T17M mutant
Objective: To study the subcellular localization and significance of rhodopsin T17M mutant.
Methods: pCDNA-3.1-T17M rhodopsin-myc plasmids and pCDNA-3.1-WT rhodopsin-myc plasmids were constructed and identified by EcoR I and BamH I double enzyme digestion and gene sequencing. The constructed plasmids were transfected into HEK293 cells, and Western blot was used to detect the differences in the expression of rhodopsin T17M mutants and wild type proteins. Immunofluorescence microscopy was used. Subcellular localization of rhodopsin T17M mutant and wild type was observed.
Results: after PCR amplification and double enzyme digestion, the 1000bp size bands were obtained. Gene sequencing showed that fiftieth base C was transformed into T, and pCDNA-3.1-T17M rhodopsin-myc plasmids and pCDNA-3.1-WT rhodopsin-myc plasmids were successfully constructed. After plasmid transfection, Western blot detected approximately 40KD bands. The transfection could efficiently express rhodopsin T17M mutation The fluorescence microscope showed that the T17 mutant of rhodopsin was clustered in the endoplasmic reticulum, and there was no co location with the Golgi body, while the wild type was mainly in the cell membrane.
Conclusion: the rhodopsin T17M mutant is located in the endoplasmic reticulum and has no co localization with Golgi apparatus. The rhodopsin type is mainly located in the cell membrane.
The second chapter of degradation pathway of rhodopsin T17M mutant
Objective: To study the degradation pathway and significance of rhodopsin T17M mutant.
Methods: MTT method was used to detect the T17M mutant of rhodopsin and the degradation rate of wild type.Western blot to detect the effect of lysosome inhibitor CQ and proteasome inhibitor MG132 on the degradation of rhodopsin T17M mutants and wild type. Immunoprecipitating detection of.Western blot detection p97/VCP-QQ (?) Erasin siRNA against rhodopsin The half-life of T17M mutant and wild type of purplish red.
Results: after the protein synthesis inhibitor CHX treated the HEK293 cells and ARPE-19 cells 6h, the CHX treated rhodopsin was labeled as 1, the relative values of the rhodopsin T17M mutants and the wild type proteins were 0.219 + 0.032 and 0.635 + 0.072 (P0.01) respectively, and the relative values of the rhodopsin T17M mutants of ARPE-19 cells and the relative values of the wild type proteins in ARPE-19 cells were divided. Don't be 0.302 + 0.041 and 0.531 + 0.052 (P0.01). After the lysosome inhibitor CQ treated HEK293 cell 12h, the T17M mutant of the rhodopsin increased from 1 to 1.023 + 0.265, and the relative value of the rhodopsin wild type protein increased from 1 to 1.433 + 0.159 (P0.05). After the proteasome inhibitor MG132 was L rational HEK293 cell 6h, the T17M mutant of the rhodopsin increased from 1 to 7.21. 3 + 2.108 (P0.01), the relative value of rhodopsin wild type protein increased from 1 to 2.011 + 0.221 (P0.05). After immunoprecipitation, the ubiquitination rhodopsin T17M mutant was increased from 1 to 2.200 + 0.361 (P0.01), and the relative value of wild type protein increased from 1 to 1.160 + 0.162. in ARPE-19 cells, and the control group and p97/VCP-QQ group of rhodopsin The relative values of the qualitative T17M mutant proteins were 0.159 + 0.052 and 0.558 + 0.095 (P0.01).Erasin siRNA respectively. The relative values of the Erasin siRNA group of the control group of the rhodopsin T17M mutant were 0.230 + 0.059 and 0.602 + 0.064 (P0.01), respectively, while the degradation rate of the rhodopsin wild type was not significantly changed.
Conclusion: compared with the wild type of rhodopsin, the degradation of T17M mutant is accelerated. The T17M mutant of rhodopsin can be degraded only through the proteasome system, while the wild type can be degraded by autophagosome system and proteasome system. The degradation of the T17M mutant of the rhodopsin is related to the ERAD of the ubiquitination. P97/VCP-QQ and Erasin siRNA are overexpressed by over expression of the mutant of the rhodopsin. Disturbance can inhibit the degradation of rhodopsin T17M mutant via ERAD pathway.
The third chapter is about the mechanism of cell death induced by T17M mutation of rhodopsin.
Objective: To study the mechanism of cell death induced by T17M mutation of rhodopsin.
Methods: the pEGFP-CL1-ARPE-19 cell line was established and the activity of proteasome was detected by Western blot. Overexpression of rhodopsin, induced endoplasmic reticulum stress reaction, and Western blot method was used to detect the expression difference of endoplasmic reticulum stress related protein BIP, GRP94, CHOP, peIF-2a, eIF-2a, active ATF-6a. The expression of stress related protein in the endoplasmic reticulum was affected by.Tunicamycin treatment of ARPE-19 cells, the number of cell deaths was detected by flow cytometry. The T17M mutant of rhodopsin was overexpressed. The level of intracellular ROS was detected by flow cytometry, and the ROS scavenger NAC and BHA were used to observe the change of cell death.
Results: pEGFP-CL1-ARPE-19 cell lines can express uGFP, T17M mutation of rhodopsin, and there is no significant change in the expression of uGFP in the wild type,.T17M mutation can make the cell endoplasmic reticulum stress protein BIP, GRP94, CHOP, peIF-2a, eIF-2a, active ATF-6a, compared with the wild type of rhodopsin The amount increased by 2.439 + 0.363 times (P0.01), 2.433 + 0.802 times (P0.01), 1.600 + 0.212 times (P0.05), 1.567 + 0.153 (P0.05), 2.167 + 0.306 times (P0.01). Compared with the wild type of rhodopsin, the expression of CHOP increased by 2.600 + 0.854 times and 1.467 + 1.600 times (P0.05) before and after PBA treatment, and the GRP94 expression was increased before and after the treatment. It was 1.203 + 0.239 times (P0.05), peIF-2a/eIF-2a was 1.733 + 0.154 times and 1.167 + 0.252 times (P0.05), active ATF-6a was 2.564 + 0.406 times and 1.349 + 0.529 times (P0.05). And the ARPE-19 cell death rate was 4.156% + 0.501% and 4.8 by using endoplasmic reticulum stress inducer before and after Tunicamycin. 14% + 0.531%, 3.879% + 0.413% and 5.712% + 0.574%, 7.021% + 0.612% and 16.213% + 3.419%, the overexpressed cell mortality of the rhodopsin T17M mutant was significantly higher than that of the empty vector and the wild type (P0.05). Compared with the no-load group, the relative ratio of the rhodopsin wild type and the rhodopsin T17M mutant ROS was respectively (P0.01) + 0.088 (P0.01). After the use of ROS scavenger NAC and BHA, the mortality of the unloaded body group, the DMSO group, the NAC group and the BHA group were 3.716% + 0.523%, 7.322% + 1.924%, 4.857% + 1.369% (compared to the DMSO group, P0.05) and 4.271% + 0.988% (compared to the DMSO group, P0.01).
Conclusion: T17M mutation of rhodopsin does not affect the.T17M mutation of proteasome activity can induce endoplasmic reticulum stress and up-regulated expression of BIP, GRP94, CHOP, peIF-2a, eIF-2a, active ATF-6a expression of endoplasmic reticulum stress protein. Chemical chaperone PBA can alleviate the T17M induced endoplasmic reticulum stress. Rhodopsin T17M mutation increases the induction of endoplasmic reticulum stress induced by the rhodopsin T17M mutation The sensitivity of the agent Tunicamycin. Mutant T17M rhodopsin increased the level of ROS in cells. ROS scavenger NAC and BHA could inhibit cell death caused by T17M mutation of rhodopsin.
【学位授予单位】：中南大学
【学位级别】：博士
【学位授予年份】：2014
【分类号】：R774.13
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