急性颅脑创伤患者脑脊液差异蛋白质组学研究
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摘要
目的：
重型颅脑创伤(traumatic brain injury, TBI)患者死亡率很高,在30%-50%左右,存活者中也有相当高的致残率,因此,颅脑创伤严重威胁着人类健康,对社会和家庭造成沉重的经济负担,引起了世界各国的广泛重视。目前如何降低该病的死亡率和致残率仍是神经外科领域的难点和热点,对其致病和修复机制的研究,一直是神经外科领域的热点课题。
在前期研究中,我们通过承担国家自然科学基金资助项目《急性脑创伤后神经元蛋白质组农达改变的研究》(项目编号：30271331),采用蛋白质组学技术平台,观察了创伤后大脑皮层神经组织内蛋白质组的变化。本研究目的是通过比较脑创伤后脑脊液(cerebrospinal fluid, CSF)蛋白组的改变,从中寻找脑源性差异蛋白,并与脑组织蛋白质组改变进行比较,为研究颅脑创伤的分子机制和生物学标志物的寻找提供宝贵的理论基础。
方法：
在第一部分,我们选用从10例人脑创伤后行颅内压监护的患者中获取的脑脊液,通过预冷丙酮除盐浓缩,采用蛋白质均衡技术(ProteoMinerTM试剂盒)去除高丰度蛋白并富集低丰度蛋白之后,进行双向凝胶电泳、硝酸银染色和凝胶图像处理,建立了高重复性的人类脑脊液蛋白质组中的高丰度蛋白去除方法,进行了方法学上的验证。
在第二部分,我们选取30例颅脑创伤患者和8例破裂动脉瘤致蛛网膜下腔出血(subarachnoid hemorrhage, SAH)但不伴实质内血肿的患者,发病后24小时内行脑室外引流术,收集的脑脊液样本离心取上清-80℃低温保存,混合样本预冷丙酮除盐浓缩,采用ProteoMinerTM试剂盒去除高丰度蛋白并富集低丰度蛋白后,Bradford法测定最终蛋白浓度,由三种荧光(Cy2, Cy3, Cy5)交叉标记的两种50μg样品和内标混合,进行双向差异凝胶电泳(two-dimensional differential in-gel electrophoresis,2D-DIGE),使用DeCyder v.5.02图像分析软件分析电泳结果。差异点通过胰蛋白酶胶内酶切、基质辅助激光解吸/电离-飞行时间串联质谱技术,对肽段的分子量进行测定,通过数据库检索,进行蛋白鉴定,推测其生物学作用。
结果：
在第一部分中,人TBI后CSF经ProteoMinerTM处理后,经过PDQuest 7.0软件自动检测到的蛋白质点数为1432±85,与常用的丙酮沉淀法检测到的蛋白质点数1123±114相比,具有统计学意义(P<0.05, F=8.885)。通过比较CSF经ProteoMinerTM处理前后2-DE图谱发现,高丰度蛋白减少,低丰度蛋白的分辨率提高。说明ProteoMinerTM起到了富集低丰度蛋白的作用,可进行下一步研究。
在第二部分的研究中,两组患者的CSF经过ProteoMinerTM富集低丰度蛋白后进行2D-DIGE分离,得到清晰的脑脊液蛋白图谱。生物学差异分析结果表明,在外伤组与对照组脑脊液蛋白共存在有表达量变化超过1.5倍的差异蛋白质点169个,其中在外伤组中表达上调1.5倍以上的有98个蛋白质点,下调1.5倍以上的有71个蛋白质点。通过质谱鉴定,47个蛋白质点被鉴别出,属于36种蛋白产物。依据蛋白可能存在的生理功能将其分类为：细胞骨架、参与代谢、信号传导、应激反应、蛋白合成与代谢和未知功能蛋白。其中铜蓝蛋白、小白蛋白、KLF6因子、磷脂转运蛋白、SLC25A23、溴区包含蛋白1、F-box蛋白7与中枢神经系统常见疾病有密切关系,在脑创伤急性期内人CSF中首次发现其表达水平出现变化。
结论：
人脑创伤后的急性期内,创伤造成的机械破坏使脑脊液蛋白质组发生明显变化,为研究颅脑创伤及其他神经系统疾病提供了最佳窗口。蛋白质均衡技术可以提高双向电泳的分辨率,有利于低丰度蛋白质的检出。伤后蛋白表达水平的升高或降低同时存在,在本次研究中发现的具有显著性差异变化的蛋白中,尽管还需要进一步的验证,但有可能成为评价损伤程度、预测预后的生物学标志物。
Objectives:
A high mortality rate about 30%-50%is associated with severe traumatic brain injury (TBI), few survived but also disabled. TBI is a major health problem and produces a considerable medical expense to the society and the family worldwide. Despite many researches focus on the pathophysiology and neuroprotective mechanism, there are currently no truly effective therapies for TBI.
During our research on "Proteomic analysis of the differential protein expression of the human cerebral cortex after acute severe traumatic brain injury" supported by National Natural Science Foundation of China (No.30271331),138 protein spots were found with altered expression,64 distinct proteins were identified by mass spectroscopy. In this study. Cerebrospinal fluid (CSF) from patients with traumatic brain injury was analyzed by differential proteome technique, aiming to identify the brain-derived differential proteins.
Methods:
In first section, CSF was gethered from a pool of 10 patients with TBI underwent ICP monitor by extraventricular drainage. CSF sample was desalted and concentrated by ice-cold acetone, thus meeting the requirements of having a concentration>50mg/mL necessary for using the ProteoMinerTM large-capacity kit. Protein equalizer technology (ProteoMinerTM) has been used for the enrichment of low abundant protein biomarkers for TBI and simultaneous reducement of the high abundant proteins in human CSF. The bound proteins were separated by two-dimensional electrophoresis. The silver-stained 2-D gels were scanned, and then analyzed by PDQuest 7.0 software package. We got these high-producible 2D gel proteome maps of human CSF with reducement of high abundant proteins.
In second section, large volumes of CSF were obtained within 24 hours from a pool of 30 patients with TBI underwent intracranial pressure (ICP) monitor via extraventricular drainage (EVD). Another pool of CSF samples from 8 patients was used as the control. which sufferring from subarachnoid hemorrhage without hemotoma in the parenchyma caused by a ruptured aneurysm. and an EVD was performed to withdraw CSF. Each sample obtained and centrifuged at 2000×g for 10 min to eliminate cells and other insoluble materials. The samples were then stored at-80℃. Low abundant proteins were enriched as mentioned in the first section.50μg bound proteins from each group and the internal standard were cross-labled with different CyDyes. Two-dimensional differential in-gel electrophoresis (2D-DIGE) was performed to get the differential expression protein spots with DeCyder v.5.02 software. These protein spots were digested with trypsin and Peptide Mass Fingerprint (PMF) was analyzed using a 4800 matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI TOF/TOFTM) Analyzer (Applied Biosystems). Protein identification by PMF was performed using the GPS ExplorerTM V3.5 software by searching in the International Protein Index (IPI) human database V3.23. And data mining about the function of these proteins were also conducted.
Results:
In first section, after the treatment by ProteoMinerTM column, the total number of spots in the 2-D gel was 1432±85, whereas 1123±114 spots were observed on the 2-D gels treated by ice-cold acetone. There were significant differences between the two prefractionation methods (P<0.05, F=8.885). Using ProteoMinerTM clearly improved the resolution and increased the intensity of the low abundance proteins compared with 2-D analysis of acetone precipitated CSF samples, and simultaneously reduced the high abundant proteins. Thus this prefractionation method was applicable for further research.
In second section, low abundant proteins in the CSF of the TBI group and the control group were enriched by ProteoMiner, and separated by 2D-DIGE, the map of CSF proteins was clear. The results of biological variation analysis (BVA) on the TBI group and the control group showed 169 protein spots with an expression change over 1.5-fold.98 up-regulated and 71 down-regulated protein spots were selected for further analysis with MALDI-TOF mass spectrometry.47 spots corresponded to 36 distinct proteins were identified. These identified proteins have been grouped into different categories based on their possible biofunctions:cytoskeleton. intermediary metabolism, signaling transduction, stress response, protein metabolism and unknown. Among these proteins, the ceruloplasmin, parvalbumin, Krueppel-like factor 6. phospholipid transfer protein, SLC25A23, Bromodomain containing protein 1 and F-box protein 7 are associated with central nervous system (CNS) diseases. This study first show expression changes in these proteins in acute TBI patients.
Conclusion:
The mechanical injury to the brain apparently affects the protein profile of CSF in the acute phase, and makes CSF a better window to study TBI and other CNS diseases. The use of the protein equalizer technology (ProteoMinerTM) increased 2-DE gel resolution and enabled detection of low abundance proteins compared with the precipitation technique. Up-regulation and down-regulation of proteins existed at the same time. Although further confirmation may need, these differential expressed proteins may become the biomarker for evaluating injury severity or predicting the clinical outcome.
重型颅脑创伤(traumatic brain injury, TBI)患者死亡率很高,在30%-50%左右,存活者中也有相当高的致残率,因此,颅脑创伤严重威胁着人类健康,对社会和家庭造成沉重的经济负担,引起了世界各国的广泛重视。目前如何降低该病的死亡率和致残率仍是神经外科领域的难点和热点,对其致病和修复机制的研究,一直是神经外科领域的热点课题。
在前期研究中,我们通过承担国家自然科学基金资助项目《急性脑创伤后神经元蛋白质组农达改变的研究》(项目编号：30271331),采用蛋白质组学技术平台,观察了创伤后大脑皮层神经组织内蛋白质组的变化。本研究目的是通过比较脑创伤后脑脊液(cerebrospinal fluid, CSF)蛋白组的改变,从中寻找脑源性差异蛋白,并与脑组织蛋白质组改变进行比较,为研究颅脑创伤的分子机制和生物学标志物的寻找提供宝贵的理论基础。
方法：
在第一部分,我们选用从10例人脑创伤后行颅内压监护的患者中获取的脑脊液,通过预冷丙酮除盐浓缩,采用蛋白质均衡技术(ProteoMinerTM试剂盒)去除高丰度蛋白并富集低丰度蛋白之后,进行双向凝胶电泳、硝酸银染色和凝胶图像处理,建立了高重复性的人类脑脊液蛋白质组中的高丰度蛋白去除方法,进行了方法学上的验证。
在第二部分,我们选取30例颅脑创伤患者和8例破裂动脉瘤致蛛网膜下腔出血(subarachnoid hemorrhage, SAH)但不伴实质内血肿的患者,发病后24小时内行脑室外引流术,收集的脑脊液样本离心取上清-80℃低温保存,混合样本预冷丙酮除盐浓缩,采用ProteoMinerTM试剂盒去除高丰度蛋白并富集低丰度蛋白后,Bradford法测定最终蛋白浓度,由三种荧光(Cy2, Cy3, Cy5)交叉标记的两种50μg样品和内标混合,进行双向差异凝胶电泳(two-dimensional differential in-gel electrophoresis,2D-DIGE),使用DeCyder v.5.02图像分析软件分析电泳结果。差异点通过胰蛋白酶胶内酶切、基质辅助激光解吸/电离-飞行时间串联质谱技术,对肽段的分子量进行测定,通过数据库检索,进行蛋白鉴定,推测其生物学作用。
结果：
在第一部分中,人TBI后CSF经ProteoMinerTM处理后,经过PDQuest 7.0软件自动检测到的蛋白质点数为1432±85,与常用的丙酮沉淀法检测到的蛋白质点数1123±114相比,具有统计学意义(P<0.05, F=8.885)。通过比较CSF经ProteoMinerTM处理前后2-DE图谱发现,高丰度蛋白减少,低丰度蛋白的分辨率提高。说明ProteoMinerTM起到了富集低丰度蛋白的作用,可进行下一步研究。
在第二部分的研究中,两组患者的CSF经过ProteoMinerTM富集低丰度蛋白后进行2D-DIGE分离,得到清晰的脑脊液蛋白图谱。生物学差异分析结果表明,在外伤组与对照组脑脊液蛋白共存在有表达量变化超过1.5倍的差异蛋白质点169个,其中在外伤组中表达上调1.5倍以上的有98个蛋白质点,下调1.5倍以上的有71个蛋白质点。通过质谱鉴定,47个蛋白质点被鉴别出,属于36种蛋白产物。依据蛋白可能存在的生理功能将其分类为：细胞骨架、参与代谢、信号传导、应激反应、蛋白合成与代谢和未知功能蛋白。其中铜蓝蛋白、小白蛋白、KLF6因子、磷脂转运蛋白、SLC25A23、溴区包含蛋白1、F-box蛋白7与中枢神经系统常见疾病有密切关系,在脑创伤急性期内人CSF中首次发现其表达水平出现变化。
结论：
人脑创伤后的急性期内,创伤造成的机械破坏使脑脊液蛋白质组发生明显变化,为研究颅脑创伤及其他神经系统疾病提供了最佳窗口。蛋白质均衡技术可以提高双向电泳的分辨率,有利于低丰度蛋白质的检出。伤后蛋白表达水平的升高或降低同时存在,在本次研究中发现的具有显著性差异变化的蛋白中,尽管还需要进一步的验证,但有可能成为评价损伤程度、预测预后的生物学标志物。
Objectives:
A high mortality rate about 30%-50%is associated with severe traumatic brain injury (TBI), few survived but also disabled. TBI is a major health problem and produces a considerable medical expense to the society and the family worldwide. Despite many researches focus on the pathophysiology and neuroprotective mechanism, there are currently no truly effective therapies for TBI.
During our research on "Proteomic analysis of the differential protein expression of the human cerebral cortex after acute severe traumatic brain injury" supported by National Natural Science Foundation of China (No.30271331),138 protein spots were found with altered expression,64 distinct proteins were identified by mass spectroscopy. In this study. Cerebrospinal fluid (CSF) from patients with traumatic brain injury was analyzed by differential proteome technique, aiming to identify the brain-derived differential proteins.
Methods:
In first section, CSF was gethered from a pool of 10 patients with TBI underwent ICP monitor by extraventricular drainage. CSF sample was desalted and concentrated by ice-cold acetone, thus meeting the requirements of having a concentration>50mg/mL necessary for using the ProteoMinerTM large-capacity kit. Protein equalizer technology (ProteoMinerTM) has been used for the enrichment of low abundant protein biomarkers for TBI and simultaneous reducement of the high abundant proteins in human CSF. The bound proteins were separated by two-dimensional electrophoresis. The silver-stained 2-D gels were scanned, and then analyzed by PDQuest 7.0 software package. We got these high-producible 2D gel proteome maps of human CSF with reducement of high abundant proteins.
In second section, large volumes of CSF were obtained within 24 hours from a pool of 30 patients with TBI underwent intracranial pressure (ICP) monitor via extraventricular drainage (EVD). Another pool of CSF samples from 8 patients was used as the control. which sufferring from subarachnoid hemorrhage without hemotoma in the parenchyma caused by a ruptured aneurysm. and an EVD was performed to withdraw CSF. Each sample obtained and centrifuged at 2000×g for 10 min to eliminate cells and other insoluble materials. The samples were then stored at-80℃. Low abundant proteins were enriched as mentioned in the first section.50μg bound proteins from each group and the internal standard were cross-labled with different CyDyes. Two-dimensional differential in-gel electrophoresis (2D-DIGE) was performed to get the differential expression protein spots with DeCyder v.5.02 software. These protein spots were digested with trypsin and Peptide Mass Fingerprint (PMF) was analyzed using a 4800 matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI TOF/TOFTM) Analyzer (Applied Biosystems). Protein identification by PMF was performed using the GPS ExplorerTM V3.5 software by searching in the International Protein Index (IPI) human database V3.23. And data mining about the function of these proteins were also conducted.
Results:
In first section, after the treatment by ProteoMinerTM column, the total number of spots in the 2-D gel was 1432±85, whereas 1123±114 spots were observed on the 2-D gels treated by ice-cold acetone. There were significant differences between the two prefractionation methods (P<0.05, F=8.885). Using ProteoMinerTM clearly improved the resolution and increased the intensity of the low abundance proteins compared with 2-D analysis of acetone precipitated CSF samples, and simultaneously reduced the high abundant proteins. Thus this prefractionation method was applicable for further research.
In second section, low abundant proteins in the CSF of the TBI group and the control group were enriched by ProteoMiner, and separated by 2D-DIGE, the map of CSF proteins was clear. The results of biological variation analysis (BVA) on the TBI group and the control group showed 169 protein spots with an expression change over 1.5-fold.98 up-regulated and 71 down-regulated protein spots were selected for further analysis with MALDI-TOF mass spectrometry.47 spots corresponded to 36 distinct proteins were identified. These identified proteins have been grouped into different categories based on their possible biofunctions:cytoskeleton. intermediary metabolism, signaling transduction, stress response, protein metabolism and unknown. Among these proteins, the ceruloplasmin, parvalbumin, Krueppel-like factor 6. phospholipid transfer protein, SLC25A23, Bromodomain containing protein 1 and F-box protein 7 are associated with central nervous system (CNS) diseases. This study first show expression changes in these proteins in acute TBI patients.
Conclusion:
The mechanical injury to the brain apparently affects the protein profile of CSF in the acute phase, and makes CSF a better window to study TBI and other CNS diseases. The use of the protein equalizer technology (ProteoMinerTM) increased 2-DE gel resolution and enabled detection of low abundance proteins compared with the precipitation technique. Up-regulation and down-regulation of proteins existed at the same time. Although further confirmation may need, these differential expressed proteins may become the biomarker for evaluating injury severity or predicting the clinical outcome.
引文
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