胆囊癌组织相关蛋白的筛选与鉴定
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摘要
背景:原发性胆囊癌是恶性程度非常高的肿瘤,发病率有逐年上升的趋势,晚期胆囊癌5年生存率低于5%,而早期胆囊癌预后较好,5年生存率可高于80%,但无特异性临床表现,早期诊断困难,缺乏特异的诊断标志,临床上发现的早期胆囊癌多为意外性胆囊癌。胆囊结石并慢性胆囊炎是胆囊癌公认的危险因子,单个结石直径>3cm是导致胆囊癌发生的重要原因。胆囊癌合并有胆囊结石发生率可高达94%。结石嵌顿引起胆管阻塞使胆汁淤积引起胆囊黏膜慢性炎症、增生与胆囊癌的癌变过程有千丝万缕的关系。研究目的:在蛋白质组学水平筛选和鉴定与胆囊癌致病相关的差异蛋白,以期找到与胆囊癌诊断、治疗、预后相关的特异性标志物,发现胆囊癌诊疗的新颖靶点,更好的探讨和了解胆囊癌的发病机理。研究方法:本研究运用成熟的双向电泳-质谱鉴定技术,在10例原发性胆囊癌中,以胆囊结石并慢性胆囊炎、正常胆囊组织和部分癌旁正常胆囊组织作为对照,进行双向电泳实验,选取有代表的三次二维电泳实验结果,通过两两比较,满足组间三次平行电泳实验平均值±SD差大于2倍的条件,被认为差异表达,以此为标准筛选差异蛋白表达点。选取依照胆囊组-癌前病变组-正常对照组或有下调趋势,或有上调趋势的差异表达点进行PMF-MALDI-TOF/TOF质谱鉴定工作,鉴定的标准包括分子量、等电点、质谱检测肽段在整个蛋白质中的覆盖率、匹配度分值,蛋白得分大于56被认为有统计学意义(p<0.05)。鉴定数据经MASCOT检索,明确蛋白名称。在此基础上,选取部分感兴趣的上调和下调蛋白运用Realtime-PCR及其Western印迹方法从mRNA水平及蛋白质水平两个方面进行表达验证。最后,选取有潜在意义的蛋白在大样本的胆囊癌组织芯片中,进行免疫组化表达验证。以探讨蛋白之间的相关性以及与胆囊癌的临床病理学行为的关系及意义。结果:第一部分双向电泳试验中,以胆囊结石并慢性胆囊炎和正常胆囊、癌旁组织为对照,共寻找到66个与胆囊癌相关的差异表达点,其中在胆囊癌中上调表达点21个,下调表达点45个。26个蛋白差异点入选质谱鉴定工作,鉴定出21个差异表达蛋白(部分蛋白重复),其中在胆囊癌中上调表达的10个,包括:膜联蛋白A4,膜突蛋白,人纤维蛋白素原β链,肌凝蛋白、肌动蛋白-胞质2、放射相关性蛋白3,血清白蛋白;下调的蛋白11个:血红蛋白β亚基,肌动蛋白-大血管平滑肌,原肌凝蛋白α-1链,(肌动蛋白)凝溶胶蛋白,凝胶溶素胶原α-1(VI)链,超(过)氧化物歧化酶[铜-锌],半乳凝素-1,角蛋白II型细胞支架,(中间丝)波形蛋白,视黄醛脱氢酶1,热休克蛋白HSP-90-β。其中下调蛋白视黄醛脱氢酶1为新颖发现,未见其与肿瘤的相关报道。第二部分我们选取上调蛋白膜联蛋白A4(AnnexinA4)、膜突蛋白(Moesin)及下调蛋白视黄醛脱氢酶1Retinal dehydrogenase1、热休克蛋白90(Heat shock protein HSP 90-beta)、波形蛋白(Vimentin)经Realtime-PCR及WesternBlot验证,结果表明:膜联蛋白A4及膜突蛋白在癌组织标本中有高于对照组表达的趋势,而视黄醛脱氢酶1在对照组中的表达有高于癌组织组的趋势。由于样本量少,在这部分中我们仅能做一个趋势的判断。最后AnnexinA4、Moesin及Retinal dehydrogenase1入选进入大样本(59例)胆囊癌组织芯片免疫组化验证,结果表明:在慢性胆囊炎及癌旁组织中ALDH1A1阳性表达,而Annexin IV和Moesin呈阴性或为弱阳性表达,在59例胆囊癌组织中,ALDH1A1,Annexin IV和Moesin三者的表达率分别为62.7%(37/59)、42.4%(25/59)和35.6%(21/59),统计结果表明慢性胆囊炎、癌旁组织、胆囊癌组织中三者表达差异有统计学意义(p<0.05)。分析三者的表达关系与胆囊癌的临床病理联系表明:Moesin阳性表达与性别(男)、浸润深度、肝脏转移以及疾病进展呈正相关,Annexin IV与淋巴结转移和疾病进展高度相关,而ALDH1A1疾病进展和组织分化呈负相关。同时三者存在着Moesin与ALDH1A1呈负相关,Moesin与Annexin IV呈正相关,而ALDH1A1与Annexin IV无相关性的表达关系。结论:我们的结果提示: Moesin和Annexin IV有可能成为胆囊癌诊断或生物治疗的新颖靶点,其中,Moesin蛋白可能与雌激素受体相关的胆囊癌又千丝万缕的关系。我们第一次发现并报道ALDH1A1蛋白在抑制胆囊癌的生长和分化中可能有重要的作用,其直接催化的产物维甲酸可能可以抑制胆囊癌细胞的生长。最后,我们首次对胆囊癌组织的差异蛋白质做出大致描绘,这些结果或许可以为了解胆囊癌的发病机理提供很好的帮助。
Background:Primary carcinoma of the gallbladder (PCG) is a highly malignant tumor. And the morbidity seem step up year by year.Historically, the 5-year survival of advanced stage Gallbladder cancer are reported to be<5%. However, in the case of early GBC in which the depth of cancer invasion is limited to the lamina propria or the muscle layer of the gallbladder wall without nodal involvement, hematogenous metastasis or peritoneal implantation, a 5-year survival rate of >80% can be expected even when a simple cholecystectomy is performed. But, those gallbladder cancer in the early stage which lack specificity marker have no special clinical manifestation almost found accidental. Cholecystolithiasis affiliate chronic cholecystitis (CC) is one of its major risk factors.Sing stone diameter>3cm verify one of imprtant cause with PCG.Gallbladder cancer which affilinated Cholecystolithiasis are high to 94%. Objective:To identify the proteins involved in PCG carcinogenesis, wishing find special maker associated with gallbladder cancer dignosis,treatment and prognosis,So as to more comprehend pathogenesis of PCG Methods:we firstly employed two-dimensional electrophoresis (2-DE) coupled with MAILDE-TOF MS/MS analysis to identify differentially expressed proteins among PCG ,adjacent nontumor tissue samples, cholecystolithiasis Samples ,and nomal gallbladder samples.from 10 gallbladder cancer patients were analyzed. A total of 21 spots were significantly up-regulated (ratio≥2, p≤0.01) in tumor samples, while 45 spots were down-regulated (ratio≤-2, p≤0.01). Twenty-one gene products were identified among these spots.with 6 of these being reported for the first time in PCG, Of the 6 newly implicated proteins.Altered expression of representative proteins including Moesin, AnnexinA4, Retinal dehydrogenase1, Vimentin, Heat shock protein 90βwas validated by RT-PCR and Western blotting. Moesin, Annexin A4 was demonstrated to be up-regulated in cancer at both the mRNA and protein levels, adversely Retinal dehydrogenase 1showed in cancer. Therefore, Moesin, Annexin A4, Retinal dehydrogenase 1 were chosen for detailed analysis. Results: There are 66 spots associate gallballder cancer contrast with adjacent nontumor tissue samples and cholecystolithiasis samples, and 26 spot were employed for MAILDE-TOF MS/MS analysis. A total of Twenty-one spots were vertified to be protein. including ten up-regulated in tumor samples: Actin,cytoplasmic 2,Annexin A4,Fibrinogen beta chain, Moesin, Tropomyosin alpha-1 chain, eleven up-regulated including Collagen alpha-1(VI) chain, Heat shock protein, Gelsolin, Retinal dehydrogenase 1, Vimentin, Tropomyosin alpha-1 chain ,Actin,aortic smooth muscle, Keratin,type II cytoskeletal 1, Galectin-1 ,Hemoglobin subunit beta ,Superoxide dismutase [Cu-Zn](some protein repeat. RT-PCR and Western blotting show that Moesin, Annexin A4 was up-regulated in cancer adversely Retinal dehydrogenase 1 down-regulated in cancer. Immunohistochemical examination in 59 case gallbladder cancer showed that the enhanced expression of AnnexinA4 was correlated with clinical stage, lymph node involvement and enhanced expression of Moesin was correlated with sex, as well as Liver metastasis Wall invasion, All those being known indicators of a relatively poor prognosis in PCG patients.On the other hand, enhanced expression of Retinal dehydrogenase 1 negative correlation tumor stage and tissue Differentiation. Conclusions:The result suggest that Moesin,AnnexinA4 may be a potential biomarker for diagnosis, prognosis, monitoring in the therapy of PCG, While Retinal dehydrogenase 1 may be a potential prognosis factor.Further, this comprehensive strategy could be used for identifying other differentially expressed proteins that have potential to be candidate biomarkers of Primary carcinoma of the gallbladder.In summary, we for the first time profiled proteome alterations in PCG tissues and these results may provide useful insights for understanding the mechanism involved in the process of Primary carcinoma of the gallbladder.
Background:Primary carcinoma of the gallbladder (PCG) is a highly malignant tumor. And the morbidity seem step up year by year.Historically, the 5-year survival of advanced stage Gallbladder cancer are reported to be<5%. However, in the case of early GBC in which the depth of cancer invasion is limited to the lamina propria or the muscle layer of the gallbladder wall without nodal involvement, hematogenous metastasis or peritoneal implantation, a 5-year survival rate of >80% can be expected even when a simple cholecystectomy is performed. But, those gallbladder cancer in the early stage which lack specificity marker have no special clinical manifestation almost found accidental. Cholecystolithiasis affiliate chronic cholecystitis (CC) is one of its major risk factors.Sing stone diameter>3cm verify one of imprtant cause with PCG.Gallbladder cancer which affilinated Cholecystolithiasis are high to 94%. Objective:To identify the proteins involved in PCG carcinogenesis, wishing find special maker associated with gallbladder cancer dignosis,treatment and prognosis,So as to more comprehend pathogenesis of PCG Methods:we firstly employed two-dimensional electrophoresis (2-DE) coupled with MAILDE-TOF MS/MS analysis to identify differentially expressed proteins among PCG ,adjacent nontumor tissue samples, cholecystolithiasis Samples ,and nomal gallbladder samples.from 10 gallbladder cancer patients were analyzed. A total of 21 spots were significantly up-regulated (ratio≥2, p≤0.01) in tumor samples, while 45 spots were down-regulated (ratio≤-2, p≤0.01). Twenty-one gene products were identified among these spots.with 6 of these being reported for the first time in PCG, Of the 6 newly implicated proteins.Altered expression of representative proteins including Moesin, AnnexinA4, Retinal dehydrogenase1, Vimentin, Heat shock protein 90βwas validated by RT-PCR and Western blotting. Moesin, Annexin A4 was demonstrated to be up-regulated in cancer at both the mRNA and protein levels, adversely Retinal dehydrogenase 1showed in cancer. Therefore, Moesin, Annexin A4, Retinal dehydrogenase 1 were chosen for detailed analysis. Results: There are 66 spots associate gallballder cancer contrast with adjacent nontumor tissue samples and cholecystolithiasis samples, and 26 spot were employed for MAILDE-TOF MS/MS analysis. A total of Twenty-one spots were vertified to be protein. including ten up-regulated in tumor samples: Actin,cytoplasmic 2,Annexin A4,Fibrinogen beta chain, Moesin, Tropomyosin alpha-1 chain, eleven up-regulated including Collagen alpha-1(VI) chain, Heat shock protein, Gelsolin, Retinal dehydrogenase 1, Vimentin, Tropomyosin alpha-1 chain ,Actin,aortic smooth muscle, Keratin,type II cytoskeletal 1, Galectin-1 ,Hemoglobin subunit beta ,Superoxide dismutase [Cu-Zn](some protein repeat. RT-PCR and Western blotting show that Moesin, Annexin A4 was up-regulated in cancer adversely Retinal dehydrogenase 1 down-regulated in cancer. Immunohistochemical examination in 59 case gallbladder cancer showed that the enhanced expression of AnnexinA4 was correlated with clinical stage, lymph node involvement and enhanced expression of Moesin was correlated with sex, as well as Liver metastasis Wall invasion, All those being known indicators of a relatively poor prognosis in PCG patients.On the other hand, enhanced expression of Retinal dehydrogenase 1 negative correlation tumor stage and tissue Differentiation. Conclusions:The result suggest that Moesin,AnnexinA4 may be a potential biomarker for diagnosis, prognosis, monitoring in the therapy of PCG, While Retinal dehydrogenase 1 may be a potential prognosis factor.Further, this comprehensive strategy could be used for identifying other differentially expressed proteins that have potential to be candidate biomarkers of Primary carcinoma of the gallbladder.In summary, we for the first time profiled proteome alterations in PCG tissues and these results may provide useful insights for understanding the mechanism involved in the process of Primary carcinoma of the gallbladder.
引文
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[8] Craven R A, Stanley A J, Hanrahan S et al Proteomic analysis of primary cell lines identifies protein changes present in renal cell carcinoma. Proteomics,2006 May; 6(9): 2853~ 64.
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[10] Ponnampalam AP, Rogers P A.Cyclic changes and hormonal regulation of annexin IV mRNA and protein in human endometrium. Mol-Hum-Reprod. 2006 Nov; 12(11): 661~ 9.
[11] Zimmermann U, Balabanov S, Giebel J,et al Increased expression and altered location of annexin IV in renal clear cell carcinoma: a possible role in tumour dissemination. Cancer-Lett. 2004 Jun 8; 209(1): 111~ 18.
[1] Lu CA, C.Altieri D, Tanigawa. Expression of a novel antiapoptosis gene, surviving, correlated with tumor cell apoptosis and p53 accumulation in gastric carcinomas. Cancer Res, 1998; 58(9):1808~ 12.
[2] Alfonso P, Canamero M, Fernandez-Carbonie F,et al. Proteome Analysis of Membrane Fractions in Colorectal Carcinomas by Using 2D-DIGE Saturation Labeling. J-Proteome-Res. 2008 Oct; 7(10): 4247~ 55.
[3] Kang JS,Cairo BF,Maygarden SJ,et al.Dysregnlation of annexin I protein expression in high·grade prostatic intraepithelial neoplasia and prostate cancer.Clin Cancer Bes,2002;8(1): l17~ 123.
[4] Emote K,Yamada Y,Sawada H,et al.Annexin II overexpression corre1ares with stromal tenascin·C overexpression a prognostic marker in colorectal carcinoma.Cancer,2001,92(6):1419~ 1426.
[5] Francia G,Mitchell SD,Mose SE,et al Idenfification by differential display of annexin-VI,a gene diferentially expressed during melanoma progression Cancer Res,1996,56(17):3855~ 3858.
[6] Srlvastava M,Bubendorf L,Srikantan V .Anx7,a candidate tumor suppressor gene for prostate cancer.Prec NadAcad Sci USA 2001;98(8):4575~ 4580.
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[8] Shen J, Person M D, Zhu J,et al. Protein expression profiles in pancreatic adenocarcinoma compared with normal pancreatic tissue and tissue affected by pancreatitis as detected by two-dimensional gel electrophoresis and mass spectrometry. Cancer-Res. 2004 Dec 15; 64(24): 9018~ 9026.
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[10]Carmeci C.Moesin expression in breast cancer Surgery l998;124:211.
[11]Balkis Budin, SF. Othman,et al.Effect of alpha lipoic acid on oxidative stress and vascular wall of diabetic rats. Rom J Morphol Embryol 2009; 50(1): 23~ 30.
[12] Daiss N MG., Lobo.Changes in postharvest quality of Swiss chard grown using 3organic preharvest treatments. J Food Sci 2008; 73(6): 314~ 20.
[13] Manicassamy SR,Ravindran.Toll-like receptor 2-dependent induction of vitamin A-metabolizing enzymes in dendritic cells promotes T regulatory responses and inhibits autoimmunity Nat Med. 2009; 567~ 72.
[14] David A. Jones, Lassmann.Alpha-folate receptor expression in epithelial ovarian carcinoma and non-neoplastic ovarian tissue.Anticancer Res2008; 28(6A): 3567~ 72.
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[3] Sreedhar AS,Soti C,Csennely P.Inhibition of Hsp90:a new strategy for inhibiting protein kinases.Biechim Biophys Acta.2004;1697(1-2):233~ 242.
[4] Schulte TW,Neckem LM.Geldanamycin induced destabilization of Raf-1 involves the proteasome.Biochem Biophys Res Commun.1997;239(3):655~ 659.
[5] Domagala W ,Wozniak J,Lasota J,et al Vimentin is preferentially expressed in high-grade ductal and med-dullary, but not in lobular breast carcinoma. Ant J.Pathol,1990;137:1059.
[6] Jun-Cheng WEI,Ming-Fu WU,Yong-Tao ZHANG et al. Vimentin affect invasion and metastatic of carcinoma of prostate.2008;Cancer 27(1):30~ 34.
[7] Kobel M, Gradhand E, Zeng K,et al Ezrin promotes ovarian carcinoma cell invasion and its retained expression predicts poor prognosis in ovarian carcinoma. Int-J-Gynecol-Pathol. 2006 Apr; 25(2): 121~ 30.
[8] Craven R A, Stanley A J, Hanrahan S et al Proteomic analysis of primary cell lines identifies protein changes present in renal cell carcinoma. Proteomics,2006 May; 6(9): 2853~ 64.
[9] Rossy J, Gutjahr M C, Blaser N, et al. Ezrin/moesin in motile Walker 256 carcinosarcoma cells: signal-dependent relocalization and role in migration. Exp-Cell-Res. 2007 Apr 1; 313(6): 1106~ 20.
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[11] Zimmermann U, Balabanov S, Giebel J,et al Increased expression and altered location of annexin IV in renal clear cell carcinoma: a possible role in tumour dissemination. Cancer-Lett. 2004 Jun 8; 209(1): 111~ 18.
[1] Lu CA, C.Altieri D, Tanigawa. Expression of a novel antiapoptosis gene, surviving, correlated with tumor cell apoptosis and p53 accumulation in gastric carcinomas. Cancer Res, 1998; 58(9):1808~ 12.
[2] Alfonso P, Canamero M, Fernandez-Carbonie F,et al. Proteome Analysis of Membrane Fractions in Colorectal Carcinomas by Using 2D-DIGE Saturation Labeling. J-Proteome-Res. 2008 Oct; 7(10): 4247~ 55.
[3] Kang JS,Cairo BF,Maygarden SJ,et al.Dysregnlation of annexin I protein expression in high·grade prostatic intraepithelial neoplasia and prostate cancer.Clin Cancer Bes,2002;8(1): l17~ 123.
[4] Emote K,Yamada Y,Sawada H,et al.Annexin II overexpression corre1ares with stromal tenascin·C overexpression a prognostic marker in colorectal carcinoma.Cancer,2001,92(6):1419~ 1426.
[5] Francia G,Mitchell SD,Mose SE,et al Idenfification by differential display of annexin-VI,a gene diferentially expressed during melanoma progression Cancer Res,1996,56(17):3855~ 3858.
[6] Srlvastava M,Bubendorf L,Srikantan V .Anx7,a candidate tumor suppressor gene for prostate cancer.Prec NadAcad Sci USA 2001;98(8):4575~ 4580.
[7] Zimmermann U, Balabanov S, Giebel J,etal Increased expression and altered location of annexin IV in renal clear cell carcinoma: a possible role in tumour dissemination. Cancer-Lett.2004 Jun 8; 209(1): 111~ 118.
[8] Shen J, Person M D, Zhu J,et al. Protein expression profiles in pancreatic adenocarcinoma compared with normal pancreatic tissue and tissue affected by pancreatitis as detected by two-dimensional gel electrophoresis and mass spectrometry. Cancer-Res. 2004 Dec 15; 64(24): 9018~ 9026.
[9]Roa L,Araya J L,Villaseca M, et al Gallbladder cancer immunohistochemical expression of the protein related to estrogen receptor(p29) and of the protein induced by estrogen(PS2 )Rev Med Chil.1995;123(11):1333.
[10]Carmeci C.Moesin expression in breast cancer Surgery l998;124:211.
[11]Balkis Budin, SF. Othman,et al.Effect of alpha lipoic acid on oxidative stress and vascular wall of diabetic rats. Rom J Morphol Embryol 2009; 50(1): 23~ 30.
[12] Daiss N MG., Lobo.Changes in postharvest quality of Swiss chard grown using 3organic preharvest treatments. J Food Sci 2008; 73(6): 314~ 20.
[13] Manicassamy SR,Ravindran.Toll-like receptor 2-dependent induction of vitamin A-metabolizing enzymes in dendritic cells promotes T regulatory responses and inhibits autoimmunity Nat Med. 2009; 567~ 72.
[14] David A. Jones, Lassmann.Alpha-folate receptor expression in epithelial ovarian carcinoma and non-neoplastic ovarian tissue.Anticancer Res2008; 28(6A): 3567~ 72.
1. Wilkins MR,Pasquali C,Appel RD,el a1.From proteins to pro-teomes:largre scale protein identification by two·dimensional ele trophoresis and anlinoacid analysis[J].Bioteehnology,1996,14(1):61~ 65.
2. Hanash SM,Bobek MP,Richman DS,et a1.Integrating cancer genomics and proteomics in the post—genome era. Proteomics 2002.2(1):69~ 75.
3. Okuzawa K,Franzen B,Lindholm J,et a1.Characterization of gene expression in clinical lung cancer materials by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis,l994.15(3-4):382~ 390.
4. Hirano T,Gong Y,Yoshida K,et a1.Usefulness of TA02 (napain A) to distinguish primary lung adenocarcinoma from metastatic lung adenocareinmoma.Lung Cancer,2003,41(2):l55~ l62.
5. Ueno T,Linder S,Elmberger G.Aspartic proteinase napsin is auseful marker for diagnosis of primary lung adenocarcinoma.Br JCancer,2003,88(8):l229~ 1233.
6. Emmert—Buck,MR.Laser capture microdissection.[J].Science,1996,274(5289),998~ 1001.
7. Unlu M,Morgan ME,Minden js.Diferential gel electrophoresis:asin~e gel method for detecting changes in protein extracts.[J].Elec·trophoresis,1997,18(11),2071~ 2077.
8. Zhukov TA.Johanson RA.Cantor AB,etal.Discovery of distinct protein profiles specific for lung tumors and pre-malignant lung lesions by SELDI mass spectrometry[J].lung Cancer.20O3,40(3):267~ 279.
9. CazaresLH,Adambl,Ward M D etal Norma1 benign prencoplastic,and malignant prostate cells have distinct protein expression profiles resolved by surface enhanced laser desorption/ionization mass spectrometry[J].Clin cancer Res.2002.8(8):254l~ 2545.
10. Liotta LA, Kohn EC. The microenvironment of the tumor-host interface.Nature, 2001, 411(6835): 375~ 379.
11. Aebersold R,Mann M.Mass spectrometry-based proteomics [J]. Nature, 2003, 422(6928):198~ 207.
12. Wu ww,Wang G,Back SJ,et a1.Comparative study of three proteomic quantitative methods,DIGE,ICAT,andiTRAQ,using 2D gel-or LC-MALDI TOF/TOF[J].J Pro.teome Res,2006,5(3):651~ 658.
13. Pon TC.Opportunities and limitations of SELDI-TOF-MS in biomedical research:practical advices.Expert Rev Proteomics,2007,4(1):51~ 65.
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