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Expressions of Calcium-binding Protein and Related Protein in the Endplate Cartilage of Patients with Idiopathic Scoliosis
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摘要:
目的 观察钙结合蛋白S100A8、热休克蛋白(heat shock protein, HSP)90和钙调蛋白(calmodulin, CaM)基因在特发性脊柱侧凸(idiopathic scoliosis, IS)患者和先天性脊柱侧凸(congenital scoliosis, CS)患者椎间盘终板内的表达。 方法 收集经临床和影像学诊断为特发性脊柱侧凸的前路脊柱手术患者的椎间盘终板和先天性脊柱侧凸患者的椎间盘终板各4例, 用TRIzol法提取终板软骨中的总蛋白, 采用Western blot技术分析和对比椎间盘终板中S100A8、HSP90和CaM基因的表达。 结果 S100A8在特发性脊柱侧凸和先天性脊柱侧凸患者中的表达有显著性差异, 而CaM和HSP90则没有明显差别。 结论 S100A8基因在特发性脊柱侧凸发生发展过程中起到一定的作用, 需对该基因的表达和调控做进一步研究。 Abstract:Objective To observe the expression of S100A8, heat shock protein(HSP)90, and calmodulin(CaM)in the discs endplate cartilage of patients with idiopathic scoliosis(IS)and congenital scoliosis(CS). Methods The discs of 4 IS patients(diagnosed by clinical and radiological data)and 4 CS patients who had undergone anterior-route surgeries were collected.Total protein was extracted from endplate cartilage with TRIzol method.The expressions of S100A8, HSP90, and CaM genes in the cartilages were analyzed using Western blot. Results The expressions of HSP90 and CaM in the cartilages were not significantly different between CS patients and IS patients, while the expression of S100A8 was significantly higher in IS patients than that in CS patients. Conclusion S100A8 may play a role in the occurrence and development of IS. -
Key words:
- scoliosis /
- endplate /
- S100A8 /
- heat shock protein 90 /
- calmodulin
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图 1 S和CS患者椎间盘终板S100A8、HSP90和CaM蛋白表达水平
41 ~ 44:CS患者顶椎终板凹侧、顶椎终板凸侧、端椎终板凹侧和端椎终板凸侧; 45 ~ 48:IS患者顶椎终板凹侧、顶椎终板凸侧、端椎终板凹侧和端椎终板凸侧; IS:特发性脊柱侧凸; CS:先天性脊柱侧凸; HSP:热休克蛋白; CaM:钙调蛋白
表 1 蛋白样品的紫外吸收和浓度数据
表 2 CS和IS患者椎间盘终板S100A8、HSP90和CaM蛋白表达水平比较
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[1] 邱贵兴, 钱文伟, 吴志宏, 等.青少年特发性脊柱侧凸脊柱关节突骨组织差异基因表达的研究[J].中华医学杂志, 2006, 86:2328-2333. http://www.wanfangdata.com.cn/details/detail.do?_type=perio&id=zhyx200633009 [2] 李洪凤, 董秀兰.CaM及其抑制剂在神经系统疾病中研究进展[J].社区医学杂志, 2007:51-53. http://www.wanfangdata.com.cn/details/detail.do?_type=perio&id=sqyxzz200717034 [3] 羊明智, 吴叶, 章亚东, 等.钙调素及其依赖性激酶对即早基因c-fos表达的影响[J].南华大学学报:医学版, 2007, 35:529-532. http://www.wanfangdata.com.cn/details/detail.do?_type=perio&id=nhdxxb-yxb200704016 [4] Machida M, Dubousset J, Imamura Y, et al.Melatonin, a possible role inpathogenesis of adolescent idiopathic scoliosis.[J].Spine(Phila Pa 1976), 1996, 21:1147-1152. doi: 10.1097/00007632-199605150-00005 [5] Inoue M, Minami S, Nakata Y, et al.Association between estrogen receptor genepolymorphisms and curveseverity of idiopathic scoliosis.[J].Spine(Phila Pa 1976), 2002, 27:2357-2362. doi: 10.1097/00007632-200211010-00009 [6] Dubousset J, Queneau P, Thillard MJ.Experimental scoliosis induced by pineal and diencephalic lesions in young chickens:its relation with clinical findings[J].Orthop Trans, 1983, 7:7. http://ci.nii.ac.jp/naid/10015785822 [7] Benitez-King G, Huerto-Delgadillo L, Anton-Tay F.Melatonin modifies calmodulin cell levelsin MDCK and N1E-115 cell lines and inhibits phosphodiesterase activity in vitro[J]. Brain Res, 1991, 557:289-292. doi: 10.1016/0006-8993(91)90146-M [8] Benitez-King G, Anton-Tay F.Calmodulinme diates melatonin cytoskeletal effects.[J].Experientia, 1993, 49:635- 641. doi: 10.1007/BF01923944 [9] Pozo D, Reiter RJ, Calvo JR, et al.Inhibition of cerebellar nitricoxide synthase and cyclic GMP production by melatonin via complex formation with calmodulin[J].J Cell Biochem, 1997, 65:430-442. doi: 10.1002/(SICI)1097-4644(19970601)65:3<430::AID-JCB12>3.0.CO;2-J [10] Huerto-Delgadillo L, Anton-Tay F, Benitez-King G.Effects of melatonin on microtubule as sembly depend on hormone concentration:role of melatonin as a calmodulin antagonist [J].J Pineal Res, 1994, 17:55-62. doi: 10.1111/j.1600-079X.1994.tb00114.x [11] Benitez-King G, Rios A, Martinez A, et al.Invitro inhibition of Ca2+ /calmodulin-dependent kinase Ⅱ activity bymelatonin[J].Biochim Biophys Acta, 1996, 1290:191-196. doi: 10.1016/0304-4165(96)00025-6 [12] 孟金兰, 兰爱平, 杨春涛, 等.热休克蛋白90在硫化氢保护PC12细胞对抗化学性缺氧损伤中的作用[J].中国药理学通报, 2010:103-107. http://www.wanfangdata.com.cn/details/detail.do?_type=perio&id=zgylxtb201001027 [13] 耿红莲, 仲人前.Toll样受体、热休克蛋白90与多发性骨髓瘤[J].中国实验诊断学, 2010, 14:1344-1345. http://www.wanfangdata.com.cn/details/detail.do?_type=perio&id=zgsyzdx201008085 [14] 刘炎.分子伴侣功能的研究进展[J].国外医学:遗传学分册, 2002, 25:70-73. [15] Pratt WB.The hsp90-based chaperone system:involvement in signal transduction from a variety of hormone and growth factor receptors[J].Proc Soc Exp Biol Med, 1998, 217: 420-434. doi: 10.3181/00379727-217-44252 [16] Richter K, Buchner J.Hsp90:chaperoning signal transduction.[J].J Cell Physiol, 2001, 188:281-290. doi: 10.1002/jcp.1131 [17] Scroggins BT, Robzyk K, Wang D, et al.Anacetylation site in the middle domain of Hsp90 regulates chaperone function[J].Mol Cell, 2007, 25:151-159. doi: 10.1016/j.molcel.2006.12.008 [18] Kim S, Kang J, Hu W, et al.Geldanamycin decreases Raf-1 and Akt levels and induces apoptosis in neurob lastomas[J]. Int J Cancer, 2003, 103:352-359. doi: 10.1002/ijc.10820 [19] Supino-Rosin L, Yoshimura A, Yarden Y, et al.Intracellular retention and degradation of the epidermal growth factor receptor, two distinct processes mediated by benzoquinone ansamycins[J].J Biol Chem, 2000, 275:21850-21855. doi: 10.1074/jbc.M001834200 [20] Xu Y, Singer MA, Lindquist S.Maturation of thetyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90 [J].Proc Natl Acad Sci USA, 1999, 96:109-114. doi: 10.1073/pnas.96.1.109 [21] Sato S, Fujita N, Tsuruo T.Modulation of Aktkinase activity by binding to Hsp90 [J].Proc Natl Acad Sci USA, 2000, 97:10832-10837. doi: 10.1073/pnas.170276797 [22] Nimmanapalli R, O'Bryan E, Bhalla K.Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lower Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts[J].Cancer Res, 2001, 61:1799-1804. http://europepmc.org/abstract/med/11280726 [23] Blagosklonny MV, Toretsky J, Bohen S, et al.Mutantconformation of p53 translated in vitro or invivo requires functional HSP90 [J].Proc Natl Acad Sci USA, 1996, 93: 8379-8383. doi: 10.1073/pnas.93.16.8379 [24] Workman P.Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone.[J].Cancer Lett, 2004, 206:149-157. doi: 10.1016/j.canlet.2003.08.032 [25] Pratt WB.The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor[J].J Biol Chem, 1993, 268:21455-21458. http://www.ncbi.nlm.nih.gov/pubmed/8407992 [26] Donato R.RAGE:a single receptor for several ligands and different cell ularresponses:the case of certain S100 proteins [J].Curr Mol Med, 2007, 7:711-724. doi: 10.2174/156652407783220688 [27] 刘睿, 张贺龙.S100蛋白家族成员与肿瘤关系的研究进展[J].现代肿瘤医学, 2010, 18:200-202. http://www.wanfangdata.com.cn/details/detail.do?_type=perio&id=sxzlyx201001077 -
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