热休克蛋白在乳腺癌中的作用

热休克蛋白是细胞受各种应激原刺激后诱导产生的一组应激蛋白，具有维持细胞蛋白稳定、促进细胞生存等功能，在细胞生长、发育、分化、基因转录等方面发挥重要作用，近年来发现热休克蛋白也与肿瘤细胞的发生、发展密切相关。在多种肿瘤组织中发现热休克蛋白存在高表达，尤其在乳腺癌中与患者预后密切相关，本文就热休克蛋白的结构、生物学功能、致癌机理以及乳腺癌的关系作一概述。     

热应激诱导兔脑热休克蛋白70的合成研究

探讨热应激与热休克诱导的脑组织不同细胞热休克蛋白７０合成。     

热休克蛋白抑制慢性心理应激引起的焦虑样行为增加

目的：采用HSFI基因敲除小鼠模型探讨热休克蛋白（heat shock protein，HSP）对慢性心理应激引起的焦虑样行为增加的抑制作用。方法：将热休克因子1（heat shock factor 1）基因野生型小鼠（HSFI＋／＋）和热休克因子1基因敲除小鼠（HSF1-／-）暴露于2个月的慢性心理应激，部分小鼠在暴露于慢性心理应激前给予热休克预处理，2个月后采用高架十字迷宫和旷场实验检测各组小鼠焦虑样行为，Western blots检测和比较HSP72，HSC70表达，采用多因素析因设计方差分析对各组小鼠焦虑样行为进行比较。结果：慢性心理应激引起焦虑样行为增加．HSF1基因敲除导致焦虑样行为增加更加明显。热休克预处理使野生型小鼠海马组织中HSP70。HSC70明显升高，并明显减轻了心理应激所致的焦虑样行为的增加。HSF1基因敲除废除了热休克所致的HSP诱导表达及其对心理应激所致焦虑样行为增加的抑制作用。结论：诱导型HSP在抑制心理应激引起的焦虑样行为增加中起着重要的作用。     

热休克蛋白在乳腺癌中的作用

热休克蛋白是细胞受各种应激原刺激后诱导产生的一组应激蛋白,具有维持细胞蛋白稳定、促进细胞生存等功能,在细胞生长、发育、分化、基因转录等方面发挥重要作用.近年来发现热休克蛋白也与肿瘤细胞的发生、发展密切相关.在多种肿瘤组织中发现热休克蛋白存在高表达,尤其在乳腺癌中与患者预后密切相关.本文就热休克蛋白的结构、生物学功能、致癌机理以及与乳腺癌的关系作一概述.     

热休克蛋白的应用前景

在不利的环境中,机体都有共同的反应,即正常基因的表达抑制和一组特殊基因热休克基因的激活和表达,这一普遍的生物现象称为热休克反应,其产物热休克蛋白是一组非常保守的蛋白分子家族。它们介导其它蛋白质的跨膜转运和正确装配,起着“分子伴侣”的重要作用,与细胞的许多重要生理过程相关,在维持细胞正常功能上起关键作用。由于它具有高度保守性及众多的生物学功能,其研究日益受到广泛重视。     

人热休克蛋白70基因的原核表达

目的 表达人热休克蛋白70（HSP70）并进行鉴定。方法 用PCR方法扩增人HSP70基因片段，经T-A克隆法克隆到载体pUCm-T中，并进行DNA测序，将人HSP70基因片段从载体pUCm-T中酶切后，构建重组表达载体pGEX-4T-1-HSP70，并转化大肠杆菌JM109，用IPTG诱导，收集细菌，菌体裂解后进行SDS-PAGE及Western blot检测。结果 人HSP70基因的PCR产物约为1.9kb。序列测定结果证实，所获目的序列与文献[3]报道的相一致，经EcoRⅠ和XhoⅠ酶切鉴定证实。人HSP70基因已成功地克隆到表达载体pGEX-4T-1中，构建的表达载体pGEX-4T-1-HSP70，能很好地在大肠杆菌中表达相对分子质量（Mr)为96000并具有抗原特性的融合蛋白，结论 成功地克隆并表达了HSP70基因，为研究HSP70的结构。功能与临床应用提供了必要条件。     

热休克蛋白调控的研究进展

热休克蛋白-肽复合物,在机体杀伤肿瘤细胞中发挥了关键的作用,因而以热休克蛋白肽为基础的肿瘤疫苗成为研究的热点。通过热休克处理、细胞因子共孵育等方法,可促进细胞表达热休克蛋白肽;口服某些化合物也能促进机体细胞热休克蛋白肽的表达。这些方法能促进热休克蛋白肽的表达,便于制备充足的疫苗应用于临床,具有广阔的发展前景。     

热休克蛋白47和热休克蛋白60在小鼠胚胎器官形成过程中的表达

目的：研究小鼠胚胎器官形成过程中热休克蛋白47（Hsp47）和热休克蛋白60（Hsp60）的表达情况。方法：于GD11～GD18,取得小鼠胚胎脑、眼、心、肺、胃、肝、四肢,于GD13-GD18取得肾,利用RT-PCR方法半定量检测Hsp47和Hsp60在各器官的表达丰度。结果：Hsp47在GD11～GD12和GD18的脑、GD11～GD12和GD17～GD18的眼、GD11～GD12和GD16～GD18的肺、GD11-GD18的肝脏不表达,在其余时间和其余器官均有表达;Hsp60在CD11～GD18时段胚胎的脑、眼、心、肺、胃、肝、肾（GD13～GD18）、四肢中均有表达。结论：Hsp47和Hsp60在小鼠胚胎器官形成过程中有不同的表达丰度,其表达模式也不一致;Hsp47在小鼠胚胎发育过程中可能有重要功能,Hsp60则具有广泛表达的特点。     

The Role of Heat Shock Protein 90 in the Regulation of Tumor Cell Apoptosis

Programmed death of Jurkat tumor cells was studied under conditions of culturing with 17-AAG selective inhibitor of heat shock protein with a molecular weight of 90 kDa and etoposide. Apoptosis realization was evaluated by fluorescent microscopy with FITC-labeled annexin V and propidium iodide. Activity of caspase-3 was evaluated spectrophotometrically. Inhibition of heat shock protein with a molecular weight of 90 kDa activated the apoptotic program in Jurkat tumor cells and etoposide-induced apoptosis. The heat shock protein with a molecular weight of 90 kDa acted as apoptosis inhibitor in tumor cells.     

HSP90以及IL-6在系统型红斑狼疮发病中的作用

目的研究系统型红斑狼疮(systemiclupuserythematosus,SLE)患者外周血单个核细胞(PBMC)中热休克蛋白90(HSP90)、血清中白细胞介素6(IL6)的水平,探讨与活动期SLE的相关性。方法应用Western印迹检测20例SLE活动期患者(A组)与20例正常人(B组)PBMC中HSP90的表达,并利用酶联免疫法(ELISA)检测其血清中IL6水平。结果①A组HSP90表达水平为0.47±0.05,B组为0.18±0.07,差异有统计学意义(P<0.01);②血清中IL6水平在A组[(32.97±8.65)pg/ml]显著高于B组[(10.46±4.33)pg/ml](P<0.05);③A组血清中IL6水平与PBMC中HSP90表达呈正相关(r=0.61,P<0.01),且与SLE疾病活动指数(SLEDAI)正相关(r=0.48,P<0.01)。结论IL6可作为病情活动监测指标,IL6与HSP90的异常高表达可能在SLE发病机制中起重要作用。     

Heat Shock Protein 47 Promotes Glioma Angiogenesis

Heat shock protein 47 (HSP47) is a collagen‐binding protein, which has been recently found to express in glioma vessels. However, the expression profile of HSP47 in glioma patients and the underlying mechanisms of HSP47 on glioma angiogenesis are not fully explored. In the current study, we found that expression of HSP47 in glioma vessels was correlated with the grades of gliomas. HSP47 knockdown by siRNAs significantly decreased cell viability in vitro and tumor volume in vivo; moreover, it reduced the microvessel density (MVD) by CD31 immunohistochemistry in vivo. HSP47 knockdown significantly inhibited tube formation, invasion and proliferation of human umbilical vein endothelial cells (HUVECs). Furthermore, conditional medium derived from HSP47 knockdown cells significantly inhibited HUVECs tube formation and migration, while it increased chemosensitivity of HUVECs cells to Avastin. Silencing of HSP47 decreased VEGF expression in glioma cells consistently, and reduced glioma vasculature. Furthermore, HSP47 promoted glioma angiogenesis through HIF1α‐VEGFR2 signaling. The present study demonstrates that HSP47 promotes glioma angiogenesis and highlights the importance of HSP47 as an attractive therapeutic target of GBM.     

热休克蛋白60KD与动脉粥样硬化

热休克蛋白（ＨｅａｔｓｈｏｃｋｐｒｏｔｅｉｎＨＳＰ）是一种应激蛋白。原核细胞和真核细胞在各种应激刺激和许多其它损伤因素包括物理因素、化学因子、缺血、缺氧、氧自由基、中毒及创伤作用下均可产生ＨＳＰ。科学家们迄今对许多进化程度不同的物种的ＨＳＰ家族成员进行了基因和序列分析,发现ＨＳＰ属生物界分布最广泛、结构最保守的蛋白质之列．从大肠杆菌到人的ＨＳＰ氨基酸序列有５０％以上同源性。ＨＳＰ广泛存在于各种病原微生物中,而且是优势免疫原。这对免疫系统无疑是一种挑战。下面将对与免疫反应有关的热休克蛋白及其动脉粥…     

热休克蛋白70对未成熟心肌细胞功能的影响

目的探讨热休克蛋白70(HSP70)对未成熟心肌细胞功能的影响。方法健康新生长耳大白兔随机分为2组。对照组(C):腹腔注射生理盐水0.4ml,注射后24h取离体心脏,常规建立Langendorff离体心脏灌注模型,灌注15min转为工作心15min后停灌45min,恢复灌注15min改为工作心30min。实验组(E):腹腔注射重酒石酸去甲肾上腺素,24h后取离体心脏,方法同对照组。测定心肌细胞中HSP70含量及相关生化指标并作统计学处理比较。结果HSP70含量E组明显高于C组;E组ATP含量、SOD活性方面均优于C组(P<0.01),MDA含量、CK、LDH漏出率方面均低于C组(P<0.01),心肌线粒体Ca2+-ATPase活性、[ATP]m均优于C组(P<0.01),心肌细胞内Ca2+含量、心肌线粒体Ca2+含量低于C组(P<0.01)。结论HSP70对缺血再灌注未成熟心肌细胞功能具有明显的保护作用。     

Short-Term Highly Intense Physiological Stress Causes an Increase in the Expression of Heat Shock Protein in Human Leukocytes

Extracellular heat shock protein with molecular weight of 70 kDa is a signal molecule of the immune system. It is secreted by the peripheral blood, liver and muscle cells in response to physiological, thermal, and mental stresses. The main goal of our study was to compare the levels of expression of heat shock protein (70 kDa) matrix ribonucleic acid in leukocytes and serum concentrations of the protein before and after physiological stress. In order to solve this problem, we developed enzyme immunoassay of serum heat shock (70 kDa) protein concentration and a method for evaluating the expression of matrix ribonucleic acid of this protein in leukocytes by the real time PCR. The concentration of 70 kDa heat shock protein in the serum increased 1.7 times as a result of even a short-term highly intense physiological stress, while the expression of its matrix ribonucleic acid in leukocytes increased 1.5 times. The individual features determine the response to physiological stress. Probable sources of 70 kDa heat shock protein are discussed. Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 147, No. 3, pp. 335–340, March, 2009     

Serological Investigation of Chlamydia trachomatis Heat Shock Protein 10

The humoral immune response to Chlamydia trachomatis 10-kDa heat shock protein (Chsp10) in populations of Russian and French origin was studied by using a recombinant Chsp10 enzyme-linked immunosorbent assay. A physiological but not a serological correlation of Chsp10 exposure with Chsp60 exposure was observed in the Russian population. In the French population studied, there was a significant association between detection of anti-r-Chsp10 immunoglobulin G (IgG) antibodies and chronic genital tract infections. Chsp10 residues 50 to 67 were found to contain an immunodominant although not universal B epitope. Cross-reactions with Chlamydia pneumoniae or Escherichia coli GroES protein are limited but may occur. Our study suggests that detection of anti-Chsp10 IgG antibodies is associated with chronicity of C. trachomatis genital tract infection and does not parallel that of anti-Chsp60 IgG antibodies.