砷与金属硫蛋白和热休克蛋白关系原研究进展

砷是国际上公认的一种致癌元素,虽然人们已从天然饮水及职业流行病学资料证实,砷可引起人类皮肤癌、肺癌、膀胱癌等多种肿瘤,但尚无被普遍认可的确切的致癌机制。现在,人们对砷的研究已深入到基因水平,而且已知金属硫蛋白（Ｍｅｔａｌ－ｌｏｔｈｉｏｎｅｉｎ,ＭＴ）和热休克蛋白（Ｈｅａｔ Ｓｈｏｃｋ ｐｒｏｔｅｉｎ,ＨＳＰ）在金属元素代谢中起重要的调控作用,本综述就砷与ＭＴ、ＨＳＰ的关系作如下讨论。１砷与全属硫蛋白（ＭＴ）１．１　ＭＴ的一般特性：ＭＴ家族广泛分布于原核生物、植物和动物体内,动物的ＭＴ基因属多基因类…     

热休克蛋白90家族异常表达与肝细胞癌变关系的研究进展

热休克蛋白（heat shock proteins,HSPs）又称应激蛋白,是机体细胞在一些应激原诱导下激活HSP基因,高效表达的具有高度保守性质的一组蛋白质,与多种蛋白形成复合体,陪伴蛋白分子在细胞内转运、跨膜,参与蛋白的折叠与伸展、多聚复合体的组装,发挥其调节靶蛋白的作用,但又不改变靶蛋白的结构,故被称为＂分子伴侣＂（Molecular Chaperone）.HSP90及gP96在肝癌（HCC）组织中表达异常,抑制细胞凋亡,与肝癌发生、发展及其预后关系密切.     

砷与金属硫蛋白和热休克蛋白关系的研究进展

砷是国际上公认的一种致癌元素,虽然人们已从天然饮水及职业流行病学资料证实,砷可引起人类皮肤癌、肺癌、膀胱癌等多种肿瘤,但尚无被普遍认可的确切的致癌机制.现在,人们对砷的研究已深入到基因水平,而且已知金属硫蛋白(Metal10thionein,MT)和热休克蛋白(Heat Shock protein,HSP)在金属元素代谢中起重要的调控作用,本综述就砷与MT、HSP的关系作如下讨论.     

热休克蛋白与心血管疾病

详尽论述了热休克蛋白与心血管疾病之间的关系。     

热休克蛋白与心肌保护

本文从细胞和分子水平上就热休克蛋白对心肌的保护作用作一介绍。     

热休克蛋白与急性胰腺炎

热休克蛋白 (ｈｅａｔｓｈｏｃｋｐｒｏｔｅｉｎｓ,ＨＳＰｓ)又称热应激蛋白 ,是指细胞被应激诱导所新合成或合成增加的一组蛋白质[1] 。用分子学术语讲 ,是指由启动区具有热休克反应元件 (或称热应激反应元件 ,ｈｅａｔｓｈｏｃｋｅｌｅ ｍｅｎｔ,ＨＳＥ)功能的基因转录、翻译所合成的一组蛋白质[2 ] 。ＨＳＥ是ＨＳＰｓ基因上游的调控元件 ,是由不同数目的核苷酸排列而成[3 ] 。热休克蛋白最初是从受热应激 (从 2 5℃升到30℃ ,30分钟 )的果蝇唾液腺中发现的 ,故取名为热休克蛋白 (或称热应激蛋白 ) [4 ] ,以后发现许多对机体有害的应激可…     

热休克蛋白与肾脏

热休克蛋白与肾脏魏建冬，姚建关键词应激反应；热休克蛋白；应激蛋白机体维护其内环境的稳定是其主要的生物属性。作为其基本功能单位的细胞，在受到外界刺激时，也能产生相应的变化，以适应或对抗这样的刺激。如当温度突然升高时．所有的细胞包括最简单的细菌到高度分化...     

热休克蛋白与结核病关系概述

热休克蛋白是一类广泛存在的具有高度保守性的应激蛋白,有着重要的生理功能。结核病是一种慢性感染性疾病,近年来流行趋势逐渐加剧,严重危害人类的健康。越来越多的研究表明热休克蛋白参与了结核的发病过程,与结核分枝杆菌的致病性、免疫性和结核病的诊断及治疗等方面有着密切的联系。     

热休克蛋白与寄生虫感染

近年来对热休克蛋白的结构和功能的研究有了长足的进展,发现其许多功能,特别是热休克蛋白的“分子伴侣”作用,可作为免疫原诱导免疫应答、参与寄生虫分化等,极地丰富了对其作为生物活性物质参与生命活动的生物学功用的认识。本就热休克蛋白家族及其在寄生虫感染中的作用的新进展作一概述。     

热休克蛋白家族成员及其与恶性肿瘤发生发展的关系

热休克蛋白(HSPs)是机体受各种应激原刺激后产生的一组应激蛋白,又称热应激蛋白.生理状态时HSPs可协助多肽或蛋白质的正确转位、折叠和装配,起"分子伴侣"的作用.近年来,HSPs与肿瘤发生、发展的关系引起了学者们的广泛关注.现将HSPs与在肿瘤发生、发展关系的研究进展综述如下.     

Relationship between Helicobacter pylori, gastric parietal cell antibodies and heat shock proteins

BACKGROUND: The relationship between Helicobacter pylori and autoimmune (type A) gastritis is unclear. Infections may trigger autoimmune phenomena but the underlying mechanisms are unknown. AIM: To determine the relationships between H. pylori infection and gastric parietal cell antibodies (PCA), and PCA and heat shock protein (HSP) antibody. METHODS: Fifty-five serum samples positive for PCA, 22 males and 33 females (median age 61 years, range 29-108 years) were compared with 60 control samples negative for PCA, 24 males and 36 females (median age, 48 years, range 11-91 years). H. pylori infection and HSP65K antibodies were determined by enzyme-linked immunosorbent assay. CagA and VacA status were determined by Western blotting. RESULTS: The prevalence of H. pylori was higher in PCA-positives than controls, 29/55 [53%, 95% confidence interval (CI) 39-66%] versus 13/60 (22%, 95% CI 12-34); P= 0.0009. Age was not a confounding factor. Odds ratio for PCA seropositivity if H. pylori-positive was 4.0 (1.79-9.07), P= 0.003. There was an interaction between age and H. pylori, particularly in younger patients. CagA strains were less common in PCA-positives than controls, 10/29 (35%, 95% CI 19-54) versus 9/13 (69%, 39-91), P< 0.05. HSP65K antibodies were elevated in H. pylori infection but to a similar degree for both PCA-positives and controls. CONCLUSION: H. pylori, particularly CagA-negative strains, are associated with autoimmune gastritis and may be implicated in the pathogenesis of autoimmune (type A) gastritis, particularly in younger persons.     

Relationship between the immune system and heat shock proteins. A literature review

Heat shock proteins (HSP) or stress proteins are produced by prokaryotic and eukaryotic cells in response to a variety of environmental stressors. The heat shock response is one of the most universal reactions known and heat shock proteins are among the most conserved molecules in phylogeny. Recent findings concerning the immune response to heat shock proteins are discussed especially with respect to the role of HSPs postulated in septic disease and inflammation, in antipathogenic immunity and in the induction of autoimmune diseases. Results and speculations considering a relationship between HSPs and gamma/delta T cells or polyreactive antibodies, possibly as part of a phylogenetic old immune system, are critically reviewed.     

Basal and infection-induced levels of heat shock proteins in human aging

Heat shock proteins (Hsp) are ubiquitously expressed proteins, which are highly inducible by a variety of stressful stimuli. As organisms age, various denatured proteins such as proteins modified by oxidation have been detected. Such abnormal proteins might serve as stress signals for the induction of Hsp, which plays indispensable roles in protecting proteins from denaturation. Although it is well known that the heat shock induced expression of Hsp decreases with age, little attention has been given to the unstimulated, basal levels of Hsp. Therefore, a study was performed to examine the expression pattern of various Hsp with aging, under normal physiological conditions in human peripheral blood cells. The basal levels of Hsp32, Hsp70 and Hsp90 increased significantly with age in controls but not patients. Moreover, the levels of Hsp32, Hsp70, Hsp90, but not Hsp27 correlated positively among each other, indicating both common and different regulatory mechanisms. Higher levels of Hsp32, Hsp70 and Hsp90 were noticed in patients with inflammation, a commonly occurring natural stimulant of Hsp production, compared to control subjects. The production of Hsp appeared to be related to the circulating levels of C-reactive protein and cytokines.     

热休克蛋白70系列与应激性溃疡之间的相互关系

生物细胞在受到各种理化因素刺激后,可以产生一系列的应激反应,诱导热休克蛋白(heat shock protein,HSP)表达.在众多的HSP中,HSP70家族是生物进化过程中最为保守也是目前人们研究最多的一组蛋白.应激可以诱导机体胃黏膜的损伤并可以降低胃黏膜的屏障保护作用,进而导致应激性溃疡的产生,同时加速热休克蛋白的合成,而热休克蛋白反过来又可预防应激性溃疡的发生,抑制胃黏膜细胞凋亡,促进胃溃疡的愈合.本文综述了主要的热休克蛋白分子的分类、调节以及在应激性溃疡中的表达和应用,并简要论述了通过诱导热休克蛋白表达而作为胃黏膜保护剂的几种药物.     

Serum heat shock protein and anti-heat shock protein antibody levels in aging

We have previously reported the presence of Hsp60 and Hsp70 in the peripheral circulation of normal individuals. Given that the capacity to generate stress proteins declines with age, this study measured Hsp60 and Hsp70 levels in the sera of 60 individuals aged between 20 and 96 years. Levels of anti-human Hsp60, anti-human Hsp70 and anti-mycobacterial Hsp65 antibody were also measured. Senieur-approximated elderly subjects were well and randomly selected from the Belfast Elderly Longitudinal Free-living Aging STudy (BELFAST). Samples from younger individuals were obtained from the Northern Ireland Blood Transfusion Service. Hsp60, anti-Hsp60, anti-Hsp70 and anti-mycobacterial Hsp65 antibodies were detected in all samples, whereas Hsp70 was detectable in only 46 of the samples analysed (77%). Regression analysis revealed a progressive decline in Hsp60 (759ng/ml < 40 years; 294ng/ml > or = 90 years) and Hsp70 (400ng/ml < 40 years; 20ng/ml > or = 90 years) levels with age whereas no relationship was apparent for anti-Hsp60 and Hsp65 antibody levels. Hsp70 antibody levels tended to increase with age (115U/ml < 40 years; 191U/ml > or = 90 years). This study in Senieur-approximated subjects demonstrates an apparent decrease in Hsp60 and Hsp70 with increasing age that does not appear to be related to anti-heat shock protein antibody status. These findings support in vitro work that demonstrates an age-related reduced ability to respond to stress. Further studies are required to understand the basis for declining serum Hsp60 and Hsp70 levels in aging and to elucidate their origin and role in the maintenance of homeostasis and resistance to environmental challenges.     

Self-degradation of heat shock proteins.

The 70-kDa heat shock protein of Drosophila decays in vivo at a much faster rate than other abundantly labeled proteins. Degradation also occurs in vitro, even during electrophoresis. It appears that this degradation is not mediated by a general protease and that the 70-kDa heat shock protein has a slow proteolytic action upon itself. Heat-induced proteins in CHO cells and a mouse cell line also degrade spontaneously in vitro, as do certain non-heat shock proteins from Drosophila tissues as well as the cell lines.     

人热休克蛋白60及其抗体与冠心病的关系

人热休克蛋白60及其抗体是冠心病的危险因素,与冠心病已建立的其他危险因素也可能存在一定的关系,并且血清中人热休克蛋白60及其抗体水平与冠状动脉病变程度相关。降低血清中人热休克蛋白60及其抗体为冠心病的治疗提供新的手段,并为冠心病患者预后提供新的依据。