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The role of the molecular chaperone heat shock protein A2 （HSPA2） in regulating human sperm-egg recognition

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Asian Journal of Andrology 2015年第4期17卷 568-573页

作者： Brett Nixon Elizabeth G Bromfield Matthew D Dun Kate A Redgrove Eileen A McLaughlin R John Aitken priority Research Centre in Reproductive Science School of Environmental and Life Sciences Discipline of Biological Sciences University of Newcastle CallaghanNSW 2308 Australia Priority Research Centre in Chemical Biology School of Environmental and Life Sciences Discipline of Biological Sciences University of NewcastleCallaghan NSW 2308 Australia Hunter Cancer Research Alliance School of Biomedical Sciences and Pharmacy Faculty of Health and Medicine NSW Australia

One of the most common lesions present in the spermatozoa of human infertility patients is an idiopathic failure of sperm-egg recognition. Although this unique cellular interaction can now be readily by-passed by assisted reproductive strategies such as intracytoplasmic sperm injection （ICSI）, recent large-scale epidemiological studies have encouraged the cautious use of this technology and highlighted the need for further research into the mechanisms responsible for defective sperm-egg recognition. Previous work in this field has established that the sperm domains responsible for oocyte interaction are formed during spermatogenesis prior to being dynamically modified during epididymal maturation and capacitation in female reproductive tract. While the factors responsible for the regulation of these sequential maturational events are undoubtedly complex, emerging research has identified the molecular chaperone, heat shock protein A2 （HSPA2）, as a key regulator of these events in human spermatozoa. HSPA2 is a testis-enriched member of the 70 kDa heat shock protein family that promotes the folding, transport, and assembly of protein complexes and has been positively correlated with in vitro fertilization （IVF） success. Furthermore, reduced expression of HSPA2 from the human sperm proteome leads to an impaired capacity for cumulus matrix dispersal, sperm-egg recognition and fertilization following both IVF and ICSI. In this review, we consider the evidence supporting the role of HSPA2 in sperm function and explore the potential mechanisms by which it is depleted in the spermatozoa of infertile patients. Such information offers novel insights into the molecular mechanisms governing sperm function.

关键词： egg fertilization heat shock protein A2 molecular chaperone sperm sperm-egg interactions

Single-step Purification of molecular chaperone GroEL by Expanded Bed Chromatography

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Chinese Journal of Chemical Engineering 2003年第4期11卷 460-463页

作者：佟晓冬杨征董晓燕孙彦 Department of Biochemical Engineering School of Chemical Engineering and TechnologyTianjin University Tianjin 300072 China

Expanded bed adsorption (EBA) is an integrative downstream processing technique for the purification of biological substances directly from unclarified feedstock. In this study, molecular chaperone GroEL, an important protein folding helper both in vivo and in vitro, was purified by the single-step EBA technique from the unclarified homogenate of recombinant E. coli cells. Compared with packed bed adsorption, the EBA technique provided a single-step approach to yield an electrophoretic purity of GroEL. After the homogenate loading and column washing in the expanded bed mode, the GroEL protein was recovered by stepwise salt-gradient elution in packed-bed or expanded-bed modes, respectively. The expanded-bed elution mode was found as efficient as the packed-bed mode in the purification of GroEL from cell disruptate.

关键词： expanded bed adsorption molecular chaperone GroEL purification

Differential Expression of molecular chaperones in PC12 Cells Treated with PSI

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Chemical Research in Chinese Universities 2010年第4期26卷 596-603页

作者： LIU Tao JIN Ying-hua ZHANG Yu CHANG Ming WANG Dan-ping HU Lin-sen Department of Neurology First Hospital Ministry of Education Jilin University Changehun 130021 P R. China Key Laboratory for molecular Enzymology and Engineering Ministry of Education Jilin University Changehun 130021 P R. China

Parkinson＇s disease（PD） is a common neurodegenerative disorder whose primary pathology features are the degeneration of dopaminergic neurons in the substantia nigra pars compacta（SNc） and the presence of eosinophilic inclusions called Lewy body in the cytoplasm of the remained neurons. Growing evidence suggests that dysfunction of the ubiquitin-proteasome system（UPS） is involved in the etiopathogenesis of PD. In order to investigate the pathogenetic mechanism of ubiquitin-proteasome dysfunction in PD, 2D-differential gel electrophoresis（2D-DIGE） and MALDI-TOF Pro MS were used to determine the proteins, which were differentially expressed, in PC12 cells that had undergone a synthetic proteasomal inhibitor PSI（10 μmol/L） treatment for 24 h. Forty-six protein spots were differentially expressed in response to PSI administration, of which 34 were increased and 12 decreased. Six of these were identified as molecular charperones： endoplasmin precursor（GRP94）, heat shock protein 105（HSP105）, HSC-70-psl, glucose ruglated protein 75（GRP75）, glucose ruglated protein 58（GRP58） and heat shock 27000 protein l（HSP27）. The results suggest that the molecular chaperones play an important role in the PD model induced by proteasomal inhibitor.

关键词： Ubiquitin-proteasome system(UPS) molecular chaperone Parkinson's disease(PD)

Application of heat shock protein expression for detecting natural adaptation and exposure to stress in natural populations

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Current Zoology 2010年第6期56卷 703-713页

作者： Jesper Givskov SφRENSEN National Environmental Research Institute Aarhus UniversityDepartment of Terrestrial Ecology

Heat-shock proteins （HSPs） play an undisputed role for maintaining cellular functioning under environmental challenges and protein denaturing conditions. Compelling evidence points to an evolutionary important role of HSPs and a strict evolutionary control of these proteins as a balance between benefits and costs. While there is a great potential for using HSP expression for detecting natural adaptation and exposure to stress in natural populations, some obstacles and key issues await investigation. From an ecological perspective these key issues needs to be resolved in order to fully appreciate the complex responses and adaptations to stress and to increase our understanding of HSPs and other molecular chaperones for stress adaptation and potential use as biomarkers. Here, the current knowledge and understanding of HSPs is reviewed and a number of key issues including the interpretation of elevated HSP levels, the complications of extrapolating between laboratory and field conditions, the effects of choice of traits and methodology and the larger intra-and extracellular networks of interactions that HSPs participate in are discussed [Current Zoology 56 （6）： 703-713, 2010].

关键词： Biomarker Hsp molecular chaperone Thermal adaptation Thermal stress

Effect of chaperone–client interaction strength on Hsp70-mediated protein folding

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Chinese Physics B 2023年第11期32卷 635-641页

作者：邹禄军陆伽俊徐秀莲 Department of Physics National Laboratory of Solid State MicrostructureNanjing UniversityNanjing 210093China School of Physics Science and Technology Yangzhou UniversityYangzhou 225002China

Protein folding in crowding cellular environment often relies on the assistance of various chaperones. Hsp70 is one of the most ubiquitous chaperones in cells. Previous studies showed that the chaperone–client interactions at the open state tend to remodel the protein folding energy landscape and direct the protein folding as a foldase. In this work, we further investigate how the chaperone–client interaction strength modulates the foldase function of Hsp70 by using molecular simulations. The results showed that the time of substrate folding(including the whole folding step and substrate release step) has a non-monotonic dependence on the interaction strength. With the increasing of the chaperone–client interaction strength, the folding time decreases first, and then increases. More detailed analysis showed that when the chaperone–client interaction is too strong, even small number of chaperones–client contacts can maintain the substrate bound with the chaperone. The sampling of the transient chaperones–client complex with sparse inter-molecule contacts makes the client protein have chance to access the misfolded state even it is bound with chaperone. The current results suggest that the interaction strength is an important factor controlling the Hsp70 chaperoning function.

关键词： protein folding molecular chaperone molecular dynamics Hsp70

Heat Shock Protein 90 Indirectly Regulates ERK Activity by Affecting Raf Protein Metabolism

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Acta Biochimica et Biophysica Sinica 2005年第7期37卷 501-505页

作者： Fei DOU Liu-Di YUAN Jing-Jing ZHU Department of Genetics and Development Biology,Southeast University Medical School,Nanjing 210009,China Department of Genetics and Development Biology Southeast University Medical SchoolNanjing 210009 China

Extracellular signal-regulated protein kinase (ERK) has been implicated in the pathogenesis ofseveral nerve system *** more and more kinases have been discovered to be the client proteins ofthe molecular chaperone Hsp90,the use of Hsp90 inhibitors to reduce abnormal kinase activity is a newtreatment strategy for nerve system *** study investigated the regulation of the ERK pathway *** showed that Hsp90 inhibitors reduce ERK phosphorylation without affecting the total ERKprotein *** investigation showed that Raf,the UPstream kinase in the Ras-Raf-MEK-ERK pathway,forms a complex with Hsp90 and *** cells with Hsp90 inhibitors facilitates Raf degradation,thereby down-regulating the activity of ERK.

关键词： molecular chaperone phosphorylation Hsp90 extracellular signal-regulated protein kinase (ERK) Raf tau

Hsp90 at the crossroads of genetics and epigenetics

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Cell Research 2006年第9期16卷 10+743-749页

作者： KeithSKWong WalidAHoury Department of Biochemistry University of Toronto1 King's College CircleMedical Sciences BuildingTorontoOntarioM5S 1A8 Canada

Hsp90 is a specialized molecular chaperone that is capable of buffering the expression of abnormal ***-bition of Hsp90 activity results in the expression of these phenotypes that are otherwise *** of offspringfrom the crossing of affected progenies results in inheritance and enrichment of these phenotypes,which can becomeindependent of their original *** current combined evidence favours a model involving the interplay betweengenetics and *** recent proteomics efforts to characterize the Hsp90 interaction networks provide further cluesinto the molecular mechanisms behind this complex *** review summarizes the most recent experimentalobservations and briefly discusses the genetic and epigenetic views used in explaining the different observations.

关键词： Hsp90 molecular chaperone genetics epigenetics

Metabolism of minor isoforms of prion proteins Cytosolic prion protein and transmembrane prion protein

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Neural Regeneration Research 2013年第30期8卷 2868-2878页

作者： Zhiqi Song Deming Zhao Lifeng Yang State Key Laboratory for Agrobiotechnology National Animal Transmissible Spongiform Encephalopathy Laboratory College of Veterinary Medicine China Agricultural University

Transmissible spongiform encephalopathy or prion disease is triggered by the conversion from cellular prion protein to pathogenic prion protein. Growing evidence has concentrated on prion protein configuration changes and their correlation with prion disease transmissibility and patho- genicity. In vivo and in vitro studies have shown that several cytosolic forms of prion protein with specific topological structure can destroy intracellular stability and contribute to prion protein pathogenicity. In this study, the latest molecular chaperone system associated with endoplasmic re- ticulum-associated protein degradation, the endoplasmic reticulum resident protein quality-control system and the ubiquitination proteasome system, is outlined. The molecular chaperone system directly correlates with the prion protein degradation pathway. Understanding the molecular mechanisms will help provide a fascinating avenue for further investigations on prion disease treatment and prion protein-induced neurodegenerative diseases.

关键词： neural regeneration neurodegeneration prion protein cytosolic form of prion protein transmem-brane form of prion protein metabolism protein degeneration ubiquitination molecular chaperone molecular mechanism neuroregeneration

Fluorogenic sensing of amorphous aggregates,amyloid fibers,and chaperone activity via a near-infrared aggregation-induced emission-active probe

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Aggregate

Aggregate 2024年第1期5卷 309-320页

作者： Wei He Yuanyuan Yang Yuhui Qian Zhuoyi Chen Yongxin Zheng Wenping Zhao Chenxu Yan Zhiqian Guo Shu Quan State Key Laboratory of Bioreactor Engineering Shanghai Collaborative Innovation Center for Biomanufacturing(SCICB)East China University of Science and TechnologyShanghaiChina Key Laboratory for Advanced Materials and Joint International Research Laboratory of Precision Chemistry and molecular Engineering Shanghai Key Laboratory of Functional Materials ChemistryFrontiers Science Center for Materiobiology and Dynamic ChemistryInstitute of Fine ChemicalsSchool of Chemistry and Molecular EngineeringEast China University of Science and TechnologyShanghaiChina Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism East China University of Science and TechnologyShanghaiChina

The presence of protein aggregates in numerous human diseases underscores the significance of detecting these aggregates to comprehend disease mechanisms and develop novel therapeutic approaches for combating these *** the development of various biosensors and fluorescent probes that selectively target amyloid fibers or amorphous aggregates,there is still a lack of tools capable of simultaneously detecting both types of ***,we demonstrate the quantitative discernment of amorphous aggregates by QM-FN-SO3,an aggregationinduced emission(AIE)probe initially designed for detecting amyloid *** probe easily penetrates the membranes of the widely-used prokaryotic model organism Escherichia coli,enabling the visualization of both amorphous aggregates and amyloid fibers through near-infrared ***,the probe exhibits sensitivity in distinguishing the varying aggregation propensities of proteins,regardless of whether they form amorphous aggregates or amyloid fibers in *** properties contribute to the successful application of the QM-FN-SO3 probe in the subsequent investigation of the antiaggregation activities of two outer membrane protein(OMP)chaperones,both in vitro and in their physiological ***,our work introduces a near-infrared fluorescent chemical probe that can quantitatively detect amyloid fibers and amorphous aggregates with high sensitivity in vitro and in ***,it demonstrates the applicability of the probe in chaperone biology and its potential as a high-throughput screening tool for protein aggregation inhibitors and folding factors.

关键词： aggregation-induced emission fluorescence molecular chaperone protein aggregation