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Study on the chaperone properties of conserved GTPases

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Protein & Cell 2012年第1期3卷 44-50页

作者： Xiang Wang Jiaying Xue Zhe Sun Yan Qin Weimin Gong RNA Lab Institute of BiophysicsChinese Academy of SciencesBeijing 100101China Graduate University of Chinese Academy of Sciences Beijing 100039China

As a large family of hydrolases,GTPases are widespread in cells and play the very important biological function of hydrolyzing GTP into GDP and inorganic phosphate through binding with it.GTPases are involved in cell cycle regulation,protein synthesis,and protein transportation.chaperones can facilitate the folding or refolding of nascent peptides and denatured proteins to their native states.However,chaperones do not occur in the native structures in which they can perform their normal biological functions.In the current study,the chaperone activity of the conserved GTPases of Escherichia coli is tested by the chemical denaturation and chaperone-assisted renaturation of citrate synthase andα-glucosidase.The effects of ribosomes and nucleotides on the chaperone activity are also examined.Our data indicate that these conserved GTPases have chaperone properties,and may be ancestral protein folding factors that have appeared before dedicated chaperones.

关键词： protein folding chaperone conserved GTPase

Progranulin acts as a shared chaperone and regulates multiple lysosomal enzymes

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Genes & Diseases 2017年第3期4卷 125-126页

作者： Jinlong Jian Aubryanna Hettinghouse Chuan-ju Liu Department of Orthopaedic Surgery New York University Medical CenterNew YorkNY10003USA Department of Cell Biology New York University School of MedicineNew YorkNY 10016USA

Multifunctional factor progranulin(PGRN)plays an important role in lysosomes,and its mutations and insufficiency are associated with lysosomal storage diseases,including neuronal ceroid lipofuscinosis and Gaucher disease(GD).The first breakthrough in understanding the molecular mechanisms of PGRN as regulator of lysosomal storage diseases came unexpectedly while investigating the role of PGRN in inflammation.Challenged PGRN null mice displayed typical features of GD.In addition,GRN gene variants were identified in GD patients and the serum levels of PGRN were significantly lower in GD patients.PGRN directly binds to and functions as a chaperone of the lysosomal enzyme β-glucocerebrosidase(GCaase),whose mutations cause GD.In addition,its C-terminus containing granulin E domain,termed Pcgin(PGRN C-terminus for GCase Interaction),is required for the association between PGRN and GCase.The concept that PGRN acts as a chaperone of lysosomal enzymes was further supported and extended by a recent article showing that PGRN acts as a chaperone molecule of lysosomal enzyme cathepsin D(CSTD),and the association between PGRN and CSTD is also mediated by PGRN’s C-terminal granulin E domain.Collectively,these reports suggest that PGRN may act as a shared chaperone and regulates multiple lysosomal enzymes.

关键词： β-glucocerebrosidase Cathepsin D chaperone Lysosomal storage diseases Lysosomal trafficking Progranulin

Differential expression of endoplasmic reticulum molecular chaperone Grp94 in human colorectal carcinoma and promyelocytic leukemia cells

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Chinese Science Bulletin 1997年第19期42卷 1651-1655页

作者： Chen, YH Song, JD Key Laboratory of Cell Biology Ministry of Public Health of China China Medical University Shenyang China

ENDOPLASMIC reticulum (ER) molecular chaperone glucose regulated protein (Grp94 ), a mem-ber of heat shock protein 90 family, is a relatively abundant luminal protein in the ER. Theexpression of the Grp94 gene is markedly increased under many stress conditions. Grp94 isprimarily involved in folding, assembly and translocation of proteins synthesized within

关键词： neoplasms endoplasmic reticulum molecular chaperone Crp94 differential expression.

Mortalin/Hspa9 involvement and therapeutic perspective in Parkinson's disease

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Neural Regeneration Research 2023年第2期18卷 293-298页

作者： Baptiste Texier Morgane Prime Djamaa Atamena Pascale Belenguer Marion Szelechowski Toulouse Institute for Infectious and Inflammatory Diseases(INFINITY) UniversitéToulouseCNRSInsermUPSToulouseFrance Centre de Recherches sur la Cognition Animale(CRCA) Centre de Biologie Intégrative(CBI)Universitéde ToulouseCNRSUPSToulouseFrance

By controlling the proper folding of proteins imported into mitochondria and ensuring crosstalk between the reticulum and mitochondria to modulate intra cellular calcium fluxes.Mortalin is a chaperone protein that plays crucial roles in neuronal homeostasis and activity.Howeve r,its expression and stability are strongly modified in response to cellular stresses,in particular upon alte red oxidative conditions during neurodegeneration.Here,we report and discuss the abundant literature that has highlighted its contribution to the pathophysiology of Parkinson's disease,as well as its therapeutic and prognostic potential in this still incurable pathology.

关键词： chaperone Hspa9 mitochondria Mortalin neurodegeneration oxidative stress Parkinson's disease prognostic and therapeutic potential

Structural insights into the functions of Raf1 and Bsd2 in hexadecameric Rubisco assembly

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Molecular Plant 2023年第12期16卷 1927-1936页

作者： Ran Wang Hui Song Wenjuan Zhang Ning Wang Shijia Zhang Ruiqi Shao Cuimin Liu State Key Laboratory of Plant Cell and Chromosome Engineering Institute of Genetics and Developmental BiologyThe Innovative Academy of Seed DesignChineseAcademyof SciencesBeijing100101China University of Chinese Academy of Sciences Bejing 100101China

Hexadecameric formI Rubisco,which consisting consists of eight large(RbcL)and eight small(RbcS)subunits,is the most abundant enzyme on earth.Extensive efforts to engineer an improved Rubisco to speed up its catalytic efficiency and ultimately increase agricultural productivity.However,difficulties with correct folding and assembly in foreign hosts or in vitro have hampered the genetic manipulation of hexadecameric Rubisco.In this study,we reconstituted Synechococcus sp.Pcc6301 Rubisco in vitro using the chaperonin system and assembly factors from cyanobacteria and Arabidopsis thaliana(At).Rubisco holoenzyme was produced in the presence of cyanobacterial Rubisco accumulation factor 1(Raf1)alone or both AtRaf1 and bundle-sheath defective-2(AtBsd2)from Arabidopsis.RbcL released from GroEL is assembly capable in the presence of ATP,and AtBsd2 functions downstream of AtRaf1.Cryo-EM structures of RbcL8-AtRaf18,RbcL8-AtRaf14-AtBsd2s,and RbcLs revealed that the interactions between RbcL and AtRaf1 are looser than those between prokaryotic RbcL and Raf1,with AtRaf1 tilting 7°farther away from RbcL.AtBsd2 stabilizes the flexible regions of RbcL,including the N and C termini,the 60s loop,and loop 6.Using these data,combined with previous findings,we propose the possible biogenesis pathways of prokaryotic and eukaryotic Rubisco.

关键词： Rubisco chaperone protein folding protein assembly assembly factor

GroESL protects superoxide dismutase (SOD)— Deficient cells against oxidative stress and is a chaperone for SOD

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Health 2013年第10期5卷 1719-1729页

作者： Gary J. Hunter Thérèse Hunter Department of Physiology and Biochemistry University of Malta Msida MSD 2080 Malta Department of Physiology and Biochemistry University of Malta Msida MSD 2080 Malta

Superoxide dismutase (SOD)-deficient Escherichia coli OX326Acells are protected against chemically-induced oxidative stress by expression of the chaperonin GroESL. This protection is equivalent to expression of superoxide dismutase even though GroESL has no inherent SOD activity. Co-overexpression of GroESL and SOD in the same cells results in higher protein yields of SOD and greater metallation of SOD when compared with expression of SOD alone. Greater metallation results in the higher specific activity of SOD that is observed in heat shock, and is not due to increased synthesis of SOD mRNA or protein.

关键词： Superoxide Dismutase chaperone Heat Shock Oxidative Stress

CD8 T cell response in a phase I study of therapeutic vaccination of advanced NSCLC with allogeneic tumor cells secreting endoplasmic reticulum-chaperone gp96-Ig-peptide complexes

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Advances in Lung Cancer 2013年第1期2卷 9-18页

作者： Luis E. Raez Gail R. Walker Paulette Baldie Eva Fisher Jorge E. Gomez Khaled Tolba Edgardo S. Santos Eckhard R. Podack Department of Medicine Division of Hematology/Oncology University of Miami Miller School of Medicine Miami USA Department of Microbiology and Immunology University of Miami Miller School of Medicine Miami USA Sylvester Comprehensive Cancer Center Biostatistics Core Facility University of Miami Miller School of Medicine Miami USA

Antigen containing, allogeneic cells secreting the genetically modified protein and peptide-chaperone gp96-Ig cross, prime and expand antigen specific CD8 T cells with therapeutic antitumor activity in mice. In a first in man phase I study, we now report the results of therapeutic vaccination of non-small cell lung cancer (NSCLC) patients with an established, allogeneic non-small cell lung adenocarcinoma cell line secreting gp96-Ig. Advanced NSCLC-patients stage IIIB or IV of any histological subtype were enrolled and treated with up to 36 vaccinations over the course of 18 weeks. Primary endpoint was safety, secondary endpoints tumor response and overall survival. Measurement of tumor antigen specific CD8 CTL responses is precluded by the lack of known NSCLC associated antigens. Therefore, we measured patient CD8 T cell-IFN-γ responses to allo-antigens of the vaccine cells as surrogate for tumor antigen specific CD8 CTL. In 7 of 18 treated patients tumor growth was stabilized, however none of the 18 patients had an objective tumor response by RECIST criteria. Of 15 patients evaluable for immune response, 11 responded to vaccination with more than twofold increase in CD8-IFN-γ frequency above baseline. These patients had a median survival time of 16.5 months. Four patients who had no CD8 response above base line had survival times from 2.1 to 6.7 months. Our data are consistent with the concept that generation of CD8 CTL by therapeutic vaccination may delay tumor growth and progression and mediate prolonged survival even in the absence of objective tumor responses. Further studies will be required to test this concept and promising result.

关键词： Heat Shock Protein chaperone Gp-96 Non-Small Cell Lung Cancer Gene Transfer Immunotherapy Allogeneic Vaccine Cytotoxic CD8 T Cells

Principles of Quantitative Estimation of the chaperone-Like Activity

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Tsinghua Science and Technology 2002年第4期7卷 331-339页

作者： Boris I.Kurganov Bach Institute of Biochemistry Russian Academy of Sciences Leninsky pr. 33 Moscow 119071 Russia

Molecular chaperones are able to interact with unfolded states of the protein molecule preventing their aggregation and facilitating folding of the polypeptide chain into the native structure. An understanding of the mechanism of protein aggregation is required to estimate the efficiency of action of chaperones in the test systems based on the suppression of aggregation of protein substrates. The kinetic regimes of aggregation of proteins are discussed. The analysis of the aggregation kinetics of proteins shows that after passing the lag phase, aggregation follows, as a rule, first order kinetics. The quantitative characterization methods of the ability of chaperones to prevent aggregation of protein substrates have been elaborated. 

关键词： aggregation chaperone chaperone like activity

Proteomic analysis reveals dysregulated cell sign aling in ejaculated spermatozoa from in fertile men

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Asian Journal of Andrology 2019年第2期21卷 121-130页

作者： Luna Samanta Rakesh Sharma Zhihong Cui Ashok Agarwal American Center for Reproductive Medicine Cleveland ClinicClevelandOH 44195USA Department of Zoology School of Life SciencesRavenshaw UniversityCuttackOdisha 753003India Institute of Toxicology The Third Military Medical UniversityChongqing 400038China

Dysfunctional sperm maturation is the primary reason for the poor sperm motility and morphology in infertile men.Spermatozoa from infertile men were fractioned on three-layer density gradient(80%,60%,and 40%).Fraction 1(Fl)refers to the least mature stage having the lowest den sity,whereas the fraction 4(F4)in eludes the most dense and morphologically mature motile spermatozoa.Fraction 2(F2)and fraction 3(F3)represent the intermediate stages.Proteins were extracted and separated by dimensional gel.Bands were digested with trypsin and analyzed on a LTQ-Orbitrap Elite hybrid mass spectrometer system.Functional annotations of proteins were obtained using bioinformatics tools and pathway databases.A total of 1585 proteins were detected in the four fractions of spermatozoa.A dysregulated protein turnover and protein folding may lead to accumulation of defective proteins or proteins that otherwise would have been eliminated during the process of maturation,resulting in the impairment of sperm fun ction.Aberra nt chaper one expressi on may be a major con tributing factor to the defective sperm function.Androge n receptor was predicted as a transcription regulator in one of the networks and the affected pathways were chaperone-mediated stress response,proteosomal pathway,and sperm function.The down regulation of key pathways and protei ns which compromises the fertilizi ng potential of spermatozoa may provide in sight into the mecha nisms that lead to male infertility.

关键词： androgen receptor chaperone immature sperm infertile men proteasome spermatozoa