The Pathology of Cellular Anti-stress Mechanisms: A New Frontier

Exposure to stressors is an omnipresent variable for all living organisms, which have evolved anti-stress mechanisms to deal with the consequences of stress. The chaperoning systems are among these mechanisms, and their central components are the molecular chaperones that play important roles in protein biogenesis. Recent data suggest that failure of the chaperoning systems due to defective chaperones, for example, leads to pathology. Consequently, medical researchers and practitioners must now also consider the chaperoning systems, both as potentially major players in pathogenesis and as diagnostic-prognostic indicators.

[1]  T. Maruyama,et al.  Archaeal peptidyl prolyl cis-trans isomerases (PPIases) update 2004. , 2004, Frontiers in bioscience : a journal and virtual library.

[2]  J. Frydman,et al.  Molecular chaperones and the art of recognizing a lost cause , 2001, Nature Cell Biology.

[3]  Kuo-Hsuan Chang,et al.  Analysis of heat-shock protein 70 gene polymorphisms and the risk of Parkinson’s disease , 2004, Human Genetics.

[4]  A. Tissières,et al.  Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. , 1974, Journal of molecular biology.

[5]  Nicholas J. Cowan,et al.  Functional Overlap between Retinitis Pigmentosa 2 Protein and the Tubulin-specific Chaperone Cofactor C* , 2002, The Journal of Biological Chemistry.

[6]  C. Dobson,et al.  Altered aggregation properties of mutant gamma-crystallins cause inherited cataract. , 2002, The EMBO journal.

[7]  N. Gusev,et al.  Some properties of human small heat shock protein Hsp20 (HspB6). , 2004, European journal of biochemistry.

[8]  S. Lenzner,et al.  Mutations in the X-linked RP2 gene cause intracellular misrouting and loss of the protein. , 2001, Human molecular genetics.

[9]  D. Ferrington,et al.  Modified αA Crystallin in the Retina: Altered Expression and Truncation with Aging† , 2003 .

[10]  T. K. Chowdary,et al.  Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity. , 2004, The Biochemical journal.

[11]  T. Lithgow,et al.  The J‐protein family: modulating protein assembly, disassembly and translocation , 2004, EMBO reports.

[12]  A. Yoshida,et al.  Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. , 1988, Genomics.

[13]  M. Prevost,et al.  A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy , 1998, Nature Genetics.

[14]  J. Leunissen,et al.  The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10. , 2003, Cell stress & chaperones.

[15]  Aaron Ciechanover,et al.  The Ubiquitin Proteasome System in Neurodegenerative Diseases Sometimes the Chicken, Sometimes the Egg , 2003, Neuron.

[16]  M. Rossi,et al.  Reversion of protein aggregation mediated by Sso7d in cell extracts of Sulfolobus solfataricus. , 2004, The Biochemical journal.

[17]  P. Stewart,et al.  Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[18]  C. Dobson,et al.  Altered aggregation properties of mutant γ‐crystallins cause inherited cataract , 2002 .

[19]  Michael Chinkers,et al.  Independent Functions of hsp90 in Neurotransmitter Release and in the Continuous Synaptic Cycling of AMPA Receptors , 2004, The Journal of Neuroscience.

[20]  N. Pfanner,et al.  Mechanisms of Protein Import into Mitochondria , 2003, Current Biology.

[21]  A. Dürr,et al.  Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. , 2002, American journal of human genetics.

[22]  T. Langer,et al.  Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding , 2001, FEBS letters.

[23]  W. Kelley Molecular chaperones: How J domains turn on Hsp70s , 1999, Current Biology.

[24]  A. Ciechanover,et al.  The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. , 2002, Physiological reviews.

[25]  P. Csermely,et al.  Chaperones and aging: role in neurodegeneration and in other civilizational diseases , 2002, Neurochemistry International.

[26]  F. Neidhardt,et al.  The genetics and regulation of heat-shock proteins. , 1984, Annual review of genetics.

[27]  Yoshiyuki Kaneko,et al.  The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s , 2000, Cell stress & chaperones.

[28]  M. Cheetham,et al.  Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. , 1998, Cell stress & chaperones.

[29]  P. Kramer,et al.  Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. , 1998, Human molecular genetics.

[30]  D. Cyr,et al.  From the cradle to the grave: molecular chaperones that may choose between folding and degradation , 2001, EMBO reports.

[31]  B. Ahring,et al.  Stress Genes and Proteins in the Archaea , 1999, Microbiology and Molecular Biology Reviews.

[32]  B. Polla,,et al.  Analysis of hsp70 gene polymorphism in allergic asthma , 1999, Allergy.

[33]  P. Csermely,et al.  Aging and molecular chaperones , 2003, Experimental Gerontology.

[34]  W. Welch Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. , 1992, Physiological reviews.

[35]  R S Reneman,et al.  Heat shock proteins and cardiovascular pathophysiology. , 2001, Physiological reviews.

[36]  M. Figueiredo-Pereira,et al.  A single amino acid substitution in a proteasome subunit triggers aggregation of ubiquitinated proteins in stressed neuronal cells , 2004, Journal of neurochemistry.

[37]  J. Leunissen,et al.  The human genome encodes 10 α-crystallin–related small heat shock proteins: HspB1–10 , 2003 .

[38]  B. Cobb,et al.  Structural and Functional Changes in the αA-Crystallin R116C Mutant in Hereditary Cataracts , 2000 .

[39]  M. Mishina,et al.  Identification of chaperonin CCTγ subunit as a determinant of retinotectal development by whole-genome subtraction cloning from zebrafish no tectal neuron mutant , 2004, Development.

[40]  A. Macario,et al.  Sick chaperones and ageing: a perspective , 2002, Ageing Research Reviews.

[41]  E. Abraham,et al.  Decreased Molecular Chaperone Property of α-Crystallins Due to Posttranslational Modifications , 1995 .

[42]  L. Sistonen,et al.  Roles of the heat shock transcription factors in regulation of the heat shock response and beyond , 2001, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[43]  A. Steven,et al.  Functional Proteolytic Complexes of the Human Mitochondrial ATP-dependent Protease, hClpXP* , 2002, The Journal of Biological Chemistry.

[44]  B. Cobb,et al.  Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts. , 2000, Biochemistry.

[45]  W. Robberecht,et al.  Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy , 2004, Nature Genetics.

[46]  C. Broeckhoven,et al.  Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy , 2004, Nature Genetics.

[47]  J. Dice,et al.  Roles of molecular chaperones in protein degradation , 1996, The Journal of cell biology.

[48]  N. Pfanner,et al.  Pam16 has an essential role in the mitochondrial protein import motor , 2004, Nature Structural &Molecular Biology.

[49]  C. Ross,et al.  Protein aggregation and neurodegenerative disease , 2004, Nature Medicine.

[50]  C. Dobson Protein folding and misfolding , 2003, Nature.

[51]  D. Easton,et al.  The chaperoning properties of mouse grp170, a member of the third family of hsp70 related proteins. , 2003, Biochemistry.

[52]  L. Biesecker,et al.  Unfolding the role of chaperones and chaperonins in human disease. , 2001, Trends in genetics : TIG.

[53]  C. Harrison GrpE, a nucleotide exchange factor for DnaK , 2003, Cell stress & chaperones.

[54]  C. Georgopoulos,et al.  Role of the major heat shock proteins as molecular chaperones. , 1993, Annual review of cell biology.

[55]  B. Bukau,et al.  The heat shock response of Escherichia coli. , 2000, International journal of food microbiology.

[56]  R. Morimoto,et al.  Regulation of the Heat Shock Transcriptional Response: Cross Talk between a Family of Heat Shock Factors, Molecular Chaperones, and Negative Regulators the Heat Shock Factor Family: Redundancy and Specialization , 2022 .

[57]  L. Hightower,et al.  Variation in hsp gene expression and Hsp polymorphism: do they contribute to differential disease susceptibility and stress tolerance? , 1997, Cell stress & chaperones.

[58]  A. Macario,et al.  Heat-shock proteins and molecular chaperones: implications for pathogenesis, diagnostics, and therapeutics , 1995, International journal of clinical & laboratory research.

[59]  N. Cairns,et al.  Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease. , 2001, Biochemical and biophysical research communications.

[60]  C. Kozany,et al.  The J domain–related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase , 2004, Nature Structural &Molecular Biology.

[61]  R. Ellis,et al.  Molecular Chaperones , 1993, Springer Netherlands.

[62]  I. Braakman,et al.  Protein folding and quality control in the endoplasmic reticulum. , 2004, Current opinion in cell biology.

[63]  H. Tokumitsu,et al.  S100A1 Is a Novel Molecular Chaperone and a Member of the Hsp70/Hsp90 Multichaperone Complex* , 2004, Journal of Biological Chemistry.

[64]  P. Muchowski Protein Misfolding, Amyloid Formation, and Neurodegeneration A Critical Role for Molecular Chaperones? , 2002, Neuron.

[65]  E. Conway de Macario,et al.  The molecular chaperone system and other anti-stress mechanisms in archaea. , 2001, Frontiers in bioscience : a journal and virtual library.

[66]  E. Craig,et al.  Getting Newly Synthesized Proteins into Shape , 2000, Cell.

[67]  M. Cheetham,et al.  Unfolding retinal dystrophies: a role for molecular chaperones? , 2001, Trends in molecular medicine.

[68]  M. Mayer,et al.  Molecular chaperones: The busy life of Hsp90 , 1999, Current Biology.

[69]  S. Wiese,et al.  Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease , 2002, The Journal of cell biology.

[70]  S. Alberti,et al.  BAG-1—a nucleotide exchange factor of Hsc70 with multiple cellular functions , 2003, Cell stress & chaperones.

[71]  R. Kopito,et al.  Aggresomes, inclusion bodies and protein aggregation. , 2000, Trends in cell biology.

[72]  K. Nagata,et al.  Prevalence of HSP47 antigen and autoantibodies to HSP47 in the sera of patients with mixed connective tissue disease. , 2003, Biochemical and biophysical research communications.

[73]  Timothy A. Whitehead,et al.  Minimal protein-folding systems in hyperthermophilic archaea , 2004, Nature Reviews Microbiology.

[74]  F. Ritossa A new puffing pattern induced by temperature shock and DNP in drosophila , 1962, Experientia.

[75]  W. Baumeister,et al.  The thermosome: archetype of group II chaperonins , 1998, FEBS letters.

[76]  Peter Tompa,et al.  The role of structural disorder in the function of RNA and protein chaperones , 2004, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[77]  E. Abraham,et al.  Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. , 1995, Biochemical and biophysical research communications.

[78]  P. Csermely,et al.  Chaperone function and chaperone overload in the aged. A preliminary analysis , 2002, Experimental Gerontology.

[79]  P. Csermely,et al.  Chaperone overload is a possible contributor to 'civilization diseases'. , 2001, Trends in genetics : TIG.

[80]  S. Ackerman,et al.  The Molecular Chaperone, Atp12p, from Homo sapiens , 2004, Journal of Biological Chemistry.

[81]  J. Tkach,et al.  Evidence for an Unfolding/Threading Mechanism for Protein Disaggregation by Saccharomyces cerevisiae Hsp104* , 2004, Journal of Biological Chemistry.

[82]  W. D. de Jong,et al.  Truncation of betaA3/A1-crystallin during aging of the bovine lens; possible implications for lens optical quality. , 1999, Experimental Eye Research.

[83]  Jennifer M Harrell,et al.  Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation. , 2004, Brain research. Molecular brain research.

[84]  A. Macario,et al.  Molecular chaperones and age-related degenerative disorders , 2001 .

[85]  E. Conway de Macario,et al.  Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain archaea. , 2004, Frontiers in bioscience : a journal and virtual library.

[86]  E. Salido,et al.  A missense mutation in Tbce causes progressive motor neuronopathy in mice , 2002, Nature Genetics.

[87]  C. Mervis,et al.  Heat shock protein 27 gene: Chromosomal and molecular location and relationship to Williams syndrome , 2003, American journal of medical genetics. Part A.

[88]  P. M. Gopinath,et al.  Novel mutations in the γ-crystallin genes cause autosomal dominant congenital cataracts , 2002 .

[89]  E. Conway de Macario,et al.  Stress and molecular chaperones in disease , 2000, International journal of clinical & laboratory research.

[90]  P. M. Gopinath,et al.  Novel mutations in the gamma-crystallin genes cause autosomal dominant congenital cataracts. , 2002, Journal of medical genetics.

[91]  F. Hartl,et al.  Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein , 2002, Science.

[92]  P. Csermely,et al.  Associate Editor: D. Shugar The 90-kDa Molecular Chaperone Family: Structure, Function, and Clinical Applications. A Comprehensive Review , 1998 .

[93]  A. Ciechanover,et al.  The Ubiquitin System: From Basic Mechanisms to the Patient Bed , 2004, IUBMB life.

[94]  H. Selye A Syndrome produced by Diverse Nocuous Agents , 1936, Nature.

[95]  A. Caplan What is a co-chaperone? , 2003, Cell stress & chaperones.

[96]  F. Narberhaus α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network , 2002, Microbiology and Molecular Biology Reviews.