Protein homeostasis: live long, won't prosper

Protein turnover is an effective way of maintaining a functional proteome, as old and potentially damaged polypeptides are destroyed and replaced by newly synthesized copies. An increasing number of intracellular proteins, however, have been identified that evade this turnover process and instead are maintained over a cell's lifetime. This diverse group of long-lived proteins might be particularly prone to accumulation of damage and thus have a crucial role in the functional deterioration of key regulatory processes during ageing.

[1]  J. Yates,et al.  Extremely Long-Lived Nuclear Pore Proteins in the Rat Brain , 2012, Science.

[2]  A. Spector,et al.  Disulfide-linked high molecular weight protein associated with human cataract. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[3]  I. Braverman,et al.  Studies in cutaneous aging: I. The elastic fiber network. , 1982, The Journal of investigative dermatology.

[4]  M. Kjaer,et al.  Structural, biochemical, cellular, and functional changes in skeletal muscle extracellular matrix with aging , 2011, Scandinavian journal of medicine & science in sports.

[5]  Christine Slingsby,et al.  Ageing and vision: structure, stability and function of lens crystallins. , 2004, Progress in biophysics and molecular biology.

[6]  P A Pevzner,et al.  Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility? , 2006, Journal of proteome research.

[7]  J. Gross,et al.  Mechanism of small heat shock protein function in vivo. A knock-in mouse model demonstrates that the R49C mutation in αA-crystallin enhances protein insolubility and cell death. , 2008, The Journal of Biological Chemistry.

[8]  C. Adams,et al.  Effect of exercise training on passive stiffness in locomotor skeletal muscle: role of extracellular matrix. , 1998, Journal of applied physiology.

[9]  Jason Feser,et al.  Chromatin structure as a mediator of aging , 2011, FEBS letters.

[10]  S. Bassnett Lens organelle degradation. , 2002, Experimental eye research.

[11]  J. Harding,et al.  Free and protein-bound glutathione in normal and cataractous human lenses. , 1970, The Biochemical journal.

[12]  L. Takemoto Quantitation of asparagine-101 deamidation from alpha-A crystallin during aging of the human lens. , 1998, Current eye research.

[13]  L. Gerace,et al.  Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins , 1996, The Journal of cell biology.

[14]  A. Davison,et al.  METABOLISM OF MYELIN LIPIDS: ESTIMATION AND SEPARATION OF BRAIN LIPIDS IN THE DEVELOPING RABBIT , 1959, Journal of neurochemistry.

[15]  M. Rout,et al.  The nuclear pore complex and nuclear transport. , 2010, Cold Spring Harbor perspectives in biology.

[16]  S. Guan,et al.  Analysis of proteome dynamics in the mouse brain , 2010, Proceedings of the National Academy of Sciences.

[17]  J. Horwitz,et al.  Evidence that α-crystallin prevents non-specific protein aggregation in the intact eye lens , 1995 .

[18]  M. Wride Lens fibre cell differentiation and organelle loss: many paths lead to clarity , 2011, Philosophical Transactions of the Royal Society B: Biological Sciences.

[19]  M. Lou,et al.  Effect of age on the thioltransferase (glutaredoxin) and thioredoxin systems in the human lens. , 2010, Investigative ophthalmology & visual science.

[20]  D. Smith,et al.  The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. , 2000, Experimental eye research.

[21]  A. Davison,et al.  METABOLISM OF MYELIN LIPIDS: INCORPORATION OF [3‐14C]SERINE IN BRAIN LIPIDS OF THE DVELOPING RABBIT AND THEIR PERSISTENCE IN THE CENTRAL NERVOUS SYSTEM , 1959 .

[22]  R. Markwald Role of extracellular matrix in morphogenesis. , 1987, Mead Johnson Symposium on Perinatal and Developmental Medicine.

[23]  M. Hetzer,et al.  Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa , 2010, Cell.

[24]  A. Spector,et al.  Absence of low-molecular-weight alpha crystallin in nuclear region of old human lenses. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[25]  R. Morimoto,et al.  The heat shock response: systems biology of proteotoxic stress in aging and disease. , 2011, Cold Spring Harbor symposia on quantitative biology.

[26]  M. Rosbash,et al.  Very long-lived messenger RNA in ovaries of Xenopus laevis. , 1977, Developmental biology.

[27]  E. De Robertis,et al.  Turnover of proteins in subcellular fractions of rat cerebral cortex. , 1971, Brain research.

[28]  Y. Sun,et al.  Post-translational modifications of water-soluble human lens crystallins from young adults. , 1994, The Journal of biological chemistry.

[29]  J. Ellenberg,et al.  Mapping the dynamic organization of the nuclear pore complex inside single living cells , 2004, Nature Cell Biology.

[30]  Paul J Thornalley,et al.  Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins. , 2003, Investigative ophthalmology & visual science.

[31]  M. Rieger,et al.  A Novel Complex of Nucleoporins, Which Includes Sec13p and a Sec13p Homolog, Is Essential for Normal Nuclear Pores , 1996, Cell.

[32]  L. Dure,et al.  Long-Lived Messenger RNA: Evidence from Cotton Seed Germination , 1965, Science.

[33]  J L Bada,et al.  Aspartic acid racemization in tooth enamel from living humans. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[34]  B. Kennedy,et al.  Replicative aging in yeast: the means to the end. , 2008, Annual review of cell and developmental biology.

[35]  S. Bassnett,et al.  Biological glass: structural determinants of eye lens transparency , 2011, Philosophical Transactions of the Royal Society B: Biological Sciences.

[36]  J. Liang,et al.  Destabilization of lens protein conformation by glutathione mixed disulfide. , 1988, Experimental eye research.

[37]  John R Yates,et al.  15N metabolic labeling of mammalian tissue with slow protein turnover. , 2007, Journal of proteome research.

[38]  M. Hetzer,et al.  Shaping the endoplasmic reticulum into the nuclear envelope , 2008, Journal of Cell Science.

[39]  P. Santhoshkumar,et al.  Lens aging: effects of crystallins. , 2009, Biochimica et biophysica acta.

[40]  B. Ortwerth,et al.  Studies on the solubilization of the water-insoluble fraction from human lens and cataract. , 1992, Experimental eye research.

[41]  Jan Ellenberg,et al.  Nuclear envelope breakdown in starfish oocytes proceeds by partial NPC disassembly followed by a rapidly spreading fenestration of nuclear membranes , 2003, The Journal of cell biology.

[42]  Ratan D. Bhardwaj,et al.  Retrospective Birth Dating of Cells in Humans , 2005, Cell.

[43]  André Hoelz,et al.  The structure of the nuclear pore complex. , 2011, Annual review of biochemistry.

[44]  J. Bada,et al.  Aspartic acid racemisation in dentine as a measure of ageing , 1976, Nature.

[45]  J. Woulfe,et al.  Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: a work in progress , 2007, Neuropathology and applied neurobiology.

[46]  E. Schleicher,et al.  Increased accumulation of the glycoxidation product N(epsilon)-(carboxymethyl)lysine in human tissues in diabetes and aging. , 1997, The Journal of clinical investigation.

[47]  Pamela A. Silver,et al.  Engineering synthetic TAL effectors with orthogonal target sites , 2012, Nucleic acids research.

[48]  J A Duerre,et al.  IN VIVO METHYLATION AND TURNOVER OF RAT BRAIN HISTONES , 1974, Journal of neurochemistry.

[49]  M. Mann,et al.  Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly. , 1997, Molecular biology of the cell.

[50]  F. J. Giblin,et al.  Glutathione: a vital lens antioxidant. , 2000, Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics.

[51]  P. Morell,et al.  Turnover of proteins in myelin and myelin-like material of mouse brain. , 1974, Brain research.

[52]  B. Chait,et al.  The molecular architecture of the nuclear pore complex , 2007, Nature.

[53]  A. Dillin,et al.  Aging as an event of proteostasis collapse. , 2011, Cold Spring Harbor perspectives in biology.

[54]  M. Hetzer,et al.  Border control at the nucleus: biogenesis and organization of the nuclear membrane and pore complexes. , 2009, Developmental cell.

[55]  J. Ellenberg,et al.  Remodelling the walls of the nucleus , 2002, Nature Reviews Molecular Cell Biology.

[56]  J. Bada,et al.  Aspartic acid racemisation in the human lens during ageing and in cataract formation , 1977, Nature.

[57]  Samuel Bernard,et al.  Evidence for Cardiomyocyte Renewal in Humans , 2008, Science.

[58]  John B. Shoven,et al.  I , Edinburgh Medical and Surgical Journal.

[59]  R. Gupta,et al.  Deamidation Affects Structural and Functional Properties of Human αA-Crystallin and Its Oligomerization with αB-Crystallin* , 2004, Journal of Biological Chemistry.

[60]  M. Lou Redox regulation in the lens , 2003, Progress in Retinal and Eye Research.

[61]  M. Cuénod,et al.  Metabolism of histones of brain and liver. , 1966, The Journal of biological chemistry.

[62]  V. Monnier,et al.  Aging of Long‐Lived Proteins: Extracellular Matrix (Collagens, Elastins, Proteoglycans) and Lens Crystallins , 2011 .

[63]  K. K. Sharma,et al.  Effect of cross-linking on the chaperone-like function of alpha crystallin. , 1995, Experimental eye research.

[64]  B. Chait,et al.  Proteomic analysis of the mammalian nuclear pore complex , 2002, The Journal of cell biology.

[65]  Michael Unser,et al.  Effect of Aging on Elastin Functionality in Human Cerebral Arteries , 2008, Stroke.

[66]  E. Hartmann,et al.  NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes , 2006, The Journal of cell biology.

[67]  Adelina Rogowska-Wrzesinska,et al.  Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective. , 2011, Journal of proteomics.

[68]  Qikai Xu,et al.  Global Protein Stability Profiling in Mammalian Cells , 2008, Science.

[69]  J. Horwitz Alpha-crystallin can function as a molecular chaperone. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[70]  J A Pierce,et al.  Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon. , 1991, The Journal of clinical investigation.

[71]  E. Cronkite,et al.  Histone turnover within nonproliferating cells. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[72]  M. D'Angelo,et al.  Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells , 2009, Cell.

[73]  K Ribbeck,et al.  Kinetic analysis of translocation through nuclear pore complexes , 2001, The EMBO journal.

[74]  Jean B. Smith,et al.  Modifications of the Water-insoluble Human Lens α-Crystallins , 1996 .

[75]  H. Bloemendal The vertebrate eye lens. , 1977, Science.

[76]  E. O’Shea,et al.  Quantification of protein half-lives in the budding yeast proteome , 2006, Proceedings of the National Academy of Sciences.

[77]  V. Monnier,et al.  Molecular Basis of Arterial Stiffening: Role of Glycation – A Mini-Review , 2012, Gerontology.

[78]  J. Rousseau,et al.  Transcription activator-like effector proteins induce the expression of the frataxin gene. , 2012, Human gene therapy.

[79]  U. Greber,et al.  A major glycoprotein of the nuclear pore complex is a membrane‐spanning polypeptide with a large lumenal domain and a small cytoplasmic tail. , 1990, The EMBO journal.

[80]  J. Bijlsma,et al.  Effect of Collagen Turnover on the Accumulation of Advanced Glycation End Products* , 2000, The Journal of Biological Chemistry.

[81]  Sung Kyu Park,et al.  A quantitative analysis software tool for mass spectrometry–based proteomics , 2008, Nature Methods.

[82]  M. Mann,et al.  Systems-wide proteomic analysis in mammalian cells reveals conserved, functional protein turnover. , 2011, Journal of proteome research.

[83]  L. Ferrucci,et al.  Does accumulation of advanced glycation end products contribute to the aging phenotype? , 2010, The journals of gerontology. Series A, Biological sciences and medical sciences.

[84]  Ralf P. Richter,et al.  FG-Rich Repeats of Nuclear Pore Proteins Form a Three-Dimensional Meshwork with Hydrogel-Like Properties , 2006, Science.

[85]  L. Garcia-Segura,et al.  Distribution of nuclear pores and chromatin organization in neurons and glial cells of the rat cerebellar cortex , 1989, The Journal of comparative neurology.

[86]  J. Graw Genetics of crystallins: cataract and beyond. , 2009, Experimental eye research.

[87]  E. Robertis,et al.  Turnover of proteins in subcellular fractions of rat cerebral cortex. , 1971 .

[88]  D. Görlich,et al.  The Permeability of Reconstituted Nuclear Pores Provides Direct Evidence for the Selective Phase Model , 2012, Cell.

[89]  N. Robinson,et al.  Deamidation of human proteins , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[90]  K. Nasmyth,et al.  Rec8-containing cohesin maintains bivalents without turnover during the growing phase of mouse oocytes. , 2010, Genes & development.

[91]  G. Blobel,et al.  An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region , 1993, The Journal of cell biology.

[92]  T. Trappe,et al.  Collagen, cross-linking, and advanced glycation end products in aging human skeletal muscle. , 2007, Journal of applied physiology.

[93]  Anne-Marie Welling,et al.  Work in progress. , 2012, Nursing standard (Royal College of Nursing (Great Britain) : 1987).