Abstract
The importance of small heat shock protein HSP in geroscience is increasing. We believe that research progress from life science should contribute to well-being. Molecular chaperone studies are considered superior when performed on model substrates and model animals. However, by itself, concrete measures for extending the healthy life of human beings are not provided. It is important to analyze the cell-animal-human results, interpret the relationship, and promote comprehensively studied HSP research. αB-crystallin (CRYAB) was identified for key molecule to explain the mechanism of exercise adaptation of slow-twitch muscle for a long ago. It is only human beings that stand up against gravity and move all day in their standing position. With CRYAB and tubulin/microtubule as a key word, we will introduce the principle of clarifying not only cells but also how to control the human body. Mechanistically fiber structure produced after protein assembly has not only multifunction but also is available as materials to make “body” and can sustain body weight by tension development at both micro- and macro-levels. This links cell’s autonomous regulating ability and human will to keep standing. This manuscript may contribute to develop a new direction of HSP Geroscience research proposing real program to healthy aging and mature human world.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsAbbreviations
- CRYAB:
-
αB-crystallin
- ECM:
-
Extracellular matrix
- FRAP:
-
Fluorescence recovery after photobleaching
- FRET:
-
Fluorescence resonance energy transfer
- Hsp:
-
Heat shock protein
- HSP:
-
Heat shock protein family
- MAP:
-
Microtubule-associated protein
- MT:
-
Microtubule
References
Ahrman, E., Lambert, W., Aquilina, J. A., Robinson, C. V., & Emanuelsson, C. S. (2007). Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthase. Protein Science, 16, 1464–1478. https://doi.org/10.1110/ps.072831607
Arac, A., Brownell, S. E., Rothbard, J. B., Chen, C., Ko, R. M., Pereira, M. P., Albers, G. W., Steinman, L., & Steinberg, G. K. (2011). Systemic augmentation of alphaB-crystallin provides therapeutic benefit twelve hours post-stroke onset via immune modulation. Proceedings of the National Academy of Sciences of the United States of America, 108, 13287–13292. https://doi.org/10.1073/pnas.1107368108
Arai, H., & Atomi, Y. (1997). Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation. Cell Structure and Function, 22, 539–544.
Arany, Z., Wagner, B. K., Ma, Y., Chinsomboon, J., Laznik, D., & Spiegelman, B. M. (2008). Gene expression-based screening identifies microtubule inhibitors as inducers of PGC-1alpha and oxidative phosphorylation. Proceedings of the National Academy of Sciences of the United States of America, 105, 4721–4726. https://doi.org/10.1073/pnas.0800979105
Arrigo, A. P. (2013). Human small heat shock proteins: Protein interactomes of homo- and hetero-oligomeric complexes: An update. FEBS Letters, 587, 1959–1969. https://doi.org/10.1016/j.febslet.2013.05.011
Atomi, Y. (2012). Innovative science and education for understanding “Life” systems. Trends In The Sciences, 17(6), 86–93. https://doi.org/10.5363/tits.17.6_86
Atomi, Y. (2015). Gravitational effects on human physiology. Sub-Cellular Biochemistry, 72, 627–659. https://doi.org/10.1007/978-94-017-9918-8_29
Atomi, Y., & Miyashita, M. (1974). Maximal aerobic power of Japanese active and sedentary adult females of different ages (20 to 62 years). Medicine and Science in Sports, 6, 223–225.
Atomi, Y., & Miyashita, M. (1980). Effect of training intensity in adult females. European Journal of Applied Physiology and Occupational Physiology, 44, 109–116.
Atomi, Y., Iwaoka, K., Hatta, H., Miyashita, M., & Yamamoto, Y. (1986). Daily physical activity levels in preadolescent boys related to VO2max and lactate threshold. European Journal of Applied Physiology and Occupational Physiology, 55, 156–161.
Atomi, Y., Fukunaga, T., Hatta, H., & Yamamoto, Y. (1987). elationship between lactate threshold during running and relative gastrocnemius area. Journal of Applied Physiology, 1985(63), 2343–2347.
Atomi, Y., Yamada, S., & Hong, Y.-M. (1990). Dynamic expression of αB-Crystallin in skeletal muscle Effects of Unweighting, Passive Stretch and Denervation. Proceedings of the Japan Academy, Series B, 66, 203–208. https://doi.org/10.2183/pjab.66.203
Atomi, Y., Yamada, S., & Nishida, T. (1991a). Early changes of alpha B-crystallin mRNA in rat skeletal muscle to mechanical tension and denervation. Biochemical and Biophysical Research Communications, 181, 1323–1330.
Atomi, Y., Yamada, S., Strohman, R., & Nonomura, Y. (1991b). Alpha B-crystallin in skeletal muscle: Purification and localization. Journal of Biochemistry, 110, 812–822.
Atomi, Y., Toro, K., Masuda, T., & Hatta, H. (2000). Fiber-type-specific alphaB-crystallin distribution and its shifts with T(3) and PTU treatments in rat hindlimb muscles. Journal of Applied Physiology, 1985(88), 1355–1364.
Atomi, T., Noriuchi, M., Oba, K., Atomi, Y., & Kikuchi, Y. (2014). Self-recognition of one’s own fall recruits the genuine bodily crisis-related brain activity. PLoS One, 9, e115303. https://doi.org/10.1371/journal.pone.0115303
Bagneris, C., Bateman, O. A., Naylor, C. E., Cronin, N., Boelens, W. C., Keep, N. H., & Slingsby, C. (2009). Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. Journal of Molecular Biology, 392, 1242–1252. https://doi.org/10.1016/j.jmb.2009.07.069.
Barnes, S., & Quinlan, R. A. (2017). Small molecules, both dietary and endogenous, influence the onset of lens cataracts. Experimental Eye Research, 156, 87–94. https://doi.org/10.1016/j.exer.2016.03.024
Bianconi, E., Piovesan, A., Facchin, F., Beraudi, A., Casadei, R., Frabetti, F., Vitale, L., Pelleri, M. C., Tassani, S., Piva, F., Perez-Amodio, S., Strippoli, P., & Canaider, S. (2013). An estimation of the number of cells in the human body. Annals of Human Biology, 40, 463–471. https://doi.org/10.3109/03014460.2013.807878
Brady, J. P., Garland, D. L., Green, D. E., Tamm, E. R., Giblin, F. J., & Wawrousek, E. F. (2001). AlphaB-crystallin in lens development and muscle integrity: A gene knockout approach. Investigative Ophthalmology & Visual Science, 42, 2924–2934.
Bramble, D. M., & Lieberman, D. E. (2004). Endurance running and the evolution of homo. Nature, 432, 345–352. https://doi.org/10.1038/nature03052
Bullard, B., Ferguson, C., Minajeva, A., Leake, M. C., Gautel, M., Labeit, D., Ding, L., Labeit, S., Horwitz, J., Leonard, K. R., & Linke, W. A. (2004). Association of the chaperone alphaB-crystallin with titin in heart muscle. The Journal of Biological Chemistry, 279, 7917–7924. https://doi.org/10.1074/jbc.M307473200
Courtine, G., Song, B., Roy, R. R., Zhong, H., Herrmann, J. E., Ao, Y., Qi, J., Edgerton, V. R., & Sofroniew, M. V. (2008). Recovery of supraspinal control of stepping via indirect propriospinal relay connections after spinal cord injury. Nature Medicine, 14, 69–74. https://doi.org/10.1038/nm1682
Datskevich, P. N., Mymrikov, E. V., & Gusev, N. B. (2012). Utilization of fluorescent chimeras for investigation of heterooligomeric complexes formed by human small heat shock proteins. Biochimie, 94, 1794–1804. https://doi.org/10.1016/j.biochi.2012.04.012
de Jong, W. W., Leunissen, J. A., & Voorter, C. E. (1993). Evolution of the alpha-crystallin/small heat-shock protein family. Molecular Biology and Evolution, 10, 103–126.
Delbecq, S. P., Jehle, S., & Klevit, R. (2012). Binding determinants of the small heat shock protein, alphaB-crystallin: Recognition of the ‘IxI’ motif. The EMBO Journal, 31, 4587–4594. https://doi.org/10.1038/emboj.2012.318
Duennwald, M. L., Echeverria, A., & Shorter, J. (2012). Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biology, 10, e1001346. https://doi.org/10.1371/journal.pbio.1001346
Eyles, S. J., & Gierasch, L. M. (2010). Nature’s molecular sponges: Small heat shock proteins grow into their chaperone roles. Proceedings of the National Academy of Sciences of the United States of America, 107, 2727–2728. https://doi.org/10.1073/pnas.0915160107
Fujita, Y., Ohto, E., Katayama, E., & Atomi, Y. (2004). alphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly. Journal of Cell Science, 117, 1719–1726. https://doi.org/10.1242/jcs.01021
Funatsu, T., Harada, Y., Tokunaga, M., Saito, K., & Yanagida, T. (1995). Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature, 374, 555–559. https://doi.org/10.1038/374555a0
Goodsell, D. S. (1991). Inside a living cell. Trends in Biochemical Sciences, 16, 203–206.
Gundersen, G. G., & Cook, T. A. (1999). Microtubules and signal transduction. Current Opinion in Cell Biology, 11, 81–94.
Haslbeck, M., & Vierling, E. (2015). A first line of stress defense: Small heat shock proteins and their function in protein homeostasis. Journal of Molecular Biology, 427, 1537–1548. https://doi.org/10.1016/j.jmb.2015.02.002
Haslbeck, M., Braun, N., Stromer, T., Richter, B., Model, N., Weinkauf, S., & Buchner, J. (2004). Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. The EMBO Journal, 23, 638–649. https://doi.org/10.1038/sj.emboj.7600080
Hatta, H., Atomi, Y., Yamamoto, Y., Shinohara, S., & Yamada, S. (1989). Incorporation of blood lactate and glucose into tissues in rats after short-term strenuous exercise. International Journal of Sports Medicine, 10, 275–278. https://doi.org/10.1055/s-2007-1024915
Hayashi, I., Vuori, K., & Liddington, R. C. (2002). The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nature Structural Biology, 9, 101–106. https://doi.org/10.1038/nsb755
Hirokawa, N. (1998). Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science, 279, 519–526.
Hochberg, G. K., Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M. R., Collier, M. P., Stroud, J., Carver, J. A., Baldwin, A. J., Robinson, C. V., Eisenberg, D. S., Benesch, J. L., & Laganowsky, A. (2014). The structured core domain of alphaB-crystallin can prevent amyloid fibrillation and associated toxicity. Proceedings of the National Academy of Sciences of the United States of America, 111, E1562–E1570. https://doi.org/10.1073/pnas.1322673111
Houck, S. A., & Clark, J. I. (2010). Dynamic subunit exchange and the regulation of microtubule assembly by the stress response protein human alphaB crystallin. PLoS One, 5, e11795. https://doi.org/10.1371/journal.pone.0011795
Hsu, A. L., Murphy, C. T., & Kenyon, C. (2003). Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science, 300, 1142–1145. https://doi.org/10.1126/science.1083701
Huang, Y., Wang, Z., Liu, Y., Xiong, H., Zhao, Y., Wu, L., Yuan, C., Wang, L., Hou, Y., Yu, G., Huang, Z., Xu, C., Chen, Q., & Wang, Q. K. (2016). alphaB-Crystallin interacts with Nav1.5 and regulates ubiquitination and internalization of cell surface Nav1.5. The Journal of Biological Chemistry, 291, 11030–11041. https://doi.org/10.1074/jbc.M115.695080
Ikeda, N., Saito, E., Kondo, N., Inoue, M., Ikeda, S., Satoh, T., Wada, K., Stickley, A., Katanoda, K., Mizoue, T., Noda, M., Iso, H., Fujino, Y., Sobue, T., Tsugane, S., Naghavi, M., Ezzati, M., & Shibuya, K. (2011). What has made the population of Japan healthy? Lancet, 378, 1094–1105. https://doi.org/10.1016/S0140-6736(11)61055-6
Ishihara, K., Nguyen, P. A., Groen, A. C., Field, C. M., & Mitchison, T. J. (2014). Microtubule nucleation remote from centrosomes may explain how asters span large cells. Proceedings of the National Academy of Sciences of the United States of America, 111, 17715–17722. https://doi.org/10.1073/pnas.1418796111
Ito, H., Okamoto, K., Nakayama, H., Isobe, T., & Kato, K. (1997). Phosphorylation of alphaB-crystallin in response to various types of stress. The Journal of Biological Chemistry, 272, 29934–29941.
Jaya, N., Garcia, V., & Vierling, E. (2009). Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proceedings of the National Academy of Sciences of the United States of America, 106, 15604–15609. https://doi.org/10.1073/pnas.0902177106
Jee, H., Sakurai, T., Kawada, S., Ishii, N., & Atomi, Y. (2009). Significant roles of microtubules in mature striated muscle deduced from the correlation between tubulin and its molecular chaperone alphaB-crystallin in rat muscles. The Journal of Physiological Sciences, 59, 149–155. https://doi.org/10.1007/s12576-008-0014-6
Jehle, S., Rajagopal, P., Bardiaux, B., Markovic, S., Kuhne, R., Stout, J. R., Higman, V. A., Klevit, R. E., van Rossum, B. J., & Oschkinat, H. (2010). Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Nature Structural & Molecular Biology, 17, 1037–1042. https://doi.org/10.1038/nsmb.1891
Kampinga, H. H., Hageman, J., Vos, M. J., Kubota, H., Tanguay, R. M., Bruford, E. A., Cheetham, M. E., Chen, B., & Hightower, L. E. (2009). Guidelines for the nomenclature of the human heat shock proteins. Cell Stress & Chaperones, 14, 105–111. https://doi.org/10.1007/s12192-008-0068-7
Kappe, G., Leunissen, J. A., & de Jong, W. W. (2002). Evolution and diversity of prokaryotic small heat shock proteins. Progress in Molecular and Subcellular Biology, 28, 1–17.
Kato, K., Goto, S., Inaguma, Y., Hasegawa, K., Morishita, R., & Asano, T. (1994). Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin. The Journal of Biological Chemistry, 269, 15302–15309.
Kennedy, B. K., Berger, S. L., Brunet, A., Campisi, J., Cuervo, A. M., Epel, E. S., Franceschi, C., Lithgow, G. J., Morimoto, R. I., Pessin, J. E., Rando, T. A., Richardson, A., Schadt, E. E., Wyss-Coray, T., & Sierra, F. (2014). Geroscience: Linking aging to chronic disease. Cell, 159, 709–713. https://doi.org/10.1016/j.cell.2014.10.039
Kenyon, C., Chang, J., Gensch, E., Rudner, A., & Tabtiang, R. (1993). A C. Elegans mutant that lives twice as long as wild type. Nature, 366, 461–464. https://doi.org/10.1038/366461a0
Kim, K. K., Kim, R., & Kim, S. H. (1998). Crystal structure of a small heat-shock protein. Nature, 394, 595–599. https://doi.org/10.1038/29106
Kim, S. G., Akaike, T., Sasagaw, T., Atomi, Y., & Kurosawa, H. (2002). Gene expression of type I and type III collagen by mechanical stretch in anterior cruciate ligament cells. Cell Structure and Function, 27, 139–144.
Koh, T. J., & Escobedo, J. (2004). Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions. American Journal of Physiology. Cell Physiology, 286, C713–C722. https://doi.org/10.1152/ajpcell.00341.2003
Kriehuber, T., Rattei, T., Weinmaier, T., Bepperling, A., Haslbeck, M., & Buchner, J. (2010). Independent evolution of the core domain and its flanking sequences in small heat shock proteins. The FASEB Journal, 24, 3633–3642. https://doi.org/10.1096/fj.10-156992
Kuipers, H. F., Yoon, J., van Horssen, J., Han, M. H., Bollyky, P. L., Palmer, T. D., & Steinman, L. (2017). Phosphorylation of alphaB-crystallin supports reactive astrogliosis in demyelination. Proceedings of the National Academy of Sciences of the United States of America, 114, E1745–E1754. https://doi.org/10.1073/pnas.1621314114
Laganowsky, A., Benesch, J. L., Landau, M., Ding, L., Sawaya, M. R., Cascio, D., Huang, Q., Robinson, C. V., Horwitz, J., & Eisenberg, D. (2010). Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Science, 19, 1031–1043. https://doi.org/10.1002/pro.380
Liu, Y., & Steinacker, J. M. (2001). Changes in skeletal muscle heat shock proteins: Pathological significance. Frontiers in Bioscience, 6, D12–D25.
Locke, M., & Noble, E. G. (1995). Stress proteins: The exercise response. Canadian Journal of Applied Physiology, 20, 155–167.
Mainz, A., Peschek, J., Stavropoulou, M., Back, K. C., Bardiaux, B., Asami, S., Prade, E., Peters, C., Weinkauf, S., Buchner, J., & Reif, B. (2015). The chaperone alphaB-crystallin uses different interfaces to capture an amorphous and an amyloid client. Nature Structural & Molecular Biology, 22, 898–905. https://doi.org/10.1038/nsmb.3108
Manenti, S., Dunia, I., & Benedetti, E. L. (1990). Fatty acid acylation of lens fiber plasma membrane proteins. MP26 and alpha-crystallin are palmitoylated. FEBS Letters, 262, 356–358.
Maruyama, K. (1976). Connectin, an elastic protein from myofibrils. Journal of Biochemistry, 80, 405–407.
McGreal, R. S., Kantorow, W. L., Chauss, D. C., Wei, J., Brennan, L. A., & Kantorow, M. (2012). AlphaB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells. Biochimica et Biophysica Acta, 1820, 921–930. https://doi.org/10.1016/j.bbagen.2012.04.004
McHaourab, H. S., Godar, J. A., & Stewart, P. L. (2009). Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins. Biochemistry, 48, 3828–3837. https://doi.org/10.1021/bi900212j
Mitchison, T., & Kirschner, M. (1984). Dynamic instability of microtubule growth. Nature, 312, 237–242.
Mitchison, T. J., & Kirschner, M. W. (1985). Properties of the kinetochore in vitro. II. Microtubule capture and ATP-dependent translocation. The Journal of Cell Biology, 101, 766–777.
Morimoto, R. I. (2008). Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes & Development, 22, 1427–1438. https://doi.org/10.1101/gad.1657108
Morner, C. T. (1894). Untersuchung der Proteinsubstanzen in den lichtbrechenden Medien des Auges (Examination of the protein-substances in the refractory media of the eye). Hoppe-Seyler’s Zeitschrift für Physiologische Chemie, 18, 61–106.
Morrow, G., & Tanguay, R. M. (2012). Small heat shock protein expression and functions during development. The International Journal of Biochemistry & Cell Biology, 44, 1613–1621. https://doi.org/10.1016/j.biocel.2012.03.009
Mymrikov, E. V., Daake, M., Richter, B., Haslbeck, M., & Buchner, J. (2017). The chaperone activity and substrate Spectrum of human small heat shock proteins. The Journal of Biological Chemistry, 292, 672–684. https://doi.org/10.1074/jbc.M116.760413
Ohkawa, T., Atomi, T., Hasegawa, K., & Atomi, Y. (2017). The free moment is associated with torsion between the pelvis and the foot during gait. Gait & Posture, 58, 415–420. https://doi.org/10.1016/j.gaitpost.2017.09.002
Ohto-Fujita, E., Fujita, Y., & Atomi, Y. (2007). Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregation. Cell Stress & Chaperones, 12, 163–171.
Patel, S., Vierling, E., & Tama, F. (2014). Replica exchange molecular dynamics simulations provide insight into substrate recognition by small heat shock proteins. Biophysical Journal, 106, 2644–2655. https://doi.org/10.1016/j.bpj.2014.04.048
Pereira, M. B., Santos, A. M., Goncalves, D. C., Cardoso, A. C., Consonni, S. R., Gozzo, F. C., Oliveira, P. S., Pereira, A. H., Figueiredo, A. R., Tiroli-Cepeda, A. O., Ramos, C. H., de Thomaz, A. A., Cesar, C. L., & Franchini, K. G. (2014). AlphaB-crystallin interacts with and prevents stress-activated proteolysis of focal adhesion kinase by calpain in cardiomyocytes. Nature Communications, 5, 5159. https://doi.org/10.1038/ncomms6159
Prosser, S. L., & Pelletier, L. (2017). Mitotic spindle assembly in animal cells: A fine balancing act. Nature Reviews. Molecular Cell Biology, 18, 187–201. https://doi.org/10.1038/nrm.2016.162
Quinlan, R. (2002). Cytoskeletal competence requires protein chaperones. In M. W. E. G. Arrigo (Ed.), Small Stress Proteins (pp. 219–233). AP.
Ralston, E., Lu, Z., & Ploug, T. (1999). The organization of the Golgi complex and microtubules in skeletal muscle is fiber type-dependent. The Journal of Neuroscience, 19, 10694–10705.
Raman, B., Ban, T., Sakai, M., Pasta, S. Y., Ramakrishna, T., Naiki, H., Goto, Y., & Rao Ch, M. (2005). AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin. The Biochemical Journal, 392, 573–581. https://doi.org/10.1042/BJ20050339
Ray, P. S., Martin, J. L., Swanson, E. A., Otani, H., Dillmann, W. H., & Das, D. K. (2001). Transgene overexpression of alphaB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion. The FASEB Journal, 15, 393–402. https://doi.org/10.1096/fj.00-0199com
Ruoslahti, E. (1997). Stretching is good for a cell. Science, 276, 1345–1346.
Sakurai, T., Fujita, Y., Ohto, E., Oguro, A., & Atomi, Y. (2005). The decrease of the cytoskeleton tubulin follows the decrease of the associating molecular chaperone alphaB-crystallin in unloaded soleus muscle atrophy without stretch. The FASEB Journal, 19, 1199–1201. https://doi.org/10.1096/fj.04-3060fje
Seevaratnam, R., Patel, B. P., & Hamadeh, M. J. (2009). Comparison of total protein concentration in skeletal muscle as measured by the Bradford and Lowry assays. Journal of Biochemistry, 145, 791–797. https://doi.org/10.1093/jb/mvp037
Sharples, A. P., Hughes, D. C., Deane, C. S., Saini, A., Selman, C., & Stewart, C. E. (2015). Longevity and skeletal muscle mass: The role of IGF signalling, the sirtuins, dietary restriction and protein intake. Aging Cell, 14, 511–523. https://doi.org/10.1111/acel.12342
Shay, J. W., & Wright, W. E. (2000). Hayflick, his limit, and cellular ageing. Nature Reviews. Molecular Cell Biology, 1, 72–76. https://doi.org/10.1038/35036093
Shigematsu, Y., Okamoto, H., Ichikawa, K., & Matsumoto, G. (1999). Temporal event association and output-dependent learning: A proposed scheme of neural molecular connections. Journal of Advanced Computational Intelligence, 3, 234–244. https://doi.org/10.20965/jaciii.1999.p0234
Shimizu, M., Tanaka, M., & Atomi, Y. (2016). Small heat shock protein alphaB-Crystallin controls shape and adhesion of glioma and myoblast cells in the absence of stress. PLoS One, 11, e0168136. https://doi.org/10.1371/journal.pone.0168136
Song, S., Hanson, M. J., Liu, B. F., Chylack, L. T., & Liang, J. J. (2008). Protein-protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching. Molecular Vision, 14, 1282–1287.
Specht, S., Miller, S. B., Mogk, A., & Bukau, B. (2011). Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces Cerevisiae. The Journal of Cell Biology, 195, 617–629. https://doi.org/10.1083/jcb.201106037
Sreekumar, P. G., Kannan, R., Kitamura, M., Spee, C., Barron, E., Ryan, S. J., & Hinton, D. R. (2010). alphaB crystallin is apically secreted within exosomes by polarized human retinal pigment epithelium and provides neuroprotection to adjacent cells. PLoS One, 5, e12578. https://doi.org/10.1371/journal.pone.0012578
Steinman, L. (2014). Immunology of relapse and remission in multiple sclerosis. Annual Review of Immunology, 32, 257–281. https://doi.org/10.1146/annurev-immunol-032713-120227
Tabata, I., Atomi, Y., Kanehisa, H., & Miyashita, M. (1990). Effect of high-intensity endurance training on isokinetic muscle power. European Journal of Applied Physiology and Occupational Physiology, 60, 254–258.
Tabony, J., & Job, D. (1992). Gravitational symmetry breaking in microtubular dissipative structures. Proceedings of the National Academy of Sciences of the United States of America, 89, 6948–6952.
Treweek, T. M., Rekas, A., Walker, M. J., & Carver, J. A. (2010). A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, alphaA- and alphaB-crystallin. Experimental Eye Research, 91, 691–699. https://doi.org/10.1016/j.exer.2010.08.015
Tsvetkova, N. M., Horvath, I., Torok, Z., Wolkers, W. F., Balogi, Z., Shigapova, N., Crowe, L. M., Tablin, F., Vierling, E., Crowe, J. H., & Vigh, L. (2002). Small heat-shock proteins regulate membrane lipid polymorphism. Proceedings of the National Academy of Sciences of the United States of America, 99, 13504–13509. https://doi.org/10.1073/pnas.192468399
Uhlen, M., Fagerberg, L., Hallstrom, B. M., Lindskog, C., Oksvold, P., Mardinoglu, A., Sivertsson, A., Kampf, C., Sjostedt, E., Asplund, A., Olsson, I., Edlund, K., Lundberg, E., Navani, S., Szigyarto, C. A., Odeberg, J., Djureinovic, D., Takanen, J. O., Hober, S., Alm, T., Edqvist, P. H., Berling, H., Tegel, H., Mulder, J., Rockberg, J., Nilsson, P., Schwenk, J. M., Hamsten, M., von Feilitzen, K., Forsberg, M., Persson, L., Johansson, F., Zwahlen, M., von Heijne, G., Nielsen, J., & Ponten, F. (2015). Proteomics. Tissue-based map of the human proteome. Science, 347, 1260419. https://doi.org/10.1126/science.1260419
Ulbricht, A., & Hohfeld, J. (2013). Tension-induced autophagy: May the chaperone be with you. Autophagy, 9, 920–922. https://doi.org/10.4161/auto.24213
Ulbricht, A., Eppler, F. J., Tapia, V. E., van der Ven, P. F., Hampe, N., Hersch, N., Vakeel, P., Stadel, D., Haas, A., Saftig, P., Behrends, C., Furst, D. O., Volkmer, R., Hoffmann, B., Kolanus, W., & Hohfeld, J. (2013). Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. Current Biology, 23, 430–435. https://doi.org/10.1016/j.cub.2013.01.064
Uversky, V. N., & Dunker, A. K. (2010). Understanding protein non-folding. Biochimica et Biophysica Acta, 1804, 1231–1264. https://doi.org/10.1016/j.bbapap.2010.01.017
van den Brand, R., Heutschi, J., Barraud, Q., DiGiovanna, J., Bartholdi, K., Huerlimann, M., Friedli, L., Vollenweider, I., Moraud, E. M., Duis, S., Dominici, N., Micera, S., Musienko, P., & Courtine, G. (2012). Restoring voluntary control of locomotion after paralyzing spinal cord injury. Science, 336, 1182–1185. https://doi.org/10.1126/science.1217416
Vandenburgh, H. H., Hatfaludy, S., Sohar, I., & Shansky, J. (1990). Stretch-induced prostaglandins and protein turnover in cultured skeletal muscle. The American Journal of Physiology, 259, C232–C240.
Varlet, A. A., Fuchs, M., Luthold, C., Lambert, H., Landry, J., & Lavoie, J. N. (2017). Fine-tuning of actin dynamics by the HSPB8-BAG3 chaperone complex facilitates cytokinesis and contributes to its impact on cell division. Cell Stress & Chaperones, 22, 553–567. https://doi.org/10.1007/s12192-017-0780-2
Walther, D. M., Kasturi, P., Zheng, M., Pinkert, S., Vecchi, G., Ciryam, P., Morimoto, R. I., Dobson, C. M., Vendruscolo, M., Mann, M., & Hartl, F. U. (2015). Widespread proteome remodeling and aggregation in Aging C. elegans. Cell, 161, 919–932. https://doi.org/10.1016/j.cell.2015.03.032
Wang, K., McClure, J., & Tu, A. (1979). Titin: Major myofibrillar components of striated muscle. Proceedings of the National Academy of Sciences of the United States of America, 76, 3698–3702.
Waters, E. R. (1995). The molecular evolution of the small heat-shock proteins in plants. Genetics, 141, 785–795.
Waters, E. R., Lee, G. J., & Vierling, E. (1996). Evolution, structure and function of the small heat shock proteins in plants. Journal of Experimental Botany, 47, 325–338.
Watson, J. D., & Crick, F. H. (1953). Molecular structure of nucleic acids; A structure for deoxyribose nucleic acid. Nature, 171, 737–738.
Westerheide, S. D., & Morimoto, R. I. (2005). Heat shock response modulators as therapeutic tools for diseases of protein conformation. The Journal of Biological Chemistry, 280, 33097–33100. https://doi.org/10.1074/jbc.R500010200
Yamaguchi, T., Suzuki, T., Arai, H., Tanabe, S., & Atomi, Y. (2010). Continuous mild heat stress induces differentiation of mammalian myoblasts, shifting fiber type from fast to slow. American Journal of Physiology. Cell Physiology, 298, C140–C148. https://doi.org/10.1152/ajpcell.00050.2009
Acknowledgements
The works described here were partially supported by Grants-in-Aid for Scientific Research from the Japan Society for the Promotion of Science, Research grant from Japan Space Utilization Promotion Center, and Research grant from Japan Space Forum.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG, part of Springer Nature
About this chapter
Cite this chapter
Atomi, Y. et al. (2018). Geroscience From Cell-body Dynamics and Proteostasis Cooperation Supported by αB-crystallin and Human will ~ A Proposal of “Body-Mind Integrative Science”. In: Asea, A., Kaur, P. (eds) Regulation of Heat Shock Protein Responses. Heat Shock Proteins, vol 13. Springer, Cham. https://doi.org/10.1007/978-3-319-74715-6_13
Download citation
DOI: https://doi.org/10.1007/978-3-319-74715-6_13
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-74714-9
Online ISBN: 978-3-319-74715-6
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)