Skip to main content
SpringerLink
Log in

Exercise Intensity and Duration Affect Blood-Soluble HSP72

  • Chapter
  • First Online:
Book cover Heat Shock Proteins and Whole Body Physiology

Part of the book series: Heat Shock Proteins ((HESP,volume 5))

Abstract

Extracellular Hsp72 (eHsp72) is elevated during and after acute bouts of exercise. Concentrations of eHsp72 in plasma or serum are dependent on the duration and intensity of exercise. Active secretory processes rather than passive release due to cell damage are considered to function in the exercise-induced release of eHsp72. Up-regulation of eHsp72 in the circulation following acute exercise may contribute to improved immune function; eHsp72 increases stress resistance after binding to stress sensitive recipients, signals tissue destruction and danger to inflammatory cells, and aids in immunosurveillance by transporting intracellular peptides to distant immune cells. It is uncertain whether this exercise-mediated mechanism for eHsp72-regulated activation of the immune system helps to prevent immunologic diseases

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Abbreviations

APC:

antigen-presenting cells

ATP:

adenosine triphosphate

CCRS:

chemokine receptors

eHsp72:

extracellular Hsp72

HSP:

heat shock proteins

Hsp72:

seventy two kilo-dalton HSP

MHC:

major histocompatibility complex

PBMC:

peripheral blood mononuclear cells

TLR:

toll-like receptor

References

  • Asea, A., Kabingu, E., Stevenson, M. A. and Calderwood, S. K. (2000) HSP70 peptidembearing and peptide-negative preparations act as chaperokines. Cell Stress Chaperones. 5, 425–431.

    Article  CAS  PubMed  Google Scholar 

  • Asea, A. (2003) Chaperokine-induced signal transduction pathways. Exerc Immunol Rev. 9, 25–33.

    PubMed  Google Scholar 

  • Asea, A. (2005) Stress proteins and initiation of immune response: chaperokine activity of hsp72. Exerc Immunol Rev. 11, 34–45.

    PubMed  Google Scholar 

  • Banfi, G., Malavazos, A., Iorio, E., Dolci, A., Doneda, L., Verna, R. and Corsi, M. M. (2005) Plasma oxidative stress biomarkers, nitric oxide and heat shock protein 70 in trained elite soccer players. Eur J Appl Physiol. 96(5), 483–486.

    Article  PubMed  Google Scholar 

  • Basu, S., Binder, R. J., Suto, R., Anderson, K. M. and Srivastava, P. K. (2000) Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int Immunol. 12, 1539–1546.

    Article  CAS  PubMed  Google Scholar 

  • Blanchard, N., Lankar, D., Faure, F., Regnault, A., Dumont, C., Raposo, G. and Hivroz, C. (2002) TCR activation of human T cells induces the production of exosomes bearing the TCR/CD3/zeta complex. J Immunol. 168(7), 3235–3241.

    CAS  PubMed  Google Scholar 

  • Broquet, A. H., Thomas, G., Masliah, J., Trugnan, G. and Bachelet, M. (2003) Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release. J Biol Chem. 278(24), 21601–21606.

    Article  CAS  PubMed  Google Scholar 

  • Calderwood, S. K., Mambula, S. S., Gray, P. J., Jr. and Theriault, J. R. (2007) Extracellular heat shock proteins in cell signaling. FEBS Lett. 581(19), 3689–3694.

    Article  CAS  PubMed  Google Scholar 

  • Campisi, J., Leem, T. H. and Fleshner, M. (2003) Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system. Cell Stress Chaperones. 8, 272–286.

    Article  CAS  PubMed  Google Scholar 

  • Clayton, A., Turkes, A., Navabi, H., Mason, M. D. and Tabi, Z. (2005) Induction of heat shock proteins in B-cell exosomes. J Cell Sci. 118(Pt 16), 3631–3638.

    Article  CAS  PubMed  Google Scholar 

  • Daniels, G. A., Sanchez-Perez, L., Diaz, R. M., Kottke, T., Thompson, J., Lai, M., Gough, M., Karim, M., Bushell, A., Chong, H., Melcher, A., Harrington, K. and Vile, R. G. (2004) A simple method to cure established tumors by inflammatory killing of normal cells. Nat Biotechnol. 22(9), 1125–1132.

    Article  CAS  PubMed  Google Scholar 

  • Delneste, Y., Magistrelli, G., Gauchat, J., Haeuw, J., Aubry, J., Nakamura, K., Kawakami-Honda, N., Goetsch, L., Sawamura, T., Bonnefoy, J. and Jeannin, P. (2002) Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation. Immunity. 17(3), 353–362.

    Article  CAS  PubMed  Google Scholar 

  • Di Girolamo, M., Dani, N., Stilla, A., Corda, D. (2005) Physiological relevance of the endogenous mono(ADP-ribosyl)ation of cellular proteins. FEBS J. 272(18), 4565–4575.

    Article  PubMed  Google Scholar 

  • Doody, A. D., Kovalchin, J. T., Mihalyo, M. A., Hagymasi, A. T., Drake, C. G. and Adler, A. J. (2004) Glycoprotein 96 can chaperone both MHC class I- and class II-restricted epitopes for in vivo presentation, but selectively primes CD8+ T cell effector function. J Immunol. 172, 6087–6092.

    CAS  PubMed  Google Scholar 

  • Febbraio, M. A., Ott, P., Nielsen, H. B., Steensberg, A., Keller, C., Krustrup, P., Secher, N. H. and Pedersen, B. K. (2002) Exercise induces hepatosplanchnic release of heat shock protein 72 in humans. J Physiol. 544, 957–962.

    Article  CAS  PubMed  Google Scholar 

  • Febbraio, M. A., Mesa, J. L., Chung, J., Steensberg, A., Keller, C., Nielsen, H. B., Krustrup, P., Ott, P., Secher, N. H. and Pedersen, B. K. (2004) Glucose ingestion attenuates the exercise-induced increase in circulating heat shock protein 72 and heat shock protein 60 in humans. Cell Stress Chaperones. 9(4), 390–396.

    Article  CAS  PubMed  Google Scholar 

  • Fehrenbach, E., Niess, A. M., Schlotz, E., Passek, F., Dickhuth, H. -H. and Northoff, H. (2000a) Transcriptional and translational regulation of heat shock proteins (HSP27, HSP70) in leukocytes of endurance runners. J Appl Physiol. 89, 704–710.

    CAS  PubMed  Google Scholar 

  • Fehrenbach, E., Passek, F., Niess, A. M., Pohla, H., Weinstock, C., Dickhuth, H.-H. and Northoff, H. (2000b) HSP expression in human leucocytes is modulated by endurance exercise. Med Sci Sports Exerc. 32, 592–600.

    Article  CAS  PubMed  Google Scholar 

  • Fehrenbach, E., Niess, A. M., Dickhuth, H.-H. and Northoff, H. (2002) Influence of exercise, heat and hypoxia on plasma-HSP72. Eur J Physiol (Pfluegers Arch). 443(Suppl.), S362.

    Article  Google Scholar 

  • Fehrenbach, E.Cellular responses to environmental stress. In: Molecular and Cellular Exercise Physiology, F. C. Mooren and K. Voelker, eds., Human Kinetics, Muenster, 2005, pp. 199–218.

    Google Scholar 

  • Fehrenbach, E., Niess, A. M., Voelker, K., Northoff, H. and Mooren, F. C. (2005) Exercise intensity and duration affect blood soluble HSP72. Int J Sports Med. 26, 552–557.

    Article  CAS  PubMed  Google Scholar 

  • Fischer, C. P., Hiscock, N. J., Basu, S., Vessby, B., Kallner, A., Sjöberg, L. B., Febbraio, M. A. and Pedersen, B. K. (2006) Vitamin E isoform-specific inhibition of the exercise-induced heat shock protein 72 expression in humans. J Appl Physiol. 100(5), 1679–1687.

    Article  CAS  PubMed  Google Scholar 

  • Fleshner, M., Campisi, J. and Johnson, J. D. (2003) Can exercise stress facilitate innate immunity? A functional role for stress-induced extracellular Hsp72. Exerc Immunol Rev. 9, 6–24.

    PubMed  Google Scholar 

  • Fleshner, M. and Johnson, J. D. (2005) Endogenous extra-cellular heat shock protein 72: releasing signal(s) and function. Int J Hyperthermia. 21, 457–471.

    Article  CAS  PubMed  Google Scholar 

  • Floto, R. A., MacAry, P. A., Boname, J. M., Mien, T. S., Kampmann, B., Hair, J. R., Huey, O. S., Houben, E. N., Pieters, J., Day, C., Oehlmann, W., Singh, M., Smith, K. G. and Lehner, P. J. (2006) Dendritic cell stimulation by mycobacterial Hsp70 is mediated through CCR5. Science. 314(5798), 454–458.

    Article  CAS  PubMed  Google Scholar 

  • Gastpar, R., Gross, C., Rossbacher, L., Ellwart, J., Riegger, J., Multhoff, G. (2004) The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. J Immunol. 172(2), 972–980.

    CAS  PubMed  Google Scholar 

  • Gomez-Merino, D., Drogou, C., Guezennec, C. Y., Burnat, P., Bourrilhon, C., Tomaszewski, A., Milhau, S. and Chennaoui, M. (2006) Comparison of systemic cytokine responses after a long distance triathlon and a 100-km run: relationship to metabolic and inflammatory processes. Eur Cytokine Netw. 17(2), 117–124.

    CAS  PubMed  Google Scholar 

  • Gu, B. J., Zhang, W. Y., Bendall, L. J., Chessell, I. P., Buell, G. N. and Wiley, J. S. (2000) Expression of P2X(7) purinoceptors on human lymphocytes and monocytes: evidence for nonfunctional P2X(7) receptors. Am J Physiol Cell Physiol. 279(4), C1189–C1197.

    CAS  PubMed  Google Scholar 

  • Hirose, L., Nosaka, K., Newton, M., Laveder, A., Kano, M., Peake, J. and Suzuki, K. (2004) Changes in inflammatory mediators following eccentric exercise of the elbow flexors. Exerc Immunol Rev. 10, 75–90.

    PubMed  Google Scholar 

  • Horn, P., Kalz, A., Lim, C. L., Pyne, D., Saunders, P., Mackinnon, L., Peake, J. and Suzuki, K. (2007) Exercise-recruited NK cells display exercise-associated eHSP-70. Exerc Immunol Rev. 13, 100–111.

    PubMed  Google Scholar 

  • Hunter-Lavin, C., Davies, E. L., Bacelar, M. M., Marshall, M. J., Andrew, S. M. and Williams, J. H. (2004) Hsp70 release from peripheral blood mononuclear cells. Biochem Biophys Res Commun. 324, 511–517.

    Article  CAS  PubMed  Google Scholar 

  • Jiang, L. H., Mackenzie, A. B., North, R. A. and Surprenant, A. (2000) Brilliant blue G selectively blocks ATP-gated rat P2X(7) receptors. Mol Pharmacol. 58(1), 82–88.

    CAS  PubMed  Google Scholar 

  • Johnson, J. D., Campisi, J., Sharkey, C. M., Kennedy, S. L., Nickerson, M. and Fleshner, M. (2005) Adrenergic receptors mediate stress-induced elevations in extracellular Hsp72. J Appl Physiol. 99(5), 1789–1795.

    Article  CAS  PubMed  Google Scholar 

  • Kregel, K. C. and Moseley, P. L. (1996) Differential effects of exercise and heat stress on liver HSP70 accumulation with aging. J Appl Physiol. 80, 547–551.

    CAS  PubMed  Google Scholar 

  • Lancaster, G. I., Moller, K., Nielsen, B., Secher, N. H., Febbraio, M. A. and Nybo, L. (2004) Exercise induces the release of heat shock protein 72 from the human brain in vivo. Cell Stress Chaperones. 9, 276–280.

    Article  CAS  PubMed  Google Scholar 

  • Lancaster, G. I. and Febbraio, M. A. (2005a) Exosome-dependent trafficking of HSP70: a novel secretory pathway for cellular stress proteins. J Biol Chem. 280, 23349–23355.

    Article  CAS  PubMed  Google Scholar 

  • Lancaster, G. I. and Febbraio, M. A. (2005b) Mechanisms of stress-induced cellular HSP72 release: implications for exercise-induced increases in extracellular HSP72. Exerc Immunol Rev. 11, 46–52.

    PubMed  Google Scholar 

  • Lovell, R., Madden, L., Carroll, S., McNaughton, L. (2007) The time-profile of the PBMC HSP70 response to in vitro heat shock appears temperature-dependent. Amino Acids. 33(1), 137–144.

    Article  CAS  PubMed  Google Scholar 

  • Mambula, S. S. and Calderwood, S. K. (2006) Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes. J Immunol. 177(11), 7849–7857.

    CAS  PubMed  Google Scholar 

  • Mambula, S. S., Stevenson, M. A., Ogawa, K. and Calderwood, S. K. (2007) Mechanisms for Hsp70 secretion: crossing membranes without a leader. Methods. 43(3), 168–175.

    Article  CAS  PubMed  Google Scholar 

  • Marshall, H. C., Ferguson, R. A. and Nimmo, M. A. (2006) Human resting extracellular heat shock protein 72 concentration decreases during the initial adaptation to exercise in a hot, humid environment. Cell Stress Chaperones. 11(2), 129–134.

    Article  CAS  PubMed  Google Scholar 

  • Matzinger, P. (2002) An innate sense of danger. Ann N Y Acad Sci. 961, 341–342.

    Article  PubMed  Google Scholar 

  • Millar, D. G., Garza, K. M., Odermatt, B., Elford, A. R., Ono, N., Li, Z. and Ohashi, P. S. (2003) Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo. Nat Med. 9(12), 1469–1476.

    Article  CAS  PubMed  Google Scholar 

  • Moseley, P. (2000) Stress proteins and the immune response. Immunopharmacology. 48, 299–302.

    Article  CAS  PubMed  Google Scholar 

  • Multhoff, G. (2002) Activation of natural killer cells by heat shock protein 70. Int J Hyperthermia. 18(6), 576–585.

    Article  CAS  PubMed  Google Scholar 

  • Niess, A. M., Fehrenbach, E., Schlotz, E., Sommer, M., Angres, C., Tschositsch, K., Battenfeld, N., Golly, I. C., Biesalski, H. K., Northoff, H. and Dickhuth, H. H. (2002) Effects of RRR-alpha-tocopherol on leukocyte expression of HSP72 in response to exhaustive treadmill exercise. Int J Sports Med. 23(6), 445–452.

    Article  CAS  PubMed  Google Scholar 

  • North, R. A. (2002) Molecular physiology of P2X receptors. Physiol Rev. 82(4), 1013–1067.

    CAS  PubMed  Google Scholar 

  • Pannicke, T., Fischer, W., Biedermann, B., Schädlich, H., Grosche, J., Faude, F., Wiedemann, P., Allgaier, C., Illes, P., Burnstock, G. and Reichenbach, A. (2000) P2X7 receptors in Müller glial cells from the human retina. J Neurosci. 20(16), 5965–5972.

    CAS  PubMed  Google Scholar 

  • Peake, J. M., Suzuki, K., Hordern, M., Wilson, G., Nosaka, K. and Coombes, J. S. (2005) Plasma cytokine changes in relation to exercise intensity and muscle damage. Eur J Appl Physiol. 95, 514–521.

    Article  CAS  PubMed  Google Scholar 

  • Pockley, A. G. (2001) Heat shock proteins in health and disease: therapeutic targets or therapeutic agents? Expert Rev Mol Med. 3(23), 1–21.

    Article  CAS  PubMed  Google Scholar 

  • Radons, J. and Multhoff, G. (2005) Immunostimulatory functions of membrane-bound and exported heat shock protein 70. Exerc Immunol Rev. 11, 17–33.

    PubMed  Google Scholar 

  • Salo, D. C., Donovan, C. M. and Davies, K. J. (1991) HSP70 and other possible heat shock or oxidative stress proteins are induced in skeletal muscle, heart, and liver during exercise. Free Radic Biol Med. 11, 239–246.

    Article  CAS  PubMed  Google Scholar 

  • Schild, H. and Rammensee, H. G. (2000) gp96-the immune system’s Swiss army knife. Nat Immunol. 1(2), 100–101.

    Article  CAS  PubMed  Google Scholar 

  • Segura, E., Amigorena, S. and Théry, C. (2005) Mature dendritic cells secrete exosomes with strong ability to induce antigen-specific effector immune responses. Blood Cells Mol Dis. 35(2), 89–93.

    Article  CAS  PubMed  Google Scholar 

  • Skokos, D., Botros, H. G., Demeure, C., Morin, J., Peronet, R., Birkenmeier, G., Boudaly, S. and Mécheri, S. (2003) Mast cell-derived exosomes induce phenotypic and functional maturation of dendritic cells and elicit specific immune responses in vivo. J Immunol. 170(6), 3037–3045.

    CAS  PubMed  Google Scholar 

  • Thériault, J. R., Mambula, S. S., Sawamura, T., Stevenson, M. A. and Calderwood, S. K. (2005) Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells. FEBS Lett. 579(9), 951–1960.

    Article  Google Scholar 

  • Vabulas, R. M., Ahmad-Nejad, P., da Costa, C., Miethke, T., Kirschning, C. J., Hacker, H. and Wagner, H. (2001) Endocytosed HSP60 s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells. J Biol Chem. 276, 31332–31339.

    Article  CAS  PubMed  Google Scholar 

  • van Niel, G., Raposo, G., Candalh, C., Boussac, M., Hershberg, R, Cerf-Bensussan N, Heyman M. (2001) Intestinal epithelial cells secrete exosome-like vesicles. Gastroenterology. 121(2), 337–349.

    Article  PubMed  Google Scholar 

  • Walsh, R. C., Koukoulas, I., Garnham, A., Moseley, P. L., Hargreaves, M. and Febbraio, M. A. (2001) Exercise increases serum Hsp72 in humans. Cell Stress Chaperones. 6, 386–393.

    Article  CAS  PubMed  Google Scholar 

  • Whitham, M., Walker, G. J. and Bishop, N. C. (2006) Effect of caffeine supplementation on the extracellular heat shock protein 72 response to exercise. J Appl Physiol. 101(4), 1222–1227.

    Article  CAS  PubMed  Google Scholar 

  • Yamada, P. M., Amorim, F. T., Moseley, P., Robergs, R. and Schneider, S. M. (2007) Effect of heat acclimation on heat shock protein 72 and interleukin-10 in humans. J Appl Physiol. 103(4), 1196–1204.

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Research Team for Social Participation and Health Promotion, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan

    Kishiko Ogawa

  2. Institute of Clinical and Experimental Transfusion Medicine (IKET), University of Tuebingen, Otfried-Mueller-Strabe 4/1, D-72076, Tuebingen, Germany

    Elvira Fehrenbach

Authors
  1. Kishiko Ogawa
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Elvira Fehrenbach
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Elvira Fehrenbach .

Editor information

Editors and Affiliations

  1. College of Medicine, Texas A & M University System, South 1st St. 1901, Temple, 76508, U.S.A.

    Alexzander A. A. Asea

  2. Rigshospitalet, University of Copenhagen, Blegdamsvej 9, Koebenhavn, 2100, Denmark

    Bente K. Pedersen

Rights and permissions

Reprints and permissions

Copyright information

© 2010 Springer Science+Business Media B.V.

About this chapter

Cite this chapter

Ogawa, K., Fehrenbach, E. (2010). Exercise Intensity and Duration Affect Blood-Soluble HSP72. In: Asea, A., Pedersen, B. (eds) Heat Shock Proteins and Whole Body Physiology. Heat Shock Proteins, vol 5. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-3381-9_15

Download citation

Publish with us

Policies and ethics

Search

Navigation