Elsevier

Medical Hypotheses

Volume 51, Issue 2, August 1998, Pages 153-163
Medical Hypotheses

Mechanisms of autoprotection and the role of stress-proteins in natural defenses, autoprotection, and salutogenesis

https://doi.org/10.1016/S0306-9877(98)90110-4Get rights and content

Abstract

We hypothesize that in all physiotherapeutically oriented procedures of naturotherapy — such as helio-, climate-, thalasso- or hydrotherapy or certain forms of physical exercise — the transient expression of stress-proteins (heat-shock proteins, HSPs) is an important element of salutogenesis. These therapeutical procedures all cause a transitory ‘disturbance’ by an unspecific stressor that leads to functional responses. These functional responses can be trained and thus increase the forces and the capacity for resistance of the organism.

The autoprotective mechanisms which we want to deal with in more detail are based on the functions of the heat-shock proteins (HSPs, stress-response proteins, ‘chaperones’) and represent archaic autoprotective responses. In addition, more complex mechanisms of autoprotection seem to have evolved that may play a role in the natural defenses against disease and which show a hierarchy of various genomically conserved strategies with different time-constants and time windows. This becomes apparent by studying autoprotective responses of the cardiovascular system of warm-blooded animals under ischemic stress. Recent extensive experimental protocols and clinical observations in elucidating the molecular basis of cardiac ischemia show that powerful autoprotective mechanisms are involved in the phenomena of ‘hibernation’, ‘stunning’, and ‘ischemic preconditioning’. The system of the heat-shock proteins may therefore be regarded as a basic model for the principle of autoprotection and salutogenesis.

References (94)

  • D.M. Yellon et al.

    Preconditioning the human myocardium

    Lancet

    (1993)
  • D. Yellon et al.

    Stress proteins and myocardial protection

    J Mol Cell Card

    (1992)
  • S.H. Rahimtoola

    The hibernating myocardium

    Am Heart J

    (1989)
  • S. Lindquist et al.

    The heat-shock proteins

    Annu Rev Genet

    (1988)
  • R.J. Ellis

    Proteins as molecular chaperones

    Nature

    (1987)
  • B. Lohff et al.

    Natural defences and autoprotection: naturotherapy, an old concept of healing in a new perspective

    Med Hypotheses

    (1998)
  • C.B. Anfinsen

    Principles that govern the folding of protein chains

    Science

    (1973)
  • L.E. Hightower

    Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides

    J Cell Physiol

    (1980)
  • J. Anathan et al.

    Abnormal proteins serve as eucaryotic stress signals and trigger the activation of heat shock genes

    Science

    (1986)
  • R. Jaenicke

    Stability and self-organization of proteins

    Naturwissenschaften

    (1988)
  • F.U. Hartl et al.

    Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60

    Ann Rev Biophys Biomol Struc

    (1992)
  • S. Lindquist

    The heat-shock response

    Ann Rev Biochem

    (1986)
  • J.C.A. Bardwell et al.

    Eukaryotic M, 83,000 heat shock protein has a homologue in Escherichia coli

  • N. Kusukawa et al.

    Effects of mutations in heat-shock genes GroES and GroEL on protein export in Escherichia coli

    EMBO J

    (1989)
  • T. Langer et al.

    Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

    Nature

    (1992)
  • A. Azem et al.

    Characterization of a functional GroEL14 (GroES)2 chaperonin hetero-oligomer

    Science

    (1994)
  • M. Schmidt et al.

    Symmetric complexes of GroE chaperonins as part of the functional cycle

    Science

    (1994)
  • M.J. Todd et al.

    Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding

    Science

    (1994)
  • M.J. Gething et al.

    Protein folding in the cell

    Nature (London)

    (1992)
  • E.G. Hutchinson et al.

    Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa mitochondria

    EMBO J

    (1989)
  • K. Braig et al.

    The crystal structure of the bacterial chaperonin GroEL at 2.8 Å

    Nature

    (1994)
  • K. Braig et al.

    Polypeptide bound to the chaperonin GroEL binds within its central cavity

  • E. Ungewickell

    The 70-Kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that release clathrin triskelia from coated vesicles

    EMBO J

    (1985)
  • B. Bukau et al.

    Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

    J Bacteriol

    (1989)
  • S.M. Sell et al.

    Isolation and characterization of dnaJ null mutants of Escherichia coli

    J Bacteriol

    (1991)
  • F.C. Neidhardt et al.

    The genetics and regulation of heat-shock proteins

    Annu Rev Genet

    (1984)
  • K. Liberek et al.

    The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the 32 transcription factor

  • K. Liberek et al.

    The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the s32 heat shock transcriptional regulator

  • B.T. Lai et al.

    Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies

    Mol Cell Biol

    (1984)
  • V. Zimarino et al.

    Induction of sequence-specific binding of Drosophila heat-shock activator protein without protein synthesis

    Nature

    (1987)
  • I.J. Benjamin et al.

    Activation of the heat shock factor by hypoxia in mammalian cells

  • S.H.E. Kaufmann

    Heat shock proteins and immune response

  • I. Portig et al.

    Autoantikörper gegen Stressproteine in Seren von Patienten mit Dilatativer Cardiomyopathie

    Z Kardiol

    (1995)
  • T.M. Shinnick et al.

    The Mycobacterium tuberculosis 65 kilo-dalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein

    Infect Immun

    (1988)
  • D.B. Young et al.

    Stress proteins are immune targets in leprosy and tuberculosis

  • P.J. Murray et al.

    Stress and immunological recognition in host-pathogen interactions

    J Bacteriol

    (1992)
  • K. Hiromatsu et al.

    A protective role of T cells in primary infection with Listeria monocytogenes in mice

    J Exp Med

    (1992)
  • Cited by (18)

    • Putative antioxidant property of sesame oil in an oxidative stress model of myocardial injury

      2013, Journal of Cardiovascular Disease Research
      Citation Excerpt :

      Enhancement of antioxidant via administration of drugs may be one of the effective therapeutic approaches to treat IHD. The antioxidant property of drugs has been proved in various types of stressful conditions, like ischemia, ROS, endotoxins and protects the myocardium from consequent exposure to injuries of similar or more severe in nature.27–29 Cardiotoxicity mediated by ISO due to stimulation of β1 – adrenergic receptor and this stimulation not only rapidly generate ROS, but also depresses the myocardial endogenous antioxidant system leading to cause myocardial IRI.30,31

    • Chronic oral administration of raw garlic protects against isoproterenol-induced myocardial necrosis in rat

      2003, Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
    • Chapter 9 Cellular and molecular basis of stress heart

      2000, Cell and Molecular Response to Stress
    View all citing articles on Scopus
    View full text