In aging mammalian cells, the levels of molecular chaperones and proteases are significandy decreased and, in parallel, irreversibly damaged proteins accumulate.29'30 In addition to their general cytotoxic effect, irreversibly damaged proteins can inhibit the activity of the remaining minority of active chaperones and proteases. At this stage, old or mutant cells often choose suicide, which may be advantageous to some forms of life, as in the case of cancer cells, or of infected plant tissues that prevent the propagation of the pathogen to the whole plant.
Interestingly, Hsp70 has been shown to protect against cell death by directly interfering with the mitochondrial apoptosis pathway.31 This is exemplified in the case of the acute respiratory distress syndrome (ARDS), which is an inflammatory response in the lungs culminating in necrosis and fatal apoptosis. Sepsis-induced ARDS in rats correlates with the specific failure of Hsp70 expression in alveolar tissues.32 In contrast, in a rat model of sepsis-induced ARDS, adenovirus-mediated transient expression of Hsp70 in the lungs effectively prevented apoptosis, lung failure and dramatically improved survival.33 The overproduction of molecular chaperones observed following treatments with various nonsteroidal anti-inflammatory drugs (NSAIDs), such as sodium salicylate,13 ibuprofen,34 and less classical Hsp-inducers such as celastrol,35 resveratrol (the French paradox), geranylgeranylacetone,37 may be responsible for the observed reduction of damages related to reactive oxygen species and induced programmed cell death in various damaging contexts, such as ARDS, post-ischemic reperfusions,39 excessive inflammation, toxic protein aggregation and protein-conformation neurodegenerative diseases and aging.40
Human societies seldom choose collective suicide in response to lawlessness, which is a noticeable difference between cellular and social levels of crime responses. Yet, as in the cell, a massive build up of law-enforcement forces, when energetically still possible, may gradually decrease lawlessness and restore cellular functions in societies, as well as in cells otherwise doomed to self destruction. This is observed in the case of apoptotic tissues treated with NSAIDs or low doses of Hsp-inducing poisons.24'40 Another major difference between criminal molecules in the cell and social criminals is the extreme dependence of human newborns toward their parents and siblings. Unlike proteins, the successful formation of a functional member of the human society demands a massive, long-term investment from the progenitors and the education system. This phenomenon, which has no obvious parallel in the cell, could not withstand selective pressures of evolution, unless the existence of powerful ties between relatives in the human society, namely affective ties, that do not readily disappear once the person has become a functional unit of the society, or a criminal. In contrast to children, nascent proteins exit the ribosome with all the information necessary for their spontaneous folding into functional units of the cell. Unlike parental education, no new information is to be transmitted to a folding protein by the molecular chaperones. Chaperones may only passively prevent proteins from leaving, or actively return astrayed proteins on their innate native folding path.
The resilient affective ties between humans, especially from the same family or clan, have gradually influenced policies of crime management by human societies, especially in recent history, with the appearance of humanism. Whereas ribosomes have apparendy no particular feelings towards the proteins they synthesize, siblings of convicted criminals and less-related humanists have become increasingly reluctant to accept irreversible radical solutions to social criminality, such as torture, amputations and executions, and encouraged solutions whereby criminals may be reeducated, pardoned, reinserted as functional members of the society, and in the worst case, incarcerated for a half life period, at most.
Nonetheless, many remarkable parallels, sometimes ethically questionable, but didactically appealing, do exist between the proteins in the cell, and humans in the society (see Table 1). These parallels were initially expressed by the adequate, albeit incomplete, social term "chaper-one", suggesting only a rather passive defence mechanism against toxic protein aggregations in the cell. They can inspire scientists and politicians alike, in their commons search for solutions to crime: may it be molecular crime, as in the case of aggregate-induced neurodegeneration and aging, or social crime, as in the case of mobs burning foreign embassies, or terrorists waging war on the democracies of the world.
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