Document Detail

The basic reality of mind and spongiform diseases.
MedLine Citation:
PMID:  11735309     Owner:  NLM     Status:  MEDLINE    
A change in handedness (chirality) in some amino acids appears to be the basic physical change in degradation-resistant proteins (prions) found in conditions such as Creutzfeldt-Jacob disease (CJD), Alzheimer's disease (AD), bovine spongiform encephalopathy (BSE) and ovine scrapie. The affected structures are primarily innervated by cholinergic nerves. Much evidence suggests that these so-called prions (here named chirons) are harmless, non-infectious products. The importance of the cholinergic system allows a new simplified interpretation of these conditions. The main steps are the acetylcholine-cholinesterase splitting of body water with release of free protons in solution, followed by electron dissipation, dioxygen activation and Ca-fluxes. Abiotic physics conserves parity and symmetry by equal amounts of L- and D-forms of molecules. In contrast, the asymmetric pattern of life must be homochiral. Such biomolecules dissolve in water and are thus able to interact in cholinergic hydrodynamics. It is supposed that the instability of the composite weak force by beta-decay causes changes in chirality. These extremely rare events are not frequent enough to explain disease pathology. Experimental, accidental, surgical and abusive inoculations will propagate chirons according to the physical law of self-replication, which also occurs in test tubes without added biological products. Chirons will not be degraded into amino acids in the alimentary canal and will, because they are indigestible, leave the body with the faeces. Chirons are inert also to the immune system and will be engulfed without reaction by phagocytosing cells. They are then stored away in tissues, where they do no harm (if not detected and suspected to be deleterious, thereby causing pathogenic anxiety). The cholinergic system reacts to all kinds of integrity threats and it is this reaction which I propose causes the so-called prion diseases. This pathology seems generally valid, and is here exemplified in AD, CJD, and Kuru disease. It is the cholinergic reaction and not the agent per se that is pathogenic. This is also true of viral infections where the interaction between viral infection and response may explain the enigmatic epidemiology of many neurodegenerative diseases. Intensity and duration of challenges will determine pathophysiology. The new variant of CJD, vCJD, is assumed to result from mutation of a slow virus agent into a more intense variant, which will give disease in younger patients. The pathology is primary protonic, with overactivity in most sub-systems of either enhancing or inhibiting character, but also functional failure or cell death by membrane damage and acidification, for instance in the CNS. The practical results of this proposal will be alleviation of the current BSE crisis. The important main aspects are: chirons are not infectious proteins but inert physical by-products; they are indigestible and not immunogenic, so beef is safe; properly processed and handled meat and bone-meal are not likely to transmit neurodegenerative diseases; chirons cannot even serve as markers in neurologic diseases.
S Axelsson
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Medical hypotheses     Volume:  57     ISSN:  0306-9877     ISO Abbreviation:  Med. Hypotheses     Publication Date:  2001 Nov 
Date Detail:
Created Date:  2001-12-12     Completed Date:  2002-02-13     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  7505668     Medline TA:  Med Hypotheses     Country:  Scotland    
Other Details:
Languages:  eng     Pagination:  549-54     Citation Subset:  IM    
Copyright Information:
Copyright 2001 Harcourt Publishers Ltd.
Department of Obstetrics and Gynaecology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
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MeSH Terms
Amino Acids / chemistry,  metabolism*
Brain / physiology*
Prion Diseases / metabolism*
Reg. No./Substance:
0/Amino Acids

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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