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Speciation 98: Abstracts
Christopher Exley Ph.D., Royal Society University Research Fellow
Birchall Centre for Inorganic Chemistry and Materials Science, Department of Chemistry, Keele University, Staffordshire, ST5 5BG, UK.
The mechanism whereby a soluble protein or peptide alters its shape and solubility to adopt a conformer with cytotoxic potential is of interest. Such a mechanism is implicated in the cell death found in non-insulin-dependent diabetes, Alzheimer's disease and number of transmissible spongiform encephalopathies.
The post-translational modification of soluble proteins/peptides through the spontaneous non-enzymatic addition of reducing sugars to their free amino groups will alter their conformation and induce them to form stable aggregates. The post-translational modifications are alternatively known as Advanced Glycation End-Products (AGE) and have been identified associated with markers for the aforementioned diseases.
The formation of AGE's in vivo is probably extremely slow.
Perhaps too slow to be aetiologically significant. Recent research
has suggested a role for aluminium in the formation of AGE's (Exley
et al., 1995 FEBS Lett. 364, 182-184). Aluminium,
and particular in combination with ATP, was found to promote the
formation of AGE's (Exley, 1997 Neuroreport 8, 3411-3414).
The mechanism of action of aluminium in accelerating non-enzymatic
glycation is currently under investigation in our laboratory and
the latest results of this research will be presented.
