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The intracellular interaction of endoplasmic-reticulum-associated binding protein (ERAB) with amyloid-beta peptide (A-beta) may play a role in the neuronal dysfunction seen in Alzheimer's disease. It is possible that amyloid precursor-protein (APP) interacts directly, through its A-beta domain, with a sorting receptor to be passaged into axonal transport vesicles. This process may be inhibited by interaction of A-beta with the sorting machinery, which could interfere with axonal transport of other proteins.

Scientists are under pressure to find a molecular explanation for infectivity of bovine spongiform encephalopathy (BSE). Two in vitro experiements have provided further evidence for the protein-only hypothesis where transmission depends on an altered inherited protein. The purified mammalian prion protein (PrP) experiment confirms the existence of empirically observed species barriers and should help the understanding of disease that generate high infectivity titres, although are not particularly contagious.

Sulphated glycosamINNglycans may play a major role in the neuropathology of Alzheimer's disease. Two types of fibrous protein deposition in the brain are both identified as the disease's cause, namely, abundant extracellular fibrils of beta-amyloid and intracellular fibrils of polymerized tau. However, Goedert et al. found that sulphated glycosamINNglycans such as heparin induce the formation of paired helical filaments by tau. Heparin was also found to inhibit tau's binding to microtubules, thus promoting microtubule disassembly. Moreover, heparan sulphate is found with tau in affected areas of the brain during the earliest stages of Alzheimer's.

A newly developed assay for the cell-free formation of protease-resistant prion protein PrPSc involves the conversion of radiolabelled normal cellular hamster protein PrPc into PrPSc. The conversion mechanism may occur on direct protein-protein reaction or oligomer generation between PrPSc and PrPc. The presence of identical amino acid sequences of PrPc and PrPSc potentiates the conversion.

Presents research which investigated the possible mechanism to explain how the amyloid-Beta peptide (A-Beta) could damage neurons and lead to Alzheimer's disease. Research by Yan et al in October 16, 1997 edition of `Nature'; Interaction of A-Beta with endoplasmic-reticulum-associated binding protein ERAB; A-Beta and neurodegeneration; Details of Yan's research; ERAB gene; Role of extracellular plaques; A-Beta in intraneuronal sorting.