Human amyloid-beta1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat.

Human amyloid-beta1-42 has been suggested to be a pathogenetic factor in Alzheimer's disease. The precise mechanism by which this peptide causes the degeneration of neurons in the affected brain is not yet fully understood. By using immunohistochemistry we explored the inhibitory effects of human amyloid-beta1-42 applied in vivo on the fast axonal transport of acetylcholinesterase, the amyloid precursor protein, the vesicular acetylcholine transporter and synaptophysin in the sciatic nerve of rat.

Vulnerability of small GABAergic neurons to human beta-amyloid pentapeptide.

beta-Amyloid peptide (A beta), the principal component of senile plaques in Alzheimer's disease, has been found to be neurotoxic. The role of A beta in the deficits of the GABAergic system in patients with Alzheimer's disease is unclear. It has been suggested that the cytotoxic activity of A beta is localized to amino acid residues 25-35 of this peptide, which contains a total of 42 amino acid residues.

Muscle-pedicle grafts or muscle-pedicle-bone grafts in the treatment of avascular necrotic femoral heads.

The paper is a microangiographic study of the revascularisation of experimentally devascularised femoral heads in rabbits. We examined the revascularisation process in muscle pedicles implanted into the devascularised femoral heads. Two forms of pediculated grafts were used: muscle-pedicle grafts and muscle-bone-pedicle grafts.