Beta-amyloid protein promotes neuritic branching in hippocampal cultures.
In the neuritic plaques of Alzheimer's disease, abnormal neuritic processes cluster around a core of beta-amyloid protein. Previous data have shown that beta 1-28, a peptide homologous to the first 28 amino acid residues of beta-amyloid protein, enhanced survival without affecting neuritic extension or branching in cultures of hippocampal neurons. In this paper we show that beta 1-42, a synthetic peptide which corresponds to the full 42 amino acid sequence of beta-amyloid protein, increased cell survival and also promoted the elongation of axon-like processes, raised the number of dendrite-like processes, and increased their arborization.
Whitson
J S
JS
Department of Psychobiology, University of California, Irvine 92717.
Glabe
C G
CG
Shintani
E
E
Abcar
A
A
Cotman
C W
CW
D000682:Amyloid / Q000494:pharmacology*; D016229:Amyloid beta-Peptides; D000818:Animals; D002454:Cell Differentiation / Q000187:drug effects; D002478:Cells, Cultured; D003712:Dendrites / Q000187:drug effects; D006624:Hippocampus / Q000166:cytology* / Q000187:drug effects; D051381:Rats
D000682:Amyloid; D016229:Amyloid beta-Peptides