PMID: 2109292Mar 2, 1990Paper

Aluminum induces the in vitro aggregation of bovine brain cytoskeletal proteins

Neuroscience Letters
J Díaz-Nido, J Avila

Abstract

The addition of aluminum to purified cytoskeletal proteins in vitro selectively induces the aggregation of highly phosphorylated proteins, such as the two larger neurofilament subunits (200 and 160 kDa) and the microtubule-associated proteins of the MAP-1 group (MAP-1A and MAP-1B). Other cytoskeletal proteins with a substantially lower phosphate content, such as the smaller neurofilament subunit (68 kDa) and tubulin, remain soluble, even in the presence of high aluminum concentrations. This suggests that aluminum interacts with phosphate groups in cytoskeletal proteins, causing their precipitation. The protein aggregates formed in the presence of aluminum are resistant to reagents such as urea and sodium dodecyl sulphate (SDS) which dissolve normal cytoskeletal polymers (neurofilaments and microtubules). These results favor the view that the neurotoxic effect of aluminum may be due primarily to the disorganization of the neuronal cytoskeleton which may occur subsequent to the precipitation of certain highly phosphorylated cytoskeletal proteins.

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Citations

Jan 16, 1999·Journal of Neuroscience Research·L S Yang, H Ksiezak-Reding
Aug 1, 1994·Molecular Neurobiology·R F Itzhaki
Feb 1, 1995·Molecular and Chemical Neuropathology·T B Shea
Jan 1, 1993·Progress in Neurobiology·H MeiriA Rousseau
Jun 1, 1995·Toxicology in Vitro : an International Journal Published in Association with BIBRA·T A Toimela, H Tähti
May 24, 1994·Proceedings of the National Academy of Sciences of the United States of America·M HollósiG D Fasman
Nov 8, 1994·Proceedings of the National Academy of Sciences of the United States of America·G D Fasman, C D Moore
Jun 1, 1992·Journal of Neurochemistry·J F LeterrierJ Ulrich
Mar 23, 2011·International Journal of Alzheimer's Disease·Masahiro Kawahara, Midori Kato-Negishi
May 8, 2018·Biological Trace Element Research·José L EsparzaJosé L Domingo

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