Abstract
Tau Isolated from paired helical filaments, aberrant structures that appear in Alzheimer disease (AD) patients' brains, show at least two posttranslational modifications: phosphorylation (Grundke-Iqbal et al., 1986; Ihara et al., 1986) and glycation (Ledesma et al., 1994; Yan et al., 1994). To test whether these modifications could affect the capacity of tau to self-aggregate, recombinant tau was phosphorylated and glycated, and its capacity to form polymers analyzed. Our results indicate that on phosphorylation and glycation, the capacity of tau to form aggregates increases, and that glycation of tau could stabilize the assembled polymers and could facilitate formation of bundles from these polymers.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Alzheimer Disease / metabolism
-
Alzheimer Disease / pathology
-
CDC2 Protein Kinase / metabolism
-
Calcium-Calmodulin-Dependent Protein Kinases / metabolism
-
Cloning, Molecular
-
Escherichia coli
-
Glucose / metabolism
-
Glycosylation
-
Humans
-
Macromolecular Substances
-
Microscopy, Electron
-
Phosphorylation
-
RNA Processing, Post-Transcriptional
-
Recombinant Proteins / biosynthesis
-
Recombinant Proteins / metabolism
-
Recombinant Proteins / ultrastructure
-
tau Proteins / biosynthesis
-
tau Proteins / metabolism*
-
tau Proteins / ultrastructure*
Substances
-
Macromolecular Substances
-
Recombinant Proteins
-
tau Proteins
-
Calcium-Calmodulin-Dependent Protein Kinases
-
CDC2 Protein Kinase
-
Glucose