Converging molecular pathways in human neural development and degeneration

Neurosci Res. 2010 Mar;66(3):330-2. doi: 10.1016/j.neures.2009.11.012. Epub 2009 Dec 2.

Abstract

Animal studies suggest that phosphorylation of microtubule-associated protein tau is a physiological way of destabilizing axons in the developing brain, promoting synaptic plasticity, while in the adult human brain tau phosphorylation is a specific sign of Alzheimer's disease. We here show, for the first time, that newborn human infants have extremely high levels of phosphorylated tau in their cerebrospinal fluid, and that these levels decrease during the first years of life. Tau phosphorylation in Alzheimer's disease may be a physiological response to Alzheimer-associated synaptotoxicity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Aging / cerebrospinal fluid*
  • Amyloid beta-Protein Precursor / cerebrospinal fluid
  • Axons / physiology
  • Biomarkers / cerebrospinal fluid
  • Child
  • Child Development*
  • Child, Preschool
  • Female
  • Humans
  • Infant
  • Infant, Newborn
  • Infant, Premature / cerebrospinal fluid
  • Male
  • Phosphorylation
  • Protease Nexins
  • Protein Isoforms / cerebrospinal fluid
  • Receptors, Cell Surface
  • tau Proteins / cerebrospinal fluid*
  • tau Proteins / genetics

Substances

  • Amyloid beta-Protein Precursor
  • Biomarkers
  • MAPT protein, human
  • Protease Nexins
  • Protein Isoforms
  • Receptors, Cell Surface
  • tau Proteins