Striatal neurons expressing full-length mutant huntingtin exhibit decreased N-cadherin and altered neuritogenesis

Hum Mol Genet. 2011 Jun 15;20(12):2344-55. doi: 10.1093/hmg/ddr127. Epub 2011 Mar 29.

Abstract

The expanded CAG repeat that causes striatal cell vulnerability in Huntington's disease (HD) encodes a polyglutamine tract in full-length huntingtin that is correlated with cellular [ATP] and [ATP/ADP]. Since striatal neurons are vulnerable to energy deficit, we have investigated, in Hdh CAG knock-in mice and striatal cells, the hypothesis that decreased energetics may affect neuronal (N)-cadherin, a candidate energy-sensitive adhesion protein that may contribute to HD striatal cell sensitivity. In vivo, N-cadherin was sensitive to ischemia and to the effects of full-length mutant huntingtin, progressively decreasing in Hdh(Q111) striatum with age. In cultured striatal cells, N-cadherin was decreased by ATP depletion and STHdh(Q111) striatal cells exhibited dramatically decreased N-cadherin, due to decreased Cdh2 mRNA and enhanced N-cadherin turnover, which was partially normalized by adenine supplementation to increase [ATP] and [ATP/ADP]. Consistent with decreased N-cadherin function, STHdh(Q111) striatal cells displayed profound deficits in calcium-dependent N-cadherin-mediated cell clustering and cell-substratum adhesion, and primary Hdh(Q111) striatal neuronal cells exhibited decreased N-cadherin and an abundance of immature neurites, featuring diffuse, rather than clustered, staining for N-cadherin and synaptic vesicle markers, which was partially rescued by adenine treatment. Thus, mutant full-length huntingtin, via energetic deficit, contributes to decreased N-cadherin levels in striatal neurons, with detrimental effects on neurite maturation, strongly suggesting that N-cadherin-mediated signaling merits investigation early in the HD pathogenic disease process.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenine
  • Adenosine Triphosphate / metabolism
  • Animals
  • Cadherins / metabolism*
  • Cell Adhesion / physiology
  • Cells, Cultured
  • Corpus Striatum / cytology*
  • Corpus Striatum / metabolism
  • DNA Primers / genetics
  • Electrophoresis, Polyacrylamide Gel
  • Gene Knock-In Techniques
  • Humans
  • Huntingtin Protein
  • Huntington Disease / metabolism*
  • Immunoblotting
  • Immunohistochemistry
  • Mice
  • Mutation / genetics
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Neurites / physiology*
  • Neurons / metabolism*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Reverse Transcriptase Polymerase Chain Reaction

Substances

  • Cadherins
  • DNA Primers
  • HTT protein, human
  • Huntingtin Protein
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Adenosine Triphosphate
  • Adenine