Creatine-supplemented diet extends Purkinje cell survival in spinocerebellar ataxia type 1 transgenic mice but does not prevent the ataxic phenotype

Neuroscience. 2001;103(3):713-24. doi: 10.1016/s0306-4522(01)00017-3.

Abstract

It is not known why expression of a protein with an expanded polyglutamine region is pathogenic in spinocerebellar ataxia, Huntington's disease and several other neurodegenerative diseases. Dietary supplementation with creatine improves survival and motor performance and delays neuronal atrophy in the R6/2 transgenic mouse model of Huntington's disease. These effects may be due to improved energy and calcium homeostasis, enhanced presynaptic glutamate uptake, or protection of mitochondria from the mitochondrial permeability transition. We tested the effects of a 2% creatine-supplemented diet and treatment with taurine-conjugated ursodeoxycholic acid, a bile constituent that can inhibit the mitochondrial permeability transition, on ataxia and Purkinje cell survival in a transgenic model of spinocerebellar ataxia type 1. After 24 weeks, transgenic mice on the 2% creatine diet had cerebellar phosphocreatine levels that were 72.5% of wildtype controls, compared to 26.8% in transgenic mice fed a control diet. The creatine diet resulted in maintenance of Purkinje cell numbers in these transgenic mice at levels comparable to wildtype controls, while transgenic mice fed a control diet lost over 25% of their Purkinje cell population. Nevertheless, the ataxic phenotype was neither improved nor delayed. Repeated s.c. ursodeoxycholic acid injections markedly elevated ursodeoxycholic acid levels in the brain without adverse effects, but provided no improvement in phenotype or cell survival in spinocerebellar ataxia type 1 mice. These results demonstrate that preserving neurons from degeneration is insufficient to prevent a behavioral phenotype in this transgenic model of polyglutamine disease. In addition, we suggest that the means by which creatine mitigates against the neurodegenerative effects of an ataxin-1 protein containing an expanded polyglutamine region is through mechanisms other than stabilization of mitochondrial membranes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Ataxin-1
  • Ataxins
  • Bile Acids and Salts / metabolism
  • Cell Count
  • Cell Survival / drug effects
  • Cerebellum / metabolism
  • Creatine / metabolism
  • Creatine / pharmacology*
  • Dietary Supplements*
  • Gait / drug effects
  • Humans
  • Injections
  • Mice
  • Mice, Transgenic / genetics
  • Motor Activity / drug effects
  • Nerve Tissue Proteins / genetics
  • Nuclear Proteins / genetics
  • Phenotype
  • Phosphocreatine / metabolism
  • Purkinje Cells / pathology
  • Purkinje Cells / physiology*
  • Reference Values
  • Spinocerebellar Ataxias / genetics
  • Spinocerebellar Ataxias / pathology
  • Spinocerebellar Ataxias / physiopathology*
  • Taurine / pharmacology
  • Ursodeoxycholic Acid / pharmacology

Substances

  • ATXN1 protein, human
  • Ataxin-1
  • Ataxins
  • Atxn1 protein, mouse
  • Bile Acids and Salts
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Phosphocreatine
  • Taurine
  • Ursodeoxycholic Acid
  • Creatine