Adult spinal motoneurons remain viable despite prolonged absence of functional synaptic contact with muscle

Exp Neurol. 1993 Sep;123(1):147-56. doi: 10.1006/exnr.1993.1147.


Several rat medial gastrocnemius (MG) motor axons were allowed to regenerate into normally innervated muscle. Under these conditions, synapse formation is known to be prevented by the existence of the original innervation of the host muscle. A study was made of the ability of the implanted spinal motoneurons to acquire and retrogradely transport horseradish peroxidase (HRP) injected into the host muscle at various postoperative intervals. HRP-labeled MG motoneurons on the implanted side were observed at postoperative intervals as long as 290 days. A comparison of the number of labeled MG motoneurons on the implanted side versus the number on the unoperated, control side indicated no significant differences. At all investigated postoperative intervals except the earliest (7 DPO), a significant decrease in the mean MG motoneuron soma cross-sectional area was observed relative to the unoperated, control side. Analysis of labeled motoneuron size distributions showed that postoperative atrophy of larger, presumably alpha, motoneurons occurred at a significantly faster rate than in smaller, presumably gamma, motoneurons. These results demonstrate that axotomized adult spinal motoneurons survive and remain viable for prolonged periods when denied the opportunity to reinnervate muscle but do so in an atrophied state. The results indicate further that alpha and gamma motoneurons differ quantitatively in their responses to peripheral axotomy.

Publication types

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

MeSH terms

  • Animals
  • Axons / physiology
  • Cell Count
  • Cell Survival
  • Denervation
  • Female
  • Horseradish Peroxidase
  • Male
  • Motor Neurons / cytology
  • Motor Neurons / physiology*
  • Muscles / innervation*
  • Rats
  • Spinal Cord / cytology
  • Spinal Cord / physiology*
  • Synapses / physiology*
  • Time Factors


  • Horseradish Peroxidase