Loss of high affinity neurotensin receptors in substantia nigra from parkinsonian subjects

Biochem Biophys Res Commun. 1984 Nov 30;125(1):395-404. doi: 10.1016/s0006-291x(84)80381-2.

Abstract

Monoiodo [125I-Tyr3]-Neurotensin binding was studied in post mortem substantia nigra from 17 control and 15 parkinsonian subjects. Binding to individual homogenates was decreased by 58%, 49% and 26% at 0.36, 1.4, 5.5 M(-9) concentration of ligand, respectively. Saturation analysis using pooled substantia nigra demonstrated an almost complete loss of the high affinity component of the neurotensin receptor complex, yielding a 24% loss of the total binding capacity, with no alteration of the low affinity component. Similarly an important loss of binding was observed in monoiodo[125I-Tyr3]-Neurotensin autoradiograms of two substantia nigra from parkinsonian subjects. These results support the hypothesis of neurotensin receptors occurring on dopamine cell bodies and/or dendrites in human substantia nigra. Role of neurotensin may be of importance in the regulation of dopamine pathway involved in parkinsonism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Animals
  • Humans
  • Male
  • Neurotensin / metabolism*
  • Parkinson Disease / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Receptors, Neurotensin
  • Receptors, Neurotransmitter / metabolism*
  • Substantia Nigra / metabolism*
  • Thermodynamics
  • Time Factors

Substances

  • Receptors, Neurotensin
  • Receptors, Neurotransmitter
  • Neurotensin