Postnatal changes in TASK-1 and TREK-1 expression in rat brain stem and cerebellum

Neuroreport. 2004 Jun 7;15(8):1321-4. doi: 10.1097/01.wnr.0000127462.15985.dc.

Abstract

Developmental changes in expression of two-pore domain K+ channels, TASK-1 and TREK-1, were investigated in the juvenile (postnatal day 13; P13) and adult (P105) rat brain stem and cerebellum using immunohistochemistry. In the juvenile, extensive TASK-1-like immunoreactivity (TASK-1-LIR) was seen among glial cells in the white matter (e.g., radial glia), which showed marked reduction in the adult. In contrast, TASK-1-LIR in neurons including cerebellar Purkinje and granule cells, hypoglossal and facial motoneurons, and ventrolateral medulla neurons was increased in the adult. TASK-1-LIR in neuroglia surrounding peripheral axons of cranial nerves was persistent. TREK-1-LIR was similar between ages, although TREK-1-LIR was neuronal and present only in juvenile cerebellar external germinal layer. Present results suggest roles for TASK-1 and K+ homeostasis in neuro-glial interaction, neurogenesis, differentiation, migration, axon guidance, synaptogenesis and myelination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aging / metabolism
  • Animals
  • Animals, Newborn
  • Axons / metabolism
  • Brain Stem / cytology
  • Brain Stem / growth & development
  • Brain Stem / metabolism*
  • Cell Differentiation / physiology
  • Cell Membrane / metabolism
  • Cerebellum / cytology
  • Cerebellum / growth & development
  • Cerebellum / metabolism*
  • Cranial Nerves / cytology
  • Cranial Nerves / growth & development
  • Cranial Nerves / metabolism
  • Down-Regulation / physiology
  • Immunohistochemistry
  • Nerve Fibers, Myelinated / metabolism
  • Nerve Tissue Proteins
  • Neuroglia / cytology
  • Neuroglia / metabolism
  • Neuronal Plasticity / physiology
  • Neurons / cytology
  • Neurons / metabolism*
  • Potassium Channels / metabolism*
  • Potassium Channels, Tandem Pore Domain*
  • Rats
  • Rats, Wistar
  • Up-Regulation / physiology

Substances

  • Nerve Tissue Proteins
  • Potassium Channels
  • Potassium Channels, Tandem Pore Domain
  • potassium channel protein TREK-1
  • potassium channel subfamily K member 3