Colocalization of parvalbumin and calbindin D-28k in neurons including chandelier cells of the human temporal neocortex

J Chem Neuroanat. 1997 Mar;12(3):165-73. doi: 10.1016/s0891-0618(96)00191-3.

Abstract

Chandelier cells are cortical GABAergic interneurons with a unique synaptic specificity enabling them to exert a strong inhibitory influence on pyramidal cells. By using immunocytochemistry for the calcium-binding protein calbindin D-28k in the human temporal neocortex, we have found numerous immunoreactive processes that were identified as chandelier cell axon terminals. This was a striking find since in previous immunocytochemical studies of the primate neocortex, chandelier cell axon terminals had been shown to be immunoreactive for another calcium-binding protein, parvalbumin, and colocalization studies indicate that parvalbumin and calbindin are present in almost completely separate neuronal populations. Here, we present double-label immunofluorescence experiments showing that parvalbumin and calbindin immunoreactivities are colocalized in certain neurons that include a subpopulation of chandelier cells whose cell bodies are located mainly in layers V and VI of the human temporal neocortex. The results suggest a selective laminar distribution of neurochemical subtypes of chandelier cells which is a peculiar feature of the organization of the human neocortex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Adult
  • Calbindins
  • Fluorescent Antibody Technique, Direct
  • Humans
  • Immunohistochemistry
  • Neurons / enzymology
  • Neurons / metabolism*
  • Parvalbumins / metabolism*
  • Presynaptic Terminals / physiology
  • Presynaptic Terminals / ultrastructure
  • S100 Calcium Binding Protein G / metabolism*
  • Temporal Lobe / cytology
  • Temporal Lobe / enzymology
  • Temporal Lobe / metabolism*

Substances

  • Calbindins
  • Parvalbumins
  • S100 Calcium Binding Protein G