Calretinin-immunoreactive neocortical interneurons are unaffected in Alzheimer's disease

Neurosci Lett. 1993 Apr 2;152(1-2):145-8. doi: 10.1016/0304-3940(93)90504-e.


Recent studies have revealed that select neuronal populations may display a differential sensitivity to degeneration in Alzheimer's disease. For example, large pyramidal neurons have been shown to be vulnerable, whereas small, local circuit neurons appear to be resistant to the pathologic process. More significantly, interneurons that contain the calcium-binding proteins parvalbumin and calbindin are particularly resistant to degeneration in Alzheimer's disease. Using a polyclonal antibody to the calcium-binding protein calretinin, we analyzed the possible changes in the subset of interneurons containing this protein in two neocortical areas that are generally devastated in Alzheimer's disease. In the prefrontal cortex as well as in the inferior temporal cortex, we observed no difference in the density of calretinin-immunoreactive neurons in Alzheimer's disease brains as compared to control cases. Moreover, the cellular morphology of these neurons was well preserved in the Alzheimer's disease cases. These data suggest that calretinin-immunoreactive neurons, like other calcium-binding protein-containing interneurons, are resistant to degeneration in Alzheimer's disease. The results support the notion that the pathological process in Alzheimer's disease involves specific cellular populations sharing particular morphological and neurochemical characteristics. In addition, it is possible that the presence of calcium-binding proteins confers a certain degree of resistance to degeneration in specific neuronal subsets.

Publication types

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

MeSH terms

  • Aged
  • Aged, 80 and over
  • Alzheimer Disease / pathology*
  • Calbindin 2
  • Cerebral Cortex / pathology*
  • Humans
  • Interneurons / chemistry*
  • Interneurons / ultrastructure
  • Nerve Degeneration
  • Nerve Tissue Proteins / analysis*
  • S100 Calcium Binding Protein G / analysis*


  • CALB2 protein, human
  • Calbindin 2
  • Nerve Tissue Proteins
  • S100 Calcium Binding Protein G