Crystalloid inclusions in brain macrophages and hemopoietic tissue in GFAP-IL3 mice resemble inclusions identified in multiple sclerosis

Ultrastruct Pathol. 1999 Sep-Oct;23(5):285-97. doi: 10.1080/019131299281437.

Abstract

Crystalloid inclusions or "pole bodies" observed in brain macrophages in human demyelinating disease represent a morphological enigma. Similar inclusions were detected in brain macrophages from the GFAP-IL3 mouse, a transgenic murine model for macrophage mediated demyelination. Mice also showed inclusions in hematopoietic tissue. They appear to be related to phagocytosis and secretion, respectively, as evidenced by the fact that in phagocytosing cells they often merged with lysozomes and that affected cells showed empty channels open to the interstitium. Based on ultrastructural and immunolocalization studies using chaperonin-10, lysozyme, and cathepsin the authors suggest that these inclusions are consistent with phagocytosis-related secretory products. This study may provide insight into the nature and significance of similar macrophage inclusions recently identified in multiple sclerosis.

Publication types

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

MeSH terms

  • Animals
  • Bone Marrow Cells / metabolism
  • Bone Marrow Cells / ultrastructure*
  • Cathepsins / metabolism
  • Cerebellum / metabolism
  • Cerebellum / pathology*
  • Chaperonin 10 / metabolism
  • Crystallization
  • Disease Models, Animal
  • Glial Fibrillary Acidic Protein / biosynthesis*
  • Glial Fibrillary Acidic Protein / genetics
  • Inclusion Bodies / metabolism
  • Inclusion Bodies / ultrastructure*
  • Interleukin-3 / biosynthesis*
  • Interleukin-3 / genetics
  • Macrophages / metabolism
  • Macrophages / ultrastructure*
  • Mice
  • Mice, Transgenic
  • Multiple Sclerosis / etiology
  • Multiple Sclerosis / metabolism
  • Multiple Sclerosis / pathology*
  • Muramidase / metabolism

Substances

  • Chaperonin 10
  • Glial Fibrillary Acidic Protein
  • Interleukin-3
  • Muramidase
  • Cathepsins