Microvillus inclusion disease: a genetic defect affecting apical membrane protein traffic in intestinal epithelium

Traffic. 2000 Jan;1(1):76-83. doi: 10.1034/j.1600-0854.2000.010111.x.

Abstract

The striking similarities between microvillus inclusions (MIs) in enterocytes in microvillus inclusion disease (MID) and vacuolar apical compartment in tissue culture epithelial cells, led us to analyze endoscopic biopsies of duodenal mucosa of a patient after the samples were used for diagnostic procedures. Samples from another patient with an unrelated disease were used as controls. The MID enterocytes showed a decrease in the thickness of the apical F-actin layer, and normal microtubules. The immunofluorescence analysis of the distribution of five apical membrane markers (sucrase isomaltase, alkaline phosphatase, NHE-3 Na+/H+ exchanger, cGMP-dependent protein kinase, and cystic fibrosis trans-membrane conductance regulator), showed low levels of these proteins in their standard localization at the apical membrane as compared with normal duodenal epithelium processed in parallel. Instead, four of these markers were found in a diffuse distribution in the apical cytoplasm, below the terminal web (as indicated by co-localization with F-actin and cytokeratin 19), and in MIs as well. The basolateral protein Na(+)-K+ATPase, in contrast, was normally localized. These results support the hypothesis that MID may represent the first genetic defect affecting apical membrane traffic, possibly in a late step of apical exocytosis.

Publication types

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

MeSH terms

  • Actins / analysis*
  • Cell Membrane / chemistry
  • Cell Membrane / ultrastructure
  • Cell Polarity
  • Cells, Cultured
  • Child, Preschool
  • Duodenal Diseases / genetics
  • Duodenal Diseases / metabolism
  • Duodenal Diseases / pathology*
  • Enterocytes / ultrastructure*
  • Female
  • Humans
  • Inclusion Bodies / chemistry
  • Inclusion Bodies / ultrastructure*
  • Keratins / analysis
  • Membrane Proteins / analysis*
  • Microvilli / chemistry
  • Microvilli / ultrastructure*
  • Protein Transport
  • Secretory Vesicles / chemistry
  • Secretory Vesicles / ultrastructure

Substances

  • Actins
  • Membrane Proteins
  • Keratins