Ultrastructural cytochemistry of non-specific esterase in murine peritoneal macrophages

L H Rademakers, W T Van Blokland, J F De Frankrijker, R A De Weger, P I Compier-Spies

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Non-specific esterase (NSE) activity was demonstrated in glutaraldehyde-fixed monolayers of murine peritoneal macrophages. Using 2-naphthylthiol acetate (NTA) as substrate and Fast Blue BB as coupling agent a strong osmiophilic reaction product was obtained. The reaction product was observed as electron-dense dots covering cisterns of the rough endoplasmic reticulum, Golgi saccules and vesicles, or as large aggregates in lysosomes. Using alpha-naphthyl butyrate (ANB) as substrate and hexazotized pararosaniline as coupling agent the osmiophilic reaction product was observed extracellularly on the plasma membrane as an electron-dense continuous layer, whereas intracytoplasmic staining of lysosomes was rare. Substitution of the coupling agents in the respective media resulted in a slight reaction with the ANB medium whereas with the NTA medium reaction product was observed only in lysosomal structures. The substrate specificity of the different types of esterases was confirmed after isoelectric focusing on thin-layer polyacrylamide gels. The results indicate that in murine peritoneal macrophages different types on NSE are detected with NTA and ANB, having distinct ultrastructural localizations.

Original languageEnglish
Pages (from-to)301-8
Number of pages8
JournalThe Histochemical journal
Volume21
Issue number5
Publication statusPublished - 1989

Keywords

  • Animals
  • Cell Membrane
  • Diazonium Compounds
  • Esterases
  • Histocytochemistry
  • Isoelectric Focusing
  • Macrophages
  • Mice
  • Mice, Inbred DBA
  • Naphthols
  • Peritoneum
  • Rosaniline Dyes
  • Sodium Fluoride
  • Toluidines

Fingerprint

Dive into the research topics of 'Ultrastructural cytochemistry of non-specific esterase in murine peritoneal macrophages'. Together they form a unique fingerprint.

Cite this