Entamoeba histolytica: Ultrastructural localization of Ca2+-dependent nucleotidases

Seiki Kobayashi, Tsutomu Takeuchi, Keizo Asami, Tatsushi Fujiwara

Research output: Contribution to journalArticle

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Abstract

Localization of nucleotidases dependent on Ca2+ was investigated cytochemically in axenically cultivated trophozoites of Entamoeba histolytica, strain HM-1:IMSS, with an electron microscope. Ca2+-dependent ATPase (EC 3.6.1.3) activity was found on the plasma membrane and on the inner surface of the limiting membrane of a few cytoplasmic vacuoles. Ca2+-dependent ADPase, Ca2+-dependent thiamine pyrophosphatase, and acid phosphatase (EC 3.1.3.2) activities were detected on the inner surface of the limiting membrane of most of the cytoplasmic vacuoles but not on the plasma membrane. Cytoplasmic vacuoles with these enzymatic activities seemed similar in morphological characteristics. Moreover, the reaction product formed by Ca2+-dependent ADPase, Ca2+-dependent thiamine pyrophosphatase and acid phosphatase was demonstrable on the inner surface of the limiting membrane of vacuoles containing ingested red blood cells. The reaction product formed by these enzymes was also observed on the periphery of ingested red blood cells. The findings suggest that cytoplasmic vacuoles with these enzymatic activities are lysosomal in nature, probably phagolysosomes; therefore, the enzymes appear to be at least partially associated with primary lysosomes of E. histolytica.

Original languageEnglish
Pages (from-to)202-212
Number of pages11
JournalExperimental Parasitology
Volume54
Issue number2
DOIs
Publication statusPublished - 1982 Oct

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Keywords

  • ATPase (EC 3.6.1.3)
  • Acid phosphatase (EC 3.1.3.2)
  • Apyrase (EC 3.6.1.5)
  • Ca-dependence
  • Cytochemistry
  • Electron microscopy
  • Entamoeba histolytica
  • Lysosome
  • Membrane, plasma
  • Nucleoside diphosphatase (EC 3.6.1.6)
  • Protozoa, parasitic

ASJC Scopus subject areas

  • Parasitology
  • Immunology
  • Infectious Diseases

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