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Arylsulphatase in echinoderm immunocompetent cells.

C Canicatti1, A Miglietta

  • 1Department of Biology, University of Lecce, Italy.

The Histochemical Journal
|July 1, 1989
PubMed
Summary

Echinoderms possess Type II arylsulphatase enzymes within their coelomocytes, specifically in spherula and amoebocyte cells. This finding highlights a common cell type with granulocyte-like functions across various echinoderm species.

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Area of Science:

  • Marine Biology
  • Biochemistry
  • Cell Biology

Background:

  • Echinoderms, a diverse phylum of marine invertebrates, possess a unique coelomic fluid system involved in immune and physiological functions.
  • Arylsulphatases are enzymes that hydrolyze sulfate esters, playing roles in various biological processes.
  • Understanding the enzymatic composition of echinoderm coelomocytes is crucial for deciphering their immune mechanisms and cellular functions.

Purpose of the Study:

  • To biochemically and histochemically characterize arylsulphatase activity in the coelomocytes of various echinoderm species.
  • To identify the specific type(s) of arylsulphatase present and their cellular localization within echinoderms.
  • To investigate the potential functional implications of arylsulphatase in echinoderm cellular defense and physiology.

Main Methods:

  • Biochemical assays were performed on coelomocyte lysate preparations from seven different Echinodermata species to detect arylsulphatase activity.
  • Enzyme activity was assessed by measuring the hydrolysis of specific substrates.
  • Inhibitory effects of sulphite and sulphate ions were used to differentiate arylsulphatase types.
  • Histochemical staining techniques were employed to localize arylsulphatase activity within specific cell types, including spherula cells and amoebocytes.

Main Results:

  • Two distinct peaks of arylsulphatase activity were consistently detected in the coelomocyte lysates across all tested species.
  • The enzyme activity was significantly inhibited by sulphite and sulphate ions, confirming the presence of Type II arylsulphatase.
  • Histochemical analysis revealed arylsulphatase localization within the granules of spherula cells in multiple echinoderm species.
  • In echinoid species, the enzyme was also found to be present in amoebocytes.

Conclusions:

  • The study confirms the presence of Type II arylsulphatase in the coelomocytes of diverse echinoderm species.
  • Arylsulphatase is primarily localized in spherula cells, suggesting these cells possess granulocyte-like functions related to enzyme secretion.
  • The findings indicate a conserved cellular mechanism involving arylsulphatase in echinoderm immune responses or physiological processes.

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