Lysozyme acts as a chemorepellent and secretagogue in Paramecium by activating a novel receptor-operated Ca++ conductance

T. M. Hennessey, M. Y. Kim, Birgit H. Satir

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Using combined intracellular recordings and behavioral bioassays, it was found that lysozyme has two different effects in Paramecium, depending upon the concentrations used. At low concentrations (0.5 n m to 1.0 μm) it acts as an effective chemorepellent that causes reliable electrophysiological changes. Lysozyme-induced somatic depolarizations, isolated by blocking K+ channels with Cs-TEA, showed concentration dependencies that were well correlated with chemorepulsion. Ion dependency experiments showed that these were Ca++ based depolarizations. Addition of either Na+ or Mg++ improves chemorepulsion by providing additional depolarizations. Both the depolarizations and chemorepulsion were blocked by 10 μm neomycin, suggesting that the depolarization is necessary for this chemosensory transduction event. At higher concentrations (100 μm), lysozyme is a secretagogue. A transient inward current, recorded in Ca++ alone solutions with Cs-TEA present, was seen in response to high lysozyme concentrations. The amplitude of this inward current was well correlated with exocytosis. Addition of neomycin (1.0 m m) eliminated both the inward current and exocytosis, suggesting a causal relationship. Neither amiloride or W-7, compounds previously suggested to affect the electrophysiological responses to secretagogues, had any significant effects. The mucopolysaccharide hydrolysis activity of lysozyme was not required for any of these responses. We propose that Paramecium have a high affinity receptor on the body plasma membrane that responds to either lysozyme or a related compound to cause an increase in a novel body Ca++ conductance. This receptor-operated Ca++ conductance causes membrane depolarization and chemorepulsion at low concentrations and triggers a sufficient Ca++ influx at high concentrations to cause exocytosis.

Original languageEnglish (US)
Pages (from-to)13-25
Number of pages13
JournalThe Journal of Membrane Biology
Volume148
Issue number1
DOIs
StatePublished - Nov 1995

Fingerprint

Paramecium
Muramidase
Exocytosis
Neomycin
Amiloride
Glycosaminoglycans
Biological Assay
Hydrolysis
Cell Membrane
Ions
Membranes

Keywords

  • Calcium
  • Chemosensory transduction
  • Exocytosis
  • Ion channels
  • Lysozyme
  • Paramecium
  • Receptors

ASJC Scopus subject areas

  • Physiology
  • Cell Biology
  • Biophysics

Cite this

Lysozyme acts as a chemorepellent and secretagogue in Paramecium by activating a novel receptor-operated Ca++ conductance. / Hennessey, T. M.; Kim, M. Y.; Satir, Birgit H.

In: The Journal of Membrane Biology, Vol. 148, No. 1, 11.1995, p. 13-25.

Research output: Contribution to journalArticle

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