학술논문

Using Inhibitors to Investigate the Involvement of Cell Signaling in Predation by Marine Phagotrophic Protists
Document Type
Report
Author abstract
Source
Journal of Eukaryotic Microbiology. Jan-Feb, 2008, Vol. 55 Issue 1, p18, 4 p.
Subject
Company legal issue
Predation (Biology) -- Investigations
Language
English
ISSN
1066-5234
Abstract
To purchase or authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1111/j.1550-7408.2007.00297.x Byline: AARON J. HARTZ (a), BARRY F. SHERR (a), EVELYN B. SHERR (a) Keywords: Cell signaling; chemosensory response; heterotrophic protist; Oxyrrhis marina; prey ingestion; Uronema sp. Abstract: ABSTRACT. Phagotrophic protists are major consumers of microbial biomass in aquatic ecosystems. However, biochemical mechanisms underlying prey recognition and phagocytosis by protists are not well understood. We investigated the potential roles of cell signaling mechanisms in chemosensory response to prey, and in capture of prey cells, by a marine ciliate (Uronema sp.) and a heterotrophic dinoflagellate (Oxyrrhis marina). Inhibition of protein kinase signal transduction biomolecules caused a decrease in both chemosensory response and predation. Inhibition of G-protein coupled receptor signaling pathways significantly decreased chemosensory response but had no effect on prey ingestion. Inhibitor compounds did not appear to affect general cell health, but had a targeted effect. These results support the idea that cell signaling pathways known in other eukaryotic organisms are involved in feeding behavior of free-living protists. Author Affiliation: (a)College of Oceanic and Atmospheric Sciences, Oregon State University, Corvallis, Oregon 97331 Article History: Received: 06/19/07, 08/31/07, 10/02/07; accepted: 10/06/07 Article note: Corresponding Author: A. Hartz, College of Oceanic and Atmospheric Sciences, Oregon State University, 104 Ocean Admin, Corvallis, OR 97331-Telephone number: +1 541 737 2359; FAX number: +1 541 737 2064; e-mail: ahartz@coas.oregonstate.edu