Close menu

SURE

Sunderland Repository records the research produced by the University of Sunderland including practice-based research and theses.

Effect of Vibrio parahaemolyticus haemolysin on human erythrocytes.

Lang, Philipp A, Kaiser, Stephanie, Mysina, Svetlana, Birka, Christina, Weinstock, Christof, Northoff, Hinnak, Wieder, Thomas, Lang, Florian and Huber, Stephan M (2004) Effect of Vibrio parahaemolyticus haemolysin on human erythrocytes. Cellular microbiology, 6 (4). pp. 391-400. ISSN 1462-5814

Item Type: Article

Abstract

Haemolysin Kanagawa, a toxin from Vibrio parahaemolyticus, is known to trigger haemolysis. Flux studies indicated that haemolysin forms a cation channel. In the present study, channel properties were elucidated by patch clamp and functional significance of ion fluxes by fluorescence-activated cell sorting (FACS) analysis. Treatment of human erythrocytes with 1 U ml-1 haemolysin within minutes induces a non-selective cation permeability. Moreover, haemolysin activates clotrimazole-sensitive K+ channels, pointing to stimulation of Ca2+-sensitive Gardos channels. Haemolysin (1 U ml-1) leads within 5 min to slight cell shrinkage, which is reversed in Ca2+-free saline. Erythrocytes treated with haemolysin (0.1 U ml-1) do not undergo significant haemolysis within the first 60 min. Replacement of extracellular Na+ with NMDG+ leads to slight cell shrinkage, which is potentiated by 0.1 U ml-1 haemolysin. According to annexin binding, treatment of erythrocytes with 0.1 U ml-1 haemolysin leads within 30 min to breakdown of phosphatidylserine asymmetry of the cell membrane, a typical feature of erythrocyte apoptosis. The annexin binding is significantly blunted at increased extracellular K+ concentrations and by K+ channel blocker clotrimazole. In conclusion, haemolysin Kanagawa induces cation permeability and activates endogenous Gardos K+ channels. Consequences include breakdown of phosphatidylserine asymmetry, which depends at least partially on cellular loss of K+.

Full text not available from this repository.

More Information

Depositing User: Svetlana Mysina

Identifiers

Item ID: 10026
ISSN: 1462-5814
URI: http://sure.sunderland.ac.uk/id/eprint/10026

Users with ORCIDS

Catalogue record

Date Deposited: 08 Oct 2018 09:11
Last Modified: 09 Oct 2018 11:16

Contributors

Author: Philipp A Lang
Author: Stephanie Kaiser
Author: Svetlana Mysina
Author: Christina Birka
Author: Christof Weinstock
Author: Hinnak Northoff
Author: Thomas Wieder
Author: Florian Lang
Author: Stephan M Huber

Subjects

Sciences > Biomedical Sciences
Sciences

Actions (login required)

View Item (Repository Staff Only) View Item (Repository Staff Only)