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

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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+.

Item Type: Article
Subjects: Sciences > Biomedical Sciences
Depositing User: Svetlana Mysina
Date Deposited: 08 Oct 2018 09:11
Last Modified: 09 Oct 2018 11:16
URI: http://sure.sunderland.ac.uk/id/eprint/10026

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