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The anionic amphiphile SDS is an antagonist for the human neutrophil formyl peptide receptor 1.

Artikel i vetenskaplig tidskrift
Författare Fredrik Bergh Thorén
Jennie Karlsson
Claes Dahlgren
Huamei Forsman
Publicerad i Biochemical pharmacology
Volym 80
Nummer/häfte 3
Sidor 389-95
ISSN 1873-2968
Publiceringsår 2010
Publicerad vid Institutionen för medicin, avdelningen för reumatologi och inflammationsforskning
Institutionen för biomedicin, avdelningen för infektionssjukdomar
Sidor 389-95
Språk en
Länkar dx.doi.org/10.1016/j.bcp.2010.04.00...
Ämnesord Anions, Dose-Response Relationship, Drug, Humans, Neutrophil Activation, drug effects, physiology, Neutrophils, drug effects, metabolism, Protein Binding, drug effects, physiology, Receptors, Formyl Peptide, antagonists & inhibitors, metabolism, Sodium Dodecyl Sulfate, chemistry, pharmacology
Ämneskategorier Immunbiologi

Sammanfattning

The anionic amphiphil sodium dodecyl sulfate (SDS) is commonly used to activate the superoxide-generating NADPH-oxidase complex in cell-free systems, but very little is known about the effects of SDS on intact cells. It was, however, recently shown that SDS causes a translocation and an activation of Rac (a small G-protein) in intact cells, but this signal is not in its own sufficient to activate the oxidase (Nigorikawa et al. (2004) [1]). We found that SDS acted as an antagonist for FPR1, one of the neutrophil members of the formyl peptide receptor family. Accordingly, SDS reduced superoxide anion production induced by the chemoattractant formylmethionyl-leucyl-phenylalanine (fMLF). The receptor specificity of SDS was fairly high, but the concentration range in which it worked was narrow. The length of the carbohydrate chain as well as the charge of the molecule was of importance for the antagonistic effects. Signaling through FPR2, a closely related receptor also expressed in neutrophils, was not inhibited by SDS. On the contrary, the response induced by the FPR2-specific agonist WKYMVM was primed by SDS. The precise mechanism behind the primed state is not known, but might be related to the effects earlier described for SDS on the small G-protein Rac, that is of importance for a proper transduction of the down-stream signals from the occupied receptor.

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