Scorpion sting--the inflammatory dimension.
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In order to investigate factors influencing the discomfort caused by the injection of different lignocaine preparations, a randomized, double-blind comparison of paired injections was performed in 32 patients. In all subjects 2% plain lignocaine was found to be more painful than 0.5% plain lignocaine. Lignocaine with adrenaline 1:200,000 was found to be significantly more painful than plain lignocaine. The presence of sodium metabisulphite (the antioxidant in commercial adrenalized lignocaine) significantly increased the discomfort. Neutralization of acidic 0.5% lignocaine (pH 4.7) reduced the discomfort caused in 44% of patients, but this was not statistically significant.
IgE antibody reactivities to the venoms of Myrmecia pilosula, Myrmecia nigrocincta, Myrmecia tarsata, Myrmecia pyriformis, Myrmecia simillima and Myrmecia gulosa have been identified in sera from subjects allergic to ant venom. Sera with IgE reactivity to only a single Myrmecia venom most often recognize M. pilosula venom although all six venoms appear capable of inducing IgE antibodies. The six different Myrmecia venoms were electrophoretically separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Western blotted to nitrocellulose and probed with sera from ant venom-allergic subjects. Four to six IgE-binding components ranging in size from 2 to 25 kDa were identified in each of the venoms. Similarities in molecular weights of the IgE-binding components exist and close taxonomic relationships between the species suggest that common or similar peptides may be present in the different venoms.
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Because of the lack of objective signs, the phenomenon of sensitive skin is hard to document. The measurement of the skin pH variations in the nasolabial fold, and on the forearm, after a single application of lactic acid on a preselected sensitive skin population, versus a control one, is proposed as a useful test to detect this kind of population.
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Signaling proteins can be regulated by their interactions with other proteins and phospholipids. As Fawcett and Pawson discuss in their Perspective, activation of the N-WASP protein (which coordinates formation of actin filaments) is far more complex, depending on the interaction of N-WASP with both a protein and a phospholipid. The authors explain new results (Prehoda et al.) demonstrating that cooperative binding of the phospholipid PIP2 and the small GTPase Cdc42 to N-WASP results in its activation. The Arp2/3 complex is then able to bind to N-WASP and to proceed with its job of initiating the assembly of actin monomers into actin filaments.