Mosquito larvicidal activity of aqueous extracts of long pepper (Piper retrofractum vahl) from Thailand.

Aqueous extracts of nine medicinal plants were bioassayed against larvae of Culex quinquefasciatus Say and Aedes aegypt (L.). Among these plants, the long pepper, Piper retrofractum Vahl (Piperaceae), showed the highest level of activity against mosquito larvae. To gain more information on larvicidal activity of P. retrofractum, fresh fruits of this plant were extracted in water and the extracts made into powder and bioassayed against 3rd and 4th instar larvae of Cx. quinquefasciatus and Ae. aegypti in the laboratory. Extracts of unripe (001/3) and ripe (002/3 and 001/4) fruits showed different levels of activity against Cx. quinquefasciatus larvae. Extracts 001/3 and 002/3 were equi-toxic to a Bacillus sphaericus resistant and susceptible strains, both from Thailand. The ripe fruit extract 002/3 was somewhat more active against Ae. aegypti than Cx. quinquefasciatus. Another ripe fruit extract (001/4) was much more toxic to both mosquito species. Diluted solutions of the solid extract (002/3) in distilled water lost their larvicidal activity upon aging. Loss of activity at 25 degrees C was greater than that stored at 4 degrees C, and greater in water than in acetone solution.     

Modification of plasma membrane protein cysteine residues by ADP-ribose in vivo

Proteins can be post-translationally modified by ADP-ribose. Previously, two classes of ADP-ribosyl protein linkages have been detected in vivo which have chemical properties indistinguishable from ADP-ribosyl arginine and ADP-ribosyl glutamate or aspartate. Reported here is the detection of a third class of endogenous ADP-ribosyl protein linkage. This class is chemically indistinguishable from ADP-ribose linked to cysteine residues by a thioglycosidic bond. The distribution of ADP-ribosyl cysteine residues was studied in subcellular fractions of rat liver. Proteins modified on cysteine were detected only in the plasma membrane fraction. Pertussis toxin is known to disrupt signal transduction of ADP-ribosylation of cysteine residues of plasma membrane GTP binding proteins. The results described here raise the interesting possibility that the endogenous modification of plasma membrane protein cysteine residues may be involved in signal transduction.