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Gäde, G. et al.

Gäde, Lee, Goldsworthy, Kellner,

Potencies of naturally-occurring AKH/RPCH peptides in Locusta migratoria in the acetate uptake assay in vitro and comparison with their potencies in the lipid mobilisation assay in vivo.

The biological potencies of a number of naturally-occurring octa- and decapeptides of the large AKH/RPCH family of peptides were determined in Locusta migratoria using the lipid-mobilising assay in vivo and the acetate uptake assay in vitro. The most potent of the newly-tested peptides in the in vitro assay, Phl-CC, differs from the endogenous major locust peptide, Lom-AKH-I, only by an exchange of serine versus threonine at position 10. However, the most active peptide in the in vitro assay remains Lom-AKH-III. At the other extreme is the peptide Mem-CC which contains a tyrosine residue at position 4 rather than the more typical phenylalanine. This peptide is over 20,000 times less potent than Lom-AKH-III in the in vitro assay, and also results in an unusual dose-response curve in the in vivo assay. Only a few peptides are approximately equipotent in both assays, but mostly the bioanalogues have a higher potency in vitro. The majority of them are 2- to 10-fold more potent in vitro, but Ani-AKH and Lom-AKH-III are 19- and 48-fold more potent. The results are discussed in relation to either the actions of proteases or of possible preferential binding of different receptors involved in the different assays.[1]

References

Potencies of naturally-occurring AKH/RPCH peptides in Locusta migratoria in the acetate uptake assay in vitro and comparison with their potencies in the lipid mobilisation assay in vivo. Gäde, G., Lee, M.J., Goldsworthy, G.J., Kellner, R. Acta. Biol. Hung. (2000) [Pubmed]

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