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• W2016046404 abstract "Abstract Protein phosphorylation was analysed in neural tissue of adult crickets (Acheta domesticus). After in vitro phosphorylation of 15,000 g supernatants and pellets, endogenous substrates for several protein kinases were separated on SDS-PAGE. Ten polypeptides with apparent molecular weights ranging from 89.5 to 20 kDa were phosphorylated in a cyclic nucleotide-dependent manner; several (70, 42, 41 and 34.5 kDa peptides) were observed in both fractions. A strong enhancement of [32P] incorporation into 57, 50, 37 and 28.5 kDa peptides was observed in the presence of Ca2+ and calmodulin. In the presence of stimulators of protein kinase C (Ca2+, PMA, phosphatidylserine), the phosphorylation of several peptides (34, 29.5, 24.5, 22, 20 and 17.5 kDa) was stimulated. Gangliosides were also demonstrated to be able to modulate the phosphorylation of several peptides, especially as 39 kDa peptide in the particulate fraction. Polyamines stimulated the phosphorylation of two peptides (53.5 and 37.5 kDa), one of which was specific for the neural tissue cytosol (53.5 kDa). By contrast, the phosphorylation of three high molecular weight peptides (207, 128 and 108 kDa) present in the supernatant and pellet decreased in the presence of polyamines. These findings were compared to results obtained in other insects." @default.
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• W2016046404 date "1994-04-01" @default.
• W2016046404 modified "2023-09-25" @default.
• W2016046404 title "Protein phosphorylation in the neural tissue of an adult cricket (Acheta domesticus): Endogenous substrates and their protein kinases" @default.
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• W2016046404 doi "https://doi.org/10.1016/0022-1910(94)90069-8" @default.
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