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Journal ArticleDOI

Structure and biosynthesis of toxins from blue-green algae (cyanobacteria)

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TLDR
Nearly 30 new microcystins have been isolated in the laboratory from cyanobacteria species and their structures assigned, largely employing tandem FAB mass spectrometry (FABMS/CID/MS) and numerous analogs identified or synthesized allow the identification of important parameters in a structure-activity relationship study.
Abstract
Microcystis andNodularia species produce cyclic hepta- and pentapeptides, microcystins and nodularin, respectively, both containing the same unusual C20 amino acid, abbreviated Adda. Biosynthesis of nodularin fromNodularia and especially of Adda employs a pathway similar to that employed byMicrocystis for producting microcystins. Nearly 30 new microcystins have been isolated in our laboratory from cyanobacteria species and their structures assigned, largely employing tandem FAB mass spectrometry (FABMS/CID/MS). Acyclic peptides, some of them presumed precursors of nodularin and microcystins, have now been isolated and characterized. The numerous analogs identified or synthesized allow the identification of important parameters in a structure-activity relationship study.

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References
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Journal ArticleDOI

Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants.

TL;DR: The cyclic heptapeptide, microcystin‐LR, inhibits protein phosphatases 1 (PP1) and 2A (PP2A) with K i, values below 0.1 nM, and this results are strikingly similar to those obtained with the tumour promoter okadaic acid.
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Liver tumor promotion by the cyanobacterial cyclic peptide toxin microcystin-LR.

TL;DR: In this paper, the authors showed that microcystin-LR, applied below the acute toxicity level, dose-dependently increases the number and percentage area of positive foci for the placental form of glutathioneS-transferase in rat liver, which was initiated with diethylnitrosamine.
Journal ArticleDOI

Inhibition of protein phosphatases by microcystins and nodularin associated with hepatotoxicity.

TL;DR: The hepatotoxicity of microcystins and nodularin may result from inhibition of protein phosphatases and the increase of phosphoproteins, which is similar to that of okadaic acid in the nanomolar range of concentration.
Journal ArticleDOI

Characterization of microcystin-LR, a potent inhibitor of type 1 and type 2A protein phosphatases.

TL;DR: Microcystin-LR inhibited the activity of both type 1 and type 2A phosphatases greater than 10-fold more potently than okadaic acid under the same conditions and may prove to be a useful probe for the study and identification cellular processes which are mediated by protein phosphatase.

Liver tumor promotion by the cyanobacterial cyclic peptide toxin microcystin-LR. J Cancer Res Clin Oncol

TL;DR: It is shown that microcystin-LR, applied below the acute toxicity level, dose-dependently increases the number and percentage area of positive foci for the placental form of glutathioneS-transferase in rat liver, which was initiated with diethylnitrosamine.
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