fostriecin and tautomycin

fostriecin has been researched along with tautomycin* in 4 studies

Reviews

2 review(s) available for fostriecin and tautomycin

ArticleYear
Serine-threonine protein phosphatase inhibitors: development of potential therapeutic strategies.
    Journal of medicinal chemistry, 2002, Mar-14, Volume: 45, Issue:6

    Topics: Alkenes; Antibiotics, Antineoplastic; Antifungal Agents; Cantharidin; Crystallography, X-Ray; Cyclosporine; Enzyme Inhibitors; Humans; Microcystins; Models, Molecular; Okadaic Acid; Peptides, Cyclic; Phosphoprotein Phosphatases; Polyenes; Pyrans; Pyrones; Spiro Compounds; Structure-Activity Relationship

2002
[Naturally occurring toxins with specific inhibitory activity against protein serine/threonine phosphatases 1 and 2A].
    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 1998, Volume: 43, Issue:8 Suppl

    Topics: Alkenes; Animals; Antifungal Agents; Cantharidin; Marine Toxins; Microcystins; Okadaic Acid; Oxazoles; Peptides, Cyclic; Phosphoprotein Phosphatases; Polyenes; Pyrans; Pyrones; Spiro Compounds

1998

Other Studies

2 other study(ies) available for fostriecin and tautomycin

ArticleYear
Regulation of immunoglobulin E-mediated secretion by protein phosphatases in human basophils and mast cells of skin and lung.
    European journal of pharmacology, 2001, Oct-26, Volume: 430, Issue:1

    A wide range of serine/threonine protein phosphatase (PP) inhibitors were studied for effects on the immunoglobulin E (IgE)-mediated release of histamine from human lung mast cells, human skin mast cells and basophils. Okadaic acid (OA) inhibited the release of histamine from all three cell types in a concentration-dependent manner. Two structural analogues of okadaic acid, okadaol and okadaone, known to be less active than the parent molecule as inhibitors of PP, were less active than okadaic acid as inhibitors of histamine release in these three cell types. A number of PP inhibitors, showing differences in selectivity for PP1 and PP2A, were also evaluated. Calyculin, which is roughly equipotent as a PP1 and PP2A inhibitor, attenuated the release of histamine from all three cell types. Similarly, tautomycin (TAU), which shows greater selectivity for PP1 over PP2A, was also effective at inhibiting histamine release in all three cell types. In contrast, fostriecin, which is very much more potent as an inhibitor of PP2A over PP1, was ineffective as an inhibitor in all three cell types. These data indicate that the regulation of mediator release by PPs is similar in lung mast cells, skin mast cells and basophils. Moreover, the data suggest that PP1 is important in the control of cellular activity.

    Topics: Alkenes; Antifungal Agents; Basophils; Enzyme Inhibitors; Histamine Release; Humans; Immunoglobulin E; Lung; Marine Toxins; Mast Cells; Okadaic Acid; Oxazoles; Phosphoprotein Phosphatases; Polyenes; Pyrans; Pyrones; Skin; Spiro Compounds

2001
Importance of the beta12-beta13 loop in protein phosphatase-1 catalytic subunit for inhibition by toxins and mammalian protein inhibitors.
    The Journal of biological chemistry, 1999, Aug-06, Volume: 274, Issue:32

    Type-1 protein serine/threonine phosphatases (PP1) are uniquely inhibited by the mammalian proteins, inhibitor-1 (I-1), inhibitor-2 (I-2), and nuclear inhibitor of PP1 (NIPP-1). In addition, several natural compounds inhibit both PP1 and the type-2 phosphatase, PP2A. Deletion of C-terminal sequences that included the beta12-beta13 loop attenuated the inhibition of the resulting PP1alpha catalytic core by I-1, I-2, NIPP-1, and several toxins, including tautomycin, microcystin-LR, calyculin A, and okadaic acid. Substitution of C-terminal sequences from the PP2A catalytic subunit produced a chimeric enzyme, CRHM2, that was inhibited by toxins with dose-response characteristics of PP1 and not PP2A. However, CRHM2 was insensitive to the PP1-specific inhibitors, I-1, I-2, and NIPP-1. The anticancer compound, fostriecin, differed from other phosphatase inhibitors in that it inhibited wild-type PP1alpha, the PP1alpha catalytic core, and CRHM2 with identical IC(50). Binding of wild-type and mutant phosphatases to immobilized microcystin-LR, NIPP-1, and I-2 established that the beta12-beta13 loop was essential for the association of PP1 with toxins and the protein inhibitors. These studies point to the importance of the beta12-beta13 loop structure and conformation for the control of PP1 functions by toxins and endogenous proteins.

    Topics: Alkenes; Amino Acid Sequence; Antifungal Agents; Enzyme Activation; Enzyme Inhibitors; Humans; Microcystins; Models, Molecular; Molecular Sequence Data; Peptides, Cyclic; Phosphoprotein Phosphatases; Polyenes; Protein Binding; Protein Phosphatase 1; Protein Structure, Secondary; Proteins; Pyrans; Pyrones; Sequence Homology, Amino Acid; Spiro Compounds

1999
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