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1. Introduction
2. Chemically-diverse natural inhibitors of PPP (1)
3. Okadaic acid and microcystin binding kinetics
4. Similar 3D motifs within the PP1 active site
5. Microcystin - PP1 binding site
6. Microcystin bonds with a cysteine residue
7. Microcystin affinity chromatography (1)
8. Microcystin affinity chromatography (2)
9. PP inhibitors trap phosphorylated substrates
10. Protein phosphorylation regulates cellular events
11. PP2B is inhibited by cyclosporin and cyclophilin
12. Chemically-diverse natural inhibitors of PPP (2)
13. Cantharidin
14. Okadaic acid
15. Microcystins and nodularins
16. Microcystin contaminated water sources
17. Enzyme/microcystin interactions - how will it help
18. Microcystin - a legal paradox (1)
19. Microcystin - a legal paradox (2)
20. Microcystin poisonings
21. Causes of cyanobacterial blooms
22. Dundee center for water law policy and science
23. Concluding remarks

Topics Covered

• Toxic inhibitors of protein PPP family serine/threonine phosphatases
• Use of these compounds to characterize the functions and structures of PPP enzymes
• The natural ecological contexts of the toxins
• Okadaic acid and the shellfish industry
• Microcystin in freshwater cyanobacteria
• Contrasts in how microcystin in regarded legally by the security and water industries
• Attempts to understand global trends in microcystin

Links

Series:

• Protein Phosphorylation

Categories:

• Biochemistry

Talk Citation

MacKintosh, C. (2010, November 30). Protein phosphatase inhibitors: a distillation of cell signaling research and water toxicology [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 26, 2024, from https://doi.org/10.69645/JHPP7739.
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Publication History

• Published on November 30, 2010

Financial Disclosures

• Prof. Carol MacKintosh has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.