14C-Labeled microcystin-LR administered to Atlantic salmon via intraperitoneal injection provides in vivo evidence for covalent binding of microcystin-LR in salmon livers

Toxicon

Volumn 35, Issue 6, 1997, Pages 985-989

  Williams, David E ^a   Craig, Marcia ^b   Dawe, Sheila C ^c   Kent, Michael L ^c   Andersen, Raymond J ^a   Holmes, Charles F B ^b  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b UNIVERSITY OF ALBERTA   (Canada)

^c PACIFIC BIOLOGICAL STATION   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 14; CYANOGINOSIN LR; PHOSPHATASE; BACTERIAL TOXIN; CARBON; CYANOGINOSIN; CYCLOPEPTIDE; DIAGNOSTIC AGENT; MARINE TOXIN;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BIOTRANSFORMATION; CONTROLLED STUDY; COVALENT BOND; IN VIVO STUDY; INTRAPERITONEAL DRUG ADMINISTRATION; LIVER; NONHUMAN; PRIORITY JOURNAL; SALMON; ANIMAL; CYANOBACTERIUM; METABOLISM; PROTEIN BINDING;

ANIMALS; BACTERIAL TOXINS; CARBON RADIOISOTOPES; CYANOBACTERIA; INJECTIONS, INTRAPERITONEAL; LIVER; MARINE TOXINS; MICROCYSTINS; PEPTIDES, CYCLIC; PROTEIN BINDING; SALMON;

EID: 0031156043     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(96)00196-1     Document Type: Article

References (18)

1. Andersen, R. J., Luu, H. A., Chen, D. Z. X., Holmes, C. F. B., Kent, M. L., Leblane, M., Taylor, 'Max' F. J. R. and Williams, D. E. (1993) Chemical and biological evidence links microcystins to salmon 'netpen liver disease'. Toxicon 31, 1315-1323.
2. Bagu, J. R., Sönnichsen, F. D., Williams, D. E., Andersen, R. J., Sykes, B. D. and Holmes, C. F. B. (1995) Comparison of the solution structures of microcystin-LR and motuporin. Nature-Struct. Biol. 2, 114-116.
3. Cohen, P. and Cohen, P. T. W. (1989) Protein phosphatases come of age. J. biol. Chem. 264, 21435-21438.
4. Craig, M., Luu, H. A., McCready, T., Williams, D. E., Andersen, R. J. and Holmes, C. F. B. (1996) Molecular mechanisms underlying the interaction of motuporin and microcystins with type-1 and 2A protein phosphatases. Biochem. Cell Biol. 74, 569-578.
5. Goldberg, J., Huang, H., Kwon, Y., Greengard, P., Nairn, A. C. and Kuriyan, J. (1995) Three-dimensional structure of the catalytic subunit of protein serine threonine phosphatase-1. Nature 376, 745-753.
6. Holmes, C. F. B. (1991) Liquid chromatography-linked protein phophatase bioassay; a highly sensitive marine bioscreen for okadaic acid and related diarrhetic shellfish toxins. Toxicon 29, 469-477.
7. Honkanen, R. E., Zwiller, J., Moore, R. E., Daily, S. L., Khatra, B. S., Dukelow, M. and Boynton, A. L. (1990) Characterization of microcystin-LR. a potent inhibitor of type 1 and type 2A protein phosphatases. J. biol. Chem. 265, 19401-19404.
8. Kent, M. L. (1990) Netpen liver disease (NLD) of salmomd fishes reared in seawater; species susceptibility. recovery and probable cause. Dis. aquat. Org. 8, 21-28.
9. Luu, H. A., Chen, D. Z. X., Magoon, J., Worms, J., Smith, J. and Holmes, C. F. B. (1993) Quantification of diarrhetic shellfish toxins and identification of novel protein phosphatase inhibitors in marine phytoplankton and mussels. Toxicon 31, 75-83.
10. MacKintosh, C., Beattie, K. A., Klumpp, S., Cohen, P. and Codd, G. A. (1990) Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. Fedn Eur. biochem. Socs Lett. 264, 187-192.
11. MacKintosh, R. W., Dalby, K. N., Campbell, D. G., Cohen, P. T. W., Cohen, P. and MacKintosh, C. (1995) The cyanobacterial toxin microcystin binds covalently to cysteine 273 on protein phosphatase 1. Fedn Eur. biochem. Socs Lett. 371, 236-240.
12. Moorhead, G., MacKintosh, R. W., Morrice, N., Gallagher, T. and MacKintosh, C. (1994) Purification of type 1 protein (serine/threonine) phosphatases by microcystin sepharose affinity chromatography. Fedn Eur. biochem. Socs Lett. 356, 46-50.
13. Nishiwaki-Matsushima, R., Nishiwaki, S., Ohta, T., Yoshizawa, S., Suganuma, M., Harada, K.-I., Watanabe, M. F. and Fujiki, H. (1991) Structure function relationships of microcystin liver tumor promoters interaction with protein phosphatase. Jpn. J. Cancer Res. 82, 993-996.
14. Robinson, N. A., Matson, C. F. and Pace, J. G. (1991a) Association of microcystin-LR and its biotransformation product with a hepatic-cytosolic protein. J. biochem. Toxic. 6, 171-180.
15. Robinson, N. A., Pace, J. G., Matson, C. F., Miura, G. A. and Lawrence, W. B. (1991b) Tissue distribution, excretion and hepatic biotransformation of microcystin-LR in mice. J. Pharmac. exp. Ther. 256, 176-182.
16. Toivola, D. M., Eriksson, J. E. and Brautigan, D. L. (1994) Identification of protein phosphatase 2A as the primary target for microcystin-LR in rat homogenates. Fedn Eur. biochem. Socs Lett. 344, 175-180.
17. Williams, D. E., Kent, M. L., Andersen, R. J. Klix, H. and Holmes, C. F. B. (1995) Tissue distribution and clearance of tritium-labeled dihydromicrocystin-LR epimers administered to Atlantic salmon via interperitoneal injection. Toxicon 33, 125-131.
18. Yoshizawa, S., Matsushima, R., Watanabe, M. F., Harada, K.-J., Ichihara, A., Carmichael, W. W. and Fujiki, H. (1990) Inhibition of protein phosphatases by microcystin and nodularin associated with hepatoloxicity. J. Cancer Res. clin. Oncol. 116, 609-614.