Novel caged fluorescein diphosphates as photoactivatable substrates for protein tyrosine phosphatases

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1601, Issue 1, 2002, Pages 19-28

  Wang, Qingping ^a   Scheigetz, John ^a   Roy, Bruno ^a   Ramachandran, Chidambaram ^a   Gresser, Michael J ^a  

^a MERCK FROSST CENTRE FOR THERAPEUTIC RESEARCH   (Canada)

Author keywords

Caged FDP; Cell permeable substrate; Photocleavable substrate; PTP; Substrate in intact cell

Indexed keywords

ALKALINE PHOSPHATASE; BENZENE DERIVATIVE; CD45 ANTIGEN; FLUORESCEIN DERIVATIVE; FLUORESCEIN MONOPHOSPHATE; INOSITOL TRISPHOSPHATE; NUCLEOTIDE; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; PYROPHOSPHORIC ACID DERIVATIVE; UNCLASSIFIED DRUG; LEUKOCYTE ANTIGEN; PHOSPHONIC ACID DERIVATIVE; PROTEIN TYROSINE PHOSPHATASE; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; CELL MEMBRANE PERMEABILITY; CELL VIABILITY; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ASSAY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; HYDROLYSIS; IMMERSION; IRRADIATION; NONHUMAN; PHOTOACTIVATION; PHOTOLYSIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; ANIMAL; ARMYWORM; CELL LINE; ENZYME SPECIFICITY; GENETIC TRANSFECTION; KINETICS; LEUKEMIA CELL LINE; METABOLISM;

ANIMALS; ANTIGENS, CD; ANTIGENS, CD45; CELL LINE; FLUORESCEINS; HUMANS; JURKAT CELLS; KINETICS; PHOSPHONIC ACIDS; PHOTOLYSIS; PROTEIN-TYROSINE-PHOSPHATASE; RECOMBINANT PROTEINS; SPODOPTERA; SUBSTRATE SPECIFICITY; TRANSFECTION;

EID: 0037137141     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(02)00412-0     Document Type: Article

References (32)

1. Klann A.G., Miller R.A., Norman E.D., Klann E. Tryosine phosphatases: cellular functions and therapeutical potential. Expert Opin. Ther. Pat. 10(5):2000;675-683.
2. Zhang Z.-Y. Protein tyrosine phosphatases: prospects for therapeutics. Curr. Opin. Chem. Biol. 5:2001;416-423.
3. Irie-Sasaki J., Sasaki T., Matsumoto W., Opavsky A., Cheng M., Welstead G., Griffiths E., Krawczyk C., Richardson C.D., Aitken K., Iscover N., Koretzky G., Johnson P., Liu P., Rothstein D.M., Penninger J.M. CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling. Nature. 409:2001;349-354.
4. Elchebly M., Payette P., Michaliszyn E., Cromlish W., Collins S., Loy A.L., Normandin D., Cheng A., Himms-Hagen J., Chan C.C., Ramachandran C., Gresser M.J., Tremblay M.L., Kennedy B.P. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science. 283:1999;1544-1547.
5. Klaman L.D., Boss O., Peroni O.D., Kim J.K., Martino J.L., Zabolothy J.M., Moghal N., Lubkin M., Kim Y-B., Sharpe A.H., Stricker-Krongrad A., Shulman G.I., Neel B.G., Kahn B.B. Increased Energy Expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell. Biol. 20(15):2000;5479-5489.
6. Kennedy B., Ramachandran C. Protein tyrosine phosphatase-1B in diabetes. Biochem. Pharmacol. 60(7):2000;877-883.
7. Brown B.B., Wagner D.S., Geysen H.M. A single-bead decode strategy using electrospray ionization mass spectrometry and a new photolabile linker: 3-amino-3-(2-nitrophenyl)propionic acid. Mol. Divers. 1:1995;4-12.
8. Brenner S., Lerner R.A. Encoded combinatorial chemistry. Proc. Natl. Acad. Sci. U. S. A. 89:1992;5381-5383.
9. Ohlmeyer M.H.J., Swanson R., Dillard L.W., Reader J.C., Asouline G., Kobayashi R., Wrigler M., Still W.C. Complex synthetic chemical libraries indexed with molecular tags. Proc. Natl. Acad. Sci. U. S. A. 90:1993;10922-10926.
10. Nestler H.P., Bartlett P.A., Still W.C. A general method for molecular tagging of encoded combinatorial chemistry libraries. J. Org. Chem. 59:1994;4723-4724.
11. Borchardt A., Liberles S.D., Biggar S.R., Crabtree G.R., Schreiber S.L. Small molecule-dependent genetic selection in stochastic nanodroplets as a means of detecting protein-ligand interactions on a large scale. Chem. Biol. 4:1997;961-968.
12. Huang Z., Wang Q., Ly H., Gorvindarajan A., Scheigetz J., Zamboni R., Desmarais S., Ramachandran C. 3,6-Fluorescein diphosphatae: a sensitive fluorogenic and chromogenic substrate for protein tyrosine phosphatases. J. Biomol. Screen. 4(6):1999;327-334.
13. Kaplan J.H., Forbush III B., Hoffman J.F. Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts. Biochemistry. 17:1978;1929-1935.
14. Kaplan J.H. Photochemical manipulation of divalent cation level. Annu. Rev. Physiol. 52:1990;897-914.
15. Adams S.R., Tsien R.Y. Controlling cell chemistry with caged compounds. Annu. Rev. Physiol. 55:1993;755-783.
16. Corrie J.e.T., Trentham D.R. Mossison H. Biological Application of Photochemical Switches. 1993;243-305 Wiley, New York.
17. Marriott G. Methods Enzymol. vol. 291:1998;1-495.
18. Corrie J., Ogden D., Canepari M., Papageorgiou G. Nitroindolinyl-caged L-glutamate - a new tool for investigating glutamate-gated ion channels. Cell Transm. 17:2001;19-20.
19. Li W.H., Liopis J., Whitney M., Ziokarnik G., Tsien R.Y. Cell-permeant caged InsP3 ester shows that Ca2+ spike frequency can optimize gene expression. Nature. 392:1998;936-941.
20. Nerbonne J.M., Richard S., Nargeot J., Lester H.A. New photoactivatable cyclic nucleotide produce intracellular jumps in cyclic AMP and cyclic GMP concentrations. Nature. 310:1984;74-76.
21. Jiang T., Sweeney G., Rudolf M.T., Klip A., Traynor-Kaplan A., Tsien R. Membrane-permeant esters of phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273:1998;11017-11024.
22. Scheigetz J., Roy B. Synthesis of fluorescein phosphorotriesters using photolabile protecting groups. Synth. Commun. 30(8):2000;1437-1445.
23. Huyer G., Liu S., Kelly J., Moffat J., Payette P., Kennedy B., Tsaprilis G., Gresser M.J., Ramachandran C. Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J. Biol. Chem. 272:1997;843-851.
24. Desmarais S., Friesen R., Zamboni R., Ramachandran C. [Difluro-(phosphono)methyl]phenylalanine-containing peptide inhibitors of protein tyrosine phosphatases. Biochem. J. 337:1999;219-223.
25. Cromlish W.A., Payette P., Kennedy B.P. Development and validation of an intact cell assay for protein tyrosine phosphatases using recombinant baculoviruses. Biochem. Pharmacol. 58:1999;1539-1546.
26. Waddelton D., Ramachandran C., Wang Q. Development of a method for evaluating protein tyrosine phosphatase CD45 inhibitors using Jurkat cell membrane. Anal. Biochem. 285:2000;58-63.
27. Haugland R.P. Handbook of fluorescent probes and research chemicals. Molecular Probe. 6th ed. 1996;219 Molecular Probes Inc. Eugene, OR.
28. Walker J.W., MacCray J.A., Hess G.P. Photolabile protecting groups for an acetylcholine receptor ligand. Synthesis and photochemistry of a new class of o-nitrobenzyl derivatives and their effects on receptor functions. Biochemistry. 25:1986;1799-1805.
29. Wang Q., Huang Z., Ramachandran C., Dinault A.N., Taylor S.D. Naphthalenebis[α,α-difluoromethylenephosphonates] as potent inhibitors of protein tyrosine phosphatases. Bioorg. Med. Chem. Lett. 8:1998;345-350.
30. Berger J., Hauber J., Hauber R., Geiger R., Cullen B. Secreted placental alkaline phosphatase: a powerful new quantitative indicator of gene expression in eukaryotic cells. Gene. 66:1988;1-10.
31. Cullen B., Malim M. Secreted placental alkaline phosphatase as a eukaryotic reporter gene. Methods Enzymol. 216:1992;362-368.
32. Bronstein I. Chemiluminescent reporter gene assays: sensitive detection of the GUS and SEAP gene products. BioTechniques. 17:1994;172-178.