Transglutaminase has intrinsic kinase activity

Details Transglutaminase has intrinsic kinase activity Transglutaminase has intrinsic kinase activity

2006-08-15

2006-08-15

Leith, Patricia (Department: 1655)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Reexamination Certificate

active

07090971

ABSTRACT:
A method of identifying compounds capable of modulating trans-glutaminase (TG) kinase activity is described. The method involves adding a test compound to a mixture of TG and a suitable TG kinase substrate, incubating the mixture under conditions promoting TG kinase activity, and determining if the test compound activates or modulates TG kinase activity as indicated by greater than expected TG-mediated phosphorylation of the TG kinase substrate or if the test compound inhibits TG kinase activity as indicated by lower than expected TG-mediated phosphorylation of the TG kinase substrate as compared to a control comprising TG and a suitable TG kinase substrate incubated under conditions promoting TG kinase activity.

REFERENCES:
Fesus et al. TRANSGLUTAMINASE 2: An Enigmatic Enzyme With Diverse Functions; Trends in Biochemical Sciences, vol. 27, No. 10 (2002) pp. 534-539.
Coverley et al. The Effect of Phosphorylation By Casein Kinase 2 on the Activity Of Insulin-Like Growth Factor-Binding Protein-3; Endocrinology, vol. 141, No. 2 (2000) pp. 564-570.
Coverley et al. Phorphorylation Of Insulin-Like Growth Factor Binding Proteins; Mol. and Cell. Endocrinology, vol. 128 (1997) pp. 1-5.
Pattison et al. Insulin-Like Growth Factor Binding Protein-3 is Secreted as a Phosphoprotein by Human Breast Cancer Cells; Mol. and Cell. Endocrinology, vol. 156 (1999) pp. 131-139.
Sakai et al. Tissue Transglutaminase Facilitates the Polymerization of Insulin-Like Growth Factor Binding Protein-1 (IGFBP-1) and Leads to the Loss of IGFBP-1's Ability To Inhibit Insulin-Like Growth Factor-1-Stimulated Protein Synthesis.
Continued: The Journal of Biological Chemistry, vol. 276, No. 12, (2001) pp. -8740-8745.

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