Thermal inactivation of the protein tyrosine kinase of the epidermal growth factor receptor

Biochemistry
R A Stein, J V Staros

Abstract

It has been shown previously that the EGF-stimulable protein tyrosine kinase in a membrane preparation from A431 cells was inactivated by heat shock (45 degrees C), under conditions where EGF binding was unaffected [Carpenter et al. (1979) J. Biol. Chem. 254, 4884-4891]. A later study found that in intact cells, the protein tyrosine kinase of the EGF receptor was insensitive to heat shock [Liu & Carpenter (1992) Biochem. J. 286, 541-547]. We have extended these previous studies to better understand the thermal stability of the protein tyrosine kinase of the EGF receptor. We have measured the rate of inactivation of the kinase in membrane vesicles in the physiological to heat shock temperature range (37-45 degrees C). At 45 degrees C, the protein tyrosine kinase is rapidly inactivated with a rate of approximately 0.14 min-1. There is, however, protection against inactivation by incubation of the EGF receptor with AMPPNP, a hydrolysis-resistant ATP analog. At 45 degrees C, the rate of inactivation of nucleotide-bound receptor is an order of magnitude lower than the rate of inactivation of unoccupied receptor. Analysis of the temperature dependence of inactivation between 37 and 45 degrees C yields an activation energy, E(a), of 4...Continue Reading

References

Jan 1, 1989·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·B O FangerJ V Staros

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Citations

Feb 28, 2002·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·R Eicher, H Ludwig
Apr 17, 2007·Ultrasonics Sonochemistry·Rassoul Kadkhodaee, Malcolm J W Povey
Apr 15, 2014·Molecular Oncology·Emmy D G FleurenOtto C Boerman
Jan 29, 2005·Journal of Clinical Oncology : Official Journal of the American Society of Clinical Oncology·Ki Young ChungLeonard B Saltz

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