Focused microwave irradiation of the brain preserves in vivo protein phosphorylation: Comparison with other methods of sacrifice and analysis of multiple phosphoproteins

Journal of Neuroscience Methods

Volumn 135, Issue 1-2, 2004, Pages 159-168

  O'Callaghan, James P ^a   Sriram, Krishnan ^a  

^a NATIONAL INSTITUTE FOR OCCUPATIONAL SAFETY AND HEALTH   (United States)

Author keywords

Activating transcription factor; ATF; BCA; Bicinchoninic acid; Calcium calmodulin dependent kinase; CAMK; CREB; Cyclic AMP response element binding protein; ERK; Extracellular signal regulated kinase; GFAP; Glial fibrillary acidic protein; HRP

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; ICE; LIQUID NITROGEN; MITOGEN ACTIVATED PROTEIN KINASE 1; PHOSPHOPROTEIN;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BRAIN RADIATION; BRAIN REGION; CONTROLLED STUDY; CORPUS STRIATUM; DECAPITATION; ENZYME PHOSPHORYLATION; FEMALE; FREEZING; HIPPOCAMPUS; IN VIVO STUDY; INTERMETHOD COMPARISON; MICROWAVE IRRADIATION; MOUSE; NONHUMAN; PRESERVATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DEPHOSPHORYLATION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; ROOM TEMPERATURE; SAMPLING; TIME;

ANIMALS; BLOTTING, WESTERN; BRAIN; BRAIN CHEMISTRY; CORPUS STRIATUM; CRYOPRESERVATION; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN; FEMALE; HIPPOCAMPUS; MICE; MICE, INBRED C57BL; MICROWAVES; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; MITOGEN-ACTIVATED PROTEIN KINASES; PHOSPHOPROTEINS; PHOSPHORYLATION; RADIATION;

EID: 1542617840     PISSN: 01650270     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jneumeth.2003.12.006     Document Type: Article

References (32)

1. Angelucci F., Gruber S.H., Mathe A.A. A pilot study of rat brain regional distribution of calcitonin, katacalcin and calcitonin gene-related peptide before and after antipsychotic treatment. Neuropeptides. 35:2001;285-291.
2. Butcher S.H., Butcher L.L., Harms M.S., Jendent D.J. Fast fixation of brain in situ by high intensity microwave irradiation: application to neurochemical studies. J. Microwave Power. 11:1976;61-65.
3. Cohen P. The origins of protein phosphorylation. Nat. Cell. Biol. 4:2002;E127-E130.
4. De Camilli P., Cameron R., Greengard P. Synapsin I (protein I), a nerve terminal-specific phosphoprotein. Part I. Its general distribution in synapses of the central and peripheral nervous system demonstrated by immunofluorescence in frozen and plastic sections. J. Cell Biol. 96:1983;1337-1354.
5. Delaney S.M., Geiger J.D. Brain regional levels of adenosine and adenosine nucleotides in rats killed by high-energy focused microwave irradiation. J. Neurosci. Methods. 64:1996;151-156.
6. Ferrer I., Friguls B., Dalfo E., Planas A.M. Early modifications in the expression of mitogen-activated protein kinase (MAPK/ERK), stress-activated kinases SAPK/JNK and p38, and their phosphorylated substrates following focal cerebral ischemia. Acta Neuropathol. (Berl.). 105:2003;425-437.
7. Gartner U., Janke C., Holzer M., Vanmechelen E., Arendt T. Postmortem changes in the phosphorylation state of tau-protein in the rat brain. Neurobiol. Aging. 19:1998;535-543.
8. Greengard P. Phosphorylated proteins as physiological effectors. Science. 199:1978;146-152.
9. Greengard P. The neurobiology of slow synaptic transmission. Science. 294:2001;1024-1030.
10. Guattari B. Simultaneous quantitative high-performance liquid chromatographic determination of cyclic adenosine 3′,5′- monophosphate and adenosine in mouse brain after microwave irradiation: application to isoprenaline effect in vivo. J. Chromatogr. 489:1989;394-398.
11. Hebert M.A., O'Callaghan J.P. Protein phosphorylation cascades associated with methamphetamine-induced glial activation. Ann. N.Y. Acad. Sci. 914:2000;238-262.
12. Hossain M.Z., Murphy L.J., Hertzberg E.L., Nagy J.I. Phosphorylated forms of connexin43 predominate in rat brain: demonstration by rapid inactivation of brain metabolism. J. Neurochem. 62:1994;2394-2403.
13. Ishikawa K., Shibanoki S., Saito S., McGaugh J.L. Effect of microwave irradiation on monoamine metabolism in dissected rat brain. Brain Res. 240:1982;158-161.
14. Jope R.S., Johnson G.V., Baird M.S. Seizure-induced protein tyrosine phosphorylation in rat brain regions. Epilepsia. 32:1991;755-760.
15. Katsura M., Iino T., Kuriyama K. Changes in content of neuroactive amino acids and acetylcholine in the rat hippocampus following transient forebrain ischemia. Neurochem. Int. 21:1992;243-249.
16. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
17. Lenox RH, Gandhi OP, Meyerhoff JL, Grove HM. A microwave applicator for in vivo rapid inactivation of enzymes in the central nervous system. IEEE Trans, Microwave Theory Technol 1976;58-61.
18. Li J., Gould T.D., Yuan P., Manji H.K., Chen G. Post-mortem interval effects on the phosphorylation of signaling proteins. Neuropsychopharmacology. 28:2003;1017-1025.
19. Mathe A.A., Stenfors C., Brodin E., Theodorsson E. Neuropeptides in brain: effects of microwave irradiation and decapitation. Life Sci. 46:1990;287-293.
20. Mobley P.L., Gonzalez N.E. The use of microwave tissue fixation to demonstrate the in vivo phosphorylation of an acidic 80,000 molecular weight protein in the rat neocortex following treatment with soman. Life Sci. 49:1991;155-163.
21. O'Callaghan J.P., Lavin K.L., Chess Q., Clouet D.H. A method for dissection of discrete brain regions of the rat brain following microwave irradiation. Brain Res. Bull. 11:1983;31-42.
22. O'Callaghan J.P., Martin P.M., Mass M.J. The MAP kinase cascade is activated prior to the induction of gliosis in the 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine (MPTP) model of dopaminergic neurotoxicity. Ann. N.Y. Acad. Sci. 844:1998;40-49.
23. O'Callaghan J.P., Imai H., Miller D.B., Minter A. Quantitative immunoblots of proteins from brain homogenates: underestimation of specific protein concentration and of treatment effects. Anal. Biochem. 274:1999;18-26.
24. Rubin C.S., Rosen O.M. Protein phosphorylation. Annu. Rev. Biochem. 44:1975;831-887.
25. Schneider D.R., Felt B.T., Goldman H. On the use of microwave irradiation energy for brain tissue fixation. J. Neurochem. 38:1982;749-752.
26. Smith P.K., Krohn R.I., Hermanson G.T., Mallia A.K., Gartner F.H., Provenzano M.D., Fujimoto E.K., Goeke N.M., Olson B.J., Klenk D.C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150:1985;76-85.
27. Snyder G.L., Allen P.B., Fienberg A.A., Valle C.G., Huganir R.L., Narin A.C., Greengard P. Regulation of phosphorylation of the GluR1 AMPA receptor in the neostriatum by dopamine and psychostimulants in vivo. J. Neurosci. 20:2000;4480-4488.
28. Sriram K, Hebert MA, Benkovic SA, Miller DB, O'Callaghan JP. JAK-STAT and MAPK pathways are associated with reactive gliosis following chemically-induced neurodegeneration. In: Keystone Symposia Abstract JAKs and STATs: Activation and Biologic Impact; 2002. p. 49.
29. Stavinoha W.B. Use of microwaves for rapid fixation of tissues in vivo. Scanning. 15:1993;115-117.
30. Theodorsson E., Stenfors C., Mathe A.A. Microwave irradiation increases recovery of neuropeptides from brain tissues. Peptides. 11:1990;1191-1197.
31. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:1979;4350-4354.
32. Veech R.L., Harris R.L., Veloso D., Veech E.H. Freeze-blowing: a new technique for the study of brain in vivo. J. Neurochem. 20:1973;183-188.