Parole chiave: Atp, Ide, Insulin, Maldi, Mass Spectrometry, Oligomer, Amyloidogenic Peptides, Cleavage Patterns, Cleavage Sites, Concentration Ratio, Desorption Ionization, Environmental Factors, Insulin-Degrading Enzymes, Proteolytic Activities, Reaction Time, Triphosphate, Amines, Atmospheric Ionization, Degradation, Enzyme Activity, Mass Spectrometers, Metal Ions, Spectrum Analysis, Zinc, Integrodifferential Equations, Adenosine Triphosphate, Copper, Insulinase, Article, Atmospheric Pressure, Concentration (parameters), Enzyme Active Site, Matrix Assisted Laser Desorption Ionization Time Of Flight Mass Spectrometry, Oligomerization, Priority Journal, Protein Cleavage, Protein Degradation, Protein Interaction, Protein Modification, Qualitative Analysis, Amino Acid Sequence, Insulysin, Molecular Sequence Data, Matrix-Assisted Laser Desorption-Ionization, Time Factors,
Affiliazioni:
*** IBB - CNR *** Dipartimento di Scienze Chimiche, Universita di Catania, Viale Andrea Doria 6, 95125, Catania, Italy. grassog@unict.it Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, Catania, Italy
Riferimenti:
Farris, W., Mansourian, S., Chang, Y., Lindsley, L., Eckman, E.A., Frosch, M.P., Eckman, C.B., Guénette, S., Insulin-degrading enzyme regulates the levels of insulin, amyloid β- protein, and the β-amyloid precursor protein intracellular domain in vivo (2003) Proceedings of the National Academy of Sciences of the United States of America, 100, p. 416
Kurochkin, I.V., Insulin-degrading enzyme: Embarking on amyloid destruction (2001) Trends in Biochemical Sciences, 26, p. 421
Blomqvist, M.E.-L., Silburn, P.A., Buchanan, D.D., Andreasen, N., Blennow, K., Pedersen, N.L., Brookes, A.J., Prince, J.A., Sequence variation in the proximity of IDE may impact age at onset of both Parkinson disease and Alzheimer disease (2004) Neurogenetics, 5, p. 115
D. G. Cook, J. B. Leverenz, P. J. McMillan, J. J. Kulstad, S. Ericksen, R. A. Roth, G. D. Schellenberg, L. W. Jin, K. S. Kovacina, S. Craft. Reduced hippocampal insulin-degrading enzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele. American Journal of Pathology 2003, 162, 313Kim, M., Hersh, L.B., Leissring, M.A., Ingelsson, M., Matsui, T., Farris, W., Lu, A., Tanzi, R.E., Decreased catalytic activity of the insulin-degrading enzyme in chromosome 10-linked Alzheimer disease families (2007) Journal of Biological Chemistry, 282, p. 7825
Shen, Y., Joachimiak, A., Rosner, M.R., Tang, W.-J., Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism (2006) Nature, 443, p. 870
Li, P., Kuo, W.L., Yousef, M., Rosner, M.R., Tang, W.-J., The C-terminal domain of human insulin degrading enzyme is required for dimerization and substrate recognition (2006) Biochemical and Biophysical Research Communications, 343, p. 1032
Song, E.S., Daily, A., Fried, M.G., Juliano, M.A., Juliano, L., Hersh, L.B., Mutation of active site residues of insulin-degrading enzyme alters allosteric interactions (2005) Journal of Biological Chemistry, 280, p. 17701
Song, E.S., Juliano, M.A., Juliano, L., Hersh, L.B., Substrate activation of insulin degrading enzyme (insulysin), A potential target for drug development (2003) Journal of Biological Chemistry, 278, p. 49789
Miners, J.S., Kehoe, P.G., Love, S., Immunocapture-based fluoromet- ric assay for the measurement of insulin-degrading enzyme activity in brain tissue homogenates (2008) Journal of Neuroscience Methods, 169, p. 177
Camberos, M.C., Perez, A.A., Udrisar, D.P., Wanderley, M.I., Cresto, J.C., ATP inhibits insulin-degrading enzyme activity (2001) Experimental Biology and Medicine, 226, p. 334
Affholter, J.A., Cascieri, M.A., Bayne, M.L., Brange, J., Casaretto, M., Roth, R.A., Identification of residues in the insulin molecule important for binding to insulin-degrading enzyme (1990) Biochemistry, 29, p. 7727
Diaz, J.L., Wilkin, T.J., Effect of iodination site on binding of radiolabeled ligand by insulin antibodies and insulin autoantibodies (1988) ClinicalChemistry, 34, p. 356
Grasso, G., Rizzarelli, E., Spoto, G., How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin (2008) Biochimica et Biophysica Acta, 1784, p. 1122
Ebrahim, A., Hamel, F.G., Bennett, R.G., Duckworth, W.C., Identification of the metal associated with the insulin degrading enzyme (1991) Biochemical and Biophysical Research Communications, 181, p. 1398
Duckworth, W.C., Insulin degradation: Mechanisms, products, and significance (1988) Endocrine Reviews, 9, p. 319
Tan, P.V., Laiko, V.V., Doroshenko, V.M., Atmospheric pressure MALDI with pulsed dynamic focusing for high-efficiency transmission of ions into a mass spectrometer (2004) Analytical Chemistry, 76, p. 2462
Schneider, B.B., Lock, C., Covey, T.R., AP and vacuum MALDI on a QqLIT instrument (2005) Journal of the American Society for Mass Spectrometry, 16, p. 176
Vu, L., Stöcklin, R., Rose, K., Offord, R.E., Facile identification by electrospray mass spectrometry of the insulin fragment A14-21-B 17-30 produced by insulin proteinase (1993) Rapid Communicationsin MassSpectrometry, 7, p. 1048
Safavi, A., Miller, B.C., Cottam, L., Hersh, L.B., Identification of γ - endorphin-generating enzyme as insulin-degrading enzyme (1996) Biochemistry, 35, p. 14318
Im, H., Manolopoulou, M., Malito, E., Shen, Y., Zhao, J., Neant-Fery, M., Sun, C.-Y., Tang, W.-J., Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE (2007) Journal of Biological Chemistry, 282, p. 25453
Sarracino, D., Richert, C., Quantitative MALDI-TOF MS of oligonucleotides and a nuclease assay (1996) Bioorganic & Medicinal Chemistry Letters, 6, p. 2543
Shevchenko, A., Evaluation of the efficiency of in-gel digestion of proteins by peptide isotopic labeling and MALDI mass spectrometry (2001) Analytical Biochemistry, 296, p. 279
Bush, A.I., Curtain, C.C., Twenty years of metallo-neurobiology: Where to now? (2008) European Biophysics Journal, 37, p. 241
Coffman, F.D., Dunn, M.F., Insulin-metal ion interactions: The binding of divalent cations to insulin hexamers and tetramers and the assembly of insulin hexamers (1988) Biochemistry, 27, p. 6179
Hudecek, J., Anzenbacher, P., Kalous, V., Interaction of insulin with metal(II) ions (1979) FEBS Letters, 100, p. 374
The prominent role that insulin-degrading enzyme (IDE) has on amyloidogenic peptides degradation has recently boosted a lot of attention toward this enzyme. Although many substrates are known to be degraded by IDE, little is known about the changes in the proteolytic activity of the enzyme upon modification of environmental factors. In a previous work we have already shown the great potentiality of atmospheric pressure/laser desorption ionization-mass spectrometry (AP/MALDI-MS) for studying the interaction between IDE and insulin. Here, the activity of IDE was investigated regarding cleavage sites' preferentiality upon modification of environmental factors by AP/MALDI-MS. The roles that IDE/insulin concentration ratio, reaction time, adenosine 5'-triphosphate (ATP) and metal ions (Zn and Cu) have on the insulin cleavage pattern produced by IDE are investigated and a plausible interpretation involving the proteolytic action of the different IDE oligomeric forms is proposed. 2009 John Wiley & Sons, Ltd.
176 Records (172 escludendo Abstract e Conferenze). Impact factor totale: 656.701 (637.77 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 675.157 (656.437 escludendo Abstract e Conferenze).
ibb.cnr.it