changes in protein profiles in bortezomib applied multiple myeloma ...

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Figure 4.1. XTT Cell Proliferation Result ..................................................................... 68 Figure 4.2. Changes in Caspase-3 Enzyme Activity ..................................................... 69 Figure 4.3. Changes in Cytoplasmic/Mitochondrial JC-1 ............................................. 70 in U-266 Cells Treated with Bortezomib ................................................. 70 Figure 4.4. 2D PAGE Maps of Bortezomib (17 nM) and Control Group ..................... 71 x
LIST OF TABLES Table Page Table 1.1 Genetic Alterations in MM ............................................................................... 8 Table 1.2. Prevalance of Important Translocations in MM .............................................. 9 Table 1.3. Laboratory Tests and Procedures to Diagnose the MM ................................ 14 Table 1.4. Durie-Salmon Staging System in MM .......................................................... 17 Table 1.5. International Staging System in MM ............................................................. 18 Table 2.1. Characteristics of protein stains ..................................................................... 34 Table 2.2. Advantages and disadvantages of protein profiling techniques .................... 44 Table 3.1. Preparation of BSA Standards and Test Sample for the Bradford Protein Assay ....................................................................... 54 Table 3.2. Dilution of Protein Sample ............................................................................ 54 Table 3.3. Required Protein Sample with Rehydration Buffer ....................................... 59 Table 3.4. Bradford results for protein samples .............................................................. 59 Table 3.5. Reconstituted sample values .......................................................................... 59 Table 3.6. PROTEAN IEF Cell Program ....................................................................... 61 Table 3.7. Time Coarse for MALDI-TOF Compatible Mass Spectrometry .................. 63 Table 4.1. Magnified Segments of Differentiated Protein Spots .................................... 72 Table 4.2. Results of Differential Proteins Identified MALDI-TOF-TOF Mass Spectrometry ......................................................................................... 78 xi
Page 1 and 2: CHANGES IN PROTEIN PROFILES IN BORT
Page 3 and 4: ACKNOWLEDGEMENTS First of all, with
Page 5 and 6: ÖZET BORTEZOMĠB UYGULANAN MULTĠP
Page 7 and 8: 2.1.4.1.2. Two-Dimensional Gel Elec
Page 9: LIST OF FIGURES Figure Page Figure
Page 13 and 14: When normal cells in the body begin
Page 15 and 16: Figure 1.2. Development of Cancer S
Page 17 and 18: the myeloma cells does not help fig
Page 19 and 20: A rare form of MM called Nonsecreto
Page 21 and 22: 1.2.3. Risk Factors for MM A risk f
Page 23 and 24: of the mineralizations by adjusting
Page 25 and 26: To measure the levels of red cells,
Page 27 and 28: The levels of blood urea nitrogen (
Page 29 and 30: By using the system introduced by D
Page 31 and 32: 1.2.7.2. Biology of The Proteasome
Page 33 and 34: Figure 1.10. Ubiquitin-Proteasome P
Page 35 and 36: Figure 1.12. Effect of Bortezomib o
Page 37 and 38: encompasses the investigation of pr
Page 39 and 40: of modification. Ubiquitin is a sma
Page 41 and 42: the given cells. On the other hand,
Page 43 and 44: is-acrylamide (N,N'-methylene-bisac
Page 45 and 46: 2.1.4.2. Detection of Protein Spots
Page 47 and 48: ange of 600-2500 Da. This is the id
Page 49 and 50: ions resolved by the mass analyzer
Page 51 and 52: 2.1.4.5.2. Mass Analyzers Figure 2.
Page 53 and 54: There is no doubt that different ma
Page 55 and 56: mask low-quantity proteins that may
Page 57 and 58: 3.1. Materials 3.1.1. Medias CHAPTE
Page 59 and 60: 3.2.5. Cell Proliferation Assay Ant
Page 61 and 62:
After 72 hour incubation period at
Page 63 and 64:
eceptors of the Tumor Necrosis Fact
Page 65 and 66:
The preparation of stock BSA Standa
Page 67 and 68:
3.2.6.3. Detection of the Loss of M
Page 69 and 70:
centrifugation, the supernatant was
Page 71 and 72:
selected symmetrically to load the
Page 73 and 74:
approximately 35 ml, the volume of
Page 75 and 76:
After electrophoresis was finished,
Page 77 and 78:
7 Day Two: Reduction, Alkylation, a
Page 79 and 80:
CHAPTER 4 RESULTS AND DISCUSSION 4.
Page 81 and 82:
% Changes in Cytoplasmic/Mitochondr
Page 83 and 84:
Table 4.1. Magnified Segments of Di
Page 85 and 86:
Table 4.1. Magnified Segments of Di
Page 87 and 88:
After labeling, black and red color
Page 89 and 90:
78 7 8 Y2S Y3S Table 4.2. Results o
Page 91 and 92:
80 12 S4Ca Table 4.2. Results of Di
Page 93 and 94:
82 27 Y5S Table 4.2. Results of Dif
Page 95 and 96:
Spot 4, Ubiquitin-conjugating enzym
Page 97 and 98:
is a transcriptional repressor, but
Page 99 and 100:
activity and loss of mitochondrial
Page 101 and 102:
distributed, but correlate with nat
Page 103 and 104:
DeMartino, G. N. and Slaughter, C.
Page 105 and 106:
proteomic analyses of a systematica
Page 107 and 108:
Mahindraa, A., Hideshimab, T. and A
Page 109 and 110:
Richardson, P. G., Hideshima, T. an
Page 111 and 112:
Terpos, E. 2008. Bortezomib Directl
Page 113 and 114:
A.1. RPMI-1640 Growth Medium APPEND
Page 115 and 116:
Table B.1. Chemicals and Reagents U
Page 117 and 118:
B.4.3. Standard Curve for BSA Table
Page 119 and 120:
Urea (8M) 4.8 g CHAPS (%2) 0.2 g DT
Page 121 and 122:
E. F. G. STOCK REAGENT PREPARATION
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