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

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Table 1.3. Laboratory Tests and Procedures to Diagnose the MM (cont.) BLOOD SPECIMEN Diagnostic Test Purpose Results Serum protein electrophoresis Immunofixation electrophoresis (IFE; also called immunoelectrophoresis) Freelite TM serum free light chain assay Detect the presence and level of various proteins, including M protein Identity the type of abnormal antibody proteins in yhe blood Measure immunoglobulin light chains URINE SPECIMEN Higher levels indicate more extensive disease; aids in classification of disease Aids in classification of disease Abnormal levels and/or ratio suggest the presence of myeloma or a related disease Diagnostic Test Purpose Results Urinalysis Assess kidney function Bence Jones protein level (performed on 24 hour specimen of urine) Urine protein and immunoelectrophoresis Define the presence and level of Bence Jones protein Determine the presence and levels of specific proteins in the urine, including M protein and Bence Jones protein BONE / BONE MARROW SPECIMEN Abnormal findings may suggest kidney damage Presence indicates disease, and higher levels indicate more extensive disease Presence of M protein or Bence Jones protein indicates disease Diagnostic Test Purpose Results Imaging studies (bone) survey, x-ray, magnetic resonance imaging (MRI), computerized tomograph (CT), positron emission tomography (PET) Biopsy (on either fluid aspirated from the bone marrow or on bone tissue) Cytogenetic analysis (e.g., fluorescence in situ hybridization (FISH)) Assess changes in the bone structure and determine the number and size of tumors in the bone Determine the number and pecentage of normal and malignant plasma cells in the bone marrow Assess the number and normalcy of chromosomes and identity the presence of translocations (mis-matching of choromosomes parts) - Presence of myeloma cells confirms the diagnosis, and higher percentage of myeloma cells indicate more extensive disease Loos of certain chromosomes (deletions) or translocations may be associated eith poor outcome Beta-2 microglobulin level is very important to understant the how much disease progress. Actually, this protein is very useful sign for staging of MM. Thus, the level of this protein produced by the malignant plasma cells can be evaluated by a test (Bataille et al, 1992). 15
The levels of blood urea nitrogen (BUN) and creatinine levels in blood is related with the kidney function. The increased levels of them mean that kidney function is impaired. Similarly, low levels of Albumin and high levels of Calcium in the blood can be a cue of advanced myeloma (Bataille et al., 1992; Jacobson et al., 2003). Bone marrow biopsy is of great importance in terms of checking the bone marrow. Because, in MM, patients have too many plasma cells in their bone marrow (Smith et al., 2006). With the progression of technology in imaging area, these types of studies begin to occupy a great place. One of these types of study is Bone x-rays. By the help of method, bone destruction caused by the myeloma cells can be detected (Ozaki, 2007). The computed tomography (CT or CAT) scan can be used as an improved x-ray procedure to take the detailed cross-sectional images of patient’s body to determine the damaged bones (Schreiman et al., 1985; Kyle et al., 1985; Winterbottom and Shaw, 2009). One another imaging methos is magnetic resonance (MRI). It can be also useful in looking at bones. It differs from the x-rays and CT in that it utilizes radio waves instead of x-rays. Firstly, this energy is absorbed and then released in a pattern produced by the type of tissue. Next, the pattern of radio waves given off by the tissues are translated into detailed image of the body (Joffe et al., 1988; Lecouvet et al., 2001). To make a diagnosis of MM, results obtained any single test are not sufficient. 1.2.6. Stages of MM Staging process is very significant in that it is the sign of cancer progress. Importance of this process stems from determining the appropriate treatment options and prognosis. MM has been staged with two systems up to now. One of them is Durie-Salmon Staging System and the other one is International Staging System. Although some doctors still use this system, its value is becoming restricted due to newer diagnostic methods. Recently, International Staging System for MM has been developed. 16
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 and 10: LIST OF FIGURES Figure Page Figure
Page 11 and 12: LIST OF TABLES Table Page Table 1.1
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: To measure the levels of red cells,
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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