Serum Proteome Profiling Detects Myelodysplastic Syndromes and Different Expression of Fibrinogen Between RAEB and RCMD

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 5082-5082
Author(s):  
Liye Zhong ◽  
TianHao Liu ◽  
SuXia Geng ◽  
Zesheng Lu ◽  
Jianyu Weng ◽  
...  

Abstract BACKGROUND&OBJECTIVE FMyelodysplastic syndromes (MDS) are among the most frequent hematologic malignancies. The diagnosis of MDS can be difficult, and there is a paucity of molecular markers. The pathophysiology is still largely unknown. Therefore, we investigated whether serum proteome profiling may serve as a noninvasive platform to discover novel molecular markers for MDS and establish the predictive models that may be of help to serologic diagnosis and classification of MDS. METHODS FSerum samples were collected from 14 MDS patients including to 8 Refractory anemia with excess blasts in transformation (RAEB) and 6 Refractory cytopenia with multilineage dysplasia (RCMD) and 18 non-MDS hematologic malignancies and 8 age- and sex-matched healthy subjects. Serum peptides were separated and purified with a purification kit of magnetic beads, using magnetic beads-based weak cation exchange chromatography (MB-WCX) and MB-IMAC Cu, bases on immobilized metal ion affinity chromatography on the surface of superparamagnetic microparticles. We generated serum proteome profiles by matrix-assisted laser desorption/ionization time of-flight mass spectrometry (MALDI-TOF- MS) and identified a profile that distinguishes MDS from non-MDS hematologic malignancies and healthy subjects. RESULTS FA totaI of 146 effective protein peaks were detected at the molecular range of 1.02 tO 10.25 ku, Among which 7 protein peaks were different significantly among MDS patients, non-MDS hematologic malignancies and healthy subjects (P<0.05). There was also different for Peptide mass fingerprinting in MDS patients, and the samples were divided into two groups, which was identical with clinical classification about RAEB and RCMD, using 3-cross validation approach. There was significantly different expression protein between RCMD and RAEB patients, which was identified as a piece of fibrinogen peptide. The expressions of fibrinogen in RAEB subtype patients were higher than RCMD subtype patients. CONCLUSION F Using the MALDI-TOF-MS technique may help to identify serum proteomic biomarkers related to MDS. The predictive models can discriminate MDS patients from other hematologic malignancies and healthy people effectively and help to identify MDS clinical classification. The different expression of Fibrinogen between RAEB and RCMD may suggested heterogeneity of etiopathogenisis in different subtypeof MDS.

Author(s):  
Xin Zhao ◽  
Jiayin Lu ◽  
Shuping Long ◽  
Winnie C. Soko ◽  
Qin Qin ◽  
...  
Keyword(s):  

2011 ◽  
Vol 12 (3) ◽  
pp. 145-151 ◽  
Author(s):  
Xiaoxue Zhang ◽  
Zhaolin Yuan ◽  
Bo Shen ◽  
Min Zhu ◽  
Chibo Liu ◽  
...  

2010 ◽  
Vol 21 (10) ◽  
pp. 1917-1924 ◽  
Author(s):  
Guangchang Zhou ◽  
Xiaoliang Yan ◽  
Ding Wu ◽  
Stephen J. Kron

2019 ◽  
Vol 26 (1) ◽  
pp. 55-62
Author(s):  
MeiHua Wan ◽  
Yichao Wang ◽  
Lingpeng Zhan ◽  
Jia Fan ◽  
Tony Y Hu

Background Serum C-peptide concentrations reflect insulin secretion and beta cell function and can be used to diagnose and distinguish type-1 and type-2 diabetes. C-peptide is a more accurate indicator of insulin status than direct insulin measurement for monitoring patients with diabetes. However, the current methods available for C-peptide quantification exhibit poor reproducibility, are costly, and require highly trained laboratory personnel. Here, we have developed and evaluated a matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS)-based assay to standardize C-peptide measurements, providing highly accurate and comparable results across testing systems and laboratories. Methods C-peptide from human serum was enriched using antibody-conjugated magnetic beads. The eluted isolates were further modified with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate (AQC) to enhance the ionization of naturally acidic C-peptide. After desalting with ZipTips, the samples were subjected to MALDI-TOF MS analysis. Recombinant human C-peptide was used to develop the assay, and a heavy isotope labeled human C-peptide was used as an internal standard for quantification. Results The MALDI-TOF MS method was validated in accordance with the restrictions of the device, with a limit of quantitation of 25 pmol/L. A correlation between the MAL-DI-TOF MS assay and a reference method was conducted using patient samples. The resulting regression revealed good agreement. Conclusions A simple, high-throughput, cost effective and quantitative MALDI-TOF MS C-peptide assay has been successfully developed and validated in clinical serum samples.


2021 ◽  
Vol 192 ◽  
pp. 113647
Author(s):  
Yu-Shan Wei ◽  
Yi-Ru Chang ◽  
Yi-Ting Tsai ◽  
Yi-Ting Yang ◽  
Shang-Hui Weng ◽  
...  

2011 ◽  
Vol 17 (2) ◽  
pp. 89-95 ◽  
Author(s):  
Shengjun Wu ◽  
Kai Xu ◽  
Guang Chen ◽  
Jun Zhang ◽  
Zhiwei Liu ◽  
...  

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