Searching biomarker candidates in serum using multidimensional native chromatography. II Method evaluation with Alport syndrome and severe inflammation

Baum, A.; Pohl, Michael; Kreusch, Stefan; Cumme, Gerhard A.; Ditze, Günter; Misselwitz, Joachim; Kiehntopf, Michael; Udby, Lene; Meier‐Hellmann, Andreas; Rhode, Heidrun

doi:10.1016/j.jchromb.2008.10.014

Cited by 14 publications

(23 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…ICP MS might be used to detect proteins that carry elemental labels (Polec-Pawlak et al, 2008;Razumienko et al, 2008). There are many possible novel combinations of technologies (Horvatovich et al, 2007;Baum et al, 2008;Dayarathna, Hancock, & Hincapie, 2008;Han & Speicher, 2008;Sihlbom et al, 2008;Tanaka et al, 2009). A combination of multiple preparative and analytical separation methods will be required to detect many low abundance blood proteins (Hoffman et al, 2007).…”

Section: H Other Methodsmentioning

confidence: 99%

“…Schizophrenia was quantitatively compared to control samples at the level of digested peptides (Levin et al, 2007;Levin et al, 2009). Multidimensional chromatography identified 32,288 peptides matching 2,669 serum proteins and revealed that alpha1B-glycoprotein, cysteine-rich secretory protein and an apparently low molecular-weight albumin were markers of severe inflammation (Horn et al, 2006;Rozet et al, 2006;Baum et al, 2008;Kreusch et al, 2008).…”

Section: Partition Chromatography Of Proteins and Peptidesmentioning

confidence: 99%

See 1 more Smart Citation

Mass spectrometry of peptides and proteins from human blood

Zhu

Bowden

Zhang

et al. 2010

Mass Spectrometry Reviews

View full text Add to dashboard Cite

It is difficult to convey the accelerating rate and growing importance of mass spectrometry applications to human blood proteins and peptides. Mass spectrometry can rapidly detect and identify the ionizable peptides from the proteins in a simple mixture and reveal many of their post-translational modifications. However, blood is a complex mixture that may contain many proteins first expressed in cells and tissues. The complete analysis of blood proteins is a daunting task that will rely on a wide range of disciplines from physics, chemistry, biochemistry, genetics, electromagnetic instrumentation, mathematics and computation. Therefore the comprehensive discovery and analysis of blood proteins will rank among the great technical challenges and require the cumulative sum of many of mankind's scientific achievements together. A variety of methods have been used to fractionate, analyze and identify proteins from blood, each yielding a small piece of the whole and throwing the great size of the task into sharp relief. The approaches attempted to date clearly indicate that enumerating the proteins and peptides of blood can be accomplished. There is no doubt that the mass spectrometry of blood will be crucial to the discovery and analysis of proteins, enzyme activities, and post-translational processes that underlay the mechanisms of disease. At present both discovery and quantification of proteins from blood are commonly reaching sensitivities of ∼1 ng/mL.

show abstract

Section: H Other Methodsmentioning

confidence: 99%

Section: Partition Chromatography Of Proteins and Peptidesmentioning

confidence: 99%

Mass spectrometry of peptides and proteins from human blood

Zhu

Bowden

Zhang

et al. 2010

Mass Spectrometry Reviews

View full text Add to dashboard Cite

show abstract

“…Information on the original states of constituents (complex formation, modification, fragmentation, activity) is available as shown in [11,19]. Summarizing, our method may be used complementarily with 2-DE, SELDI-procedures, peptidomics investigations, and various bottom-up proteomic schedules to achieve more comprehensive characterization of biological samples.…”

Section: Resultsmentioning

confidence: 99%

“…Protease inhibitors were not used throughout the analyses to avoid possible affecting of fractionation, subsequent tryptic digestion, and MS analysis (cf., e.g., [9]). Moreover, sufficient recovery was found for a panel of proteins in 2D-fractions by immuno-reactivity and enzyme activity [11,19,20], indicating that heavy proteolysis did not take place. Furthermore, for clinical application, solely biomarker candidates that resist endogen proteolysis will be useful.…”

Section: General Remarksmentioning

confidence: 99%

Searching biomarker candidates in serum using multidimensional native chromatographyI. Enhanced separation method

Kreusch

Schulze

Cumme

et al. 2008

Journal of Chromatography B

View full text Add to dashboard Cite

“…All these proteins have been previously linked to various inflammatory conditions, confirming that these markers are associated with the inflammatory state. For example, chromatography has demonstrated an association between sepsis, a whole-body, severe inflammation, and a decrease in A1BG protein [21]. It has been reported that COL1A1 is increased in mouse models of colitis, including dextran sodium sulfate (DSS) and 2,4,6-trinitrobenzenesulfonic acid (TNBS) models [22, 23].…”

Section: Discussionmentioning

confidence: 99%

Longitudinal study of circulating protein biomarkers in inflammatory bowel disease

Viennois

Baker

Xiao

et al. 2015

Journal of Proteomics

View full text Add to dashboard Cite

Inflammatory bowel diseases (IBD) are chronic and progressive inflammatory disorders of the gastrointestinal tract. In IBD, protein serological biomarkers could be relevant tools for assessing disease activity, performing early-stage diagnosis and managing the treatment. Using the interleukin-10 knockout (IL-10−/−) mouse, a model that develops a time-dependent IBD-like disorder that predominates in the colon; we performed longitudinal studies of circulating protein biomarkers in IBD. Circulating protein profiles in serum samples collected from 30-, 93-, and 135-day-old IL-10−/− mice were investigated using two-dimensional differential gel electrophoresis and MALDI TOF/TOF tandem mass spectrometry. A total of 15 different proteins were identified and confirmed by ELISA and Western blot to be differentially accumulated in serum samples from mid- to late-stage IL-10−/− mice compared to early non-inflamed IL-10−/− mice. The use of another model of colitis and an extra-intestinal inflammation model validated this biomarker panel and demonstrated that comprised some global inflammatory markers, some intestinal inflammation-specific markers and some chronic intestinal inflammation markers. Statistical analyses using misclassification error rate charts validated the use of these identified proteins as powerful biomarkers of colitis. Unlike standard biomarker screening studies, our analyses identified a panel of proteins that allowed the definition of protein signatures that reflect colitis status.

show abstract

Searching biomarker candidates in serum using multidimensional native chromatography. II Method evaluation with Alport syndrome and severe inflammation

Cited by 14 publications

References 54 publications

Mass spectrometry of peptides and proteins from human blood

Mass spectrometry of peptides and proteins from human blood

Searching biomarker candidates in serum using multidimensional native chromatographyI. Enhanced separation method

Longitudinal study of circulating protein biomarkers in inflammatory bowel disease

Contact Info

Product

Resources

About