Temporally resolved differential proteomic analysis of human ventricular CSF for monitoring traumatic brain injury biomarker candidates

Hanrieder, Jörg; Wetterhall, Magnus; Enblad, Per; Hillered, Lars; Bergquist, Jonas

doi:10.1016/j.jneumeth.2008.10.038

Cited by 63 publications

(53 citation statements)

References 44 publications

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“…Mass-spectrometry has been used to detect small amounts of GFAP and better characterise the post-translational modifications of GFAP (Herskowitz et al, 2010;Cunningham et al, 2013;Hanrieder et al, 2009;Ishigami et al, 2005;Joachim et al, 2007;Nomura et al, 2009;Ekegren et al, 2006). An important finding from these studies was that compared to other proteins GFAP is an extremely stable and robust candidate biomarker for massspectrometry (Ekegren et al, 2006).…”

Section: Mass-spectrometrymentioning

confidence: 99%

Glial fibrillary acidic protein is a body fluid biomarker for glial pathology in human disease

Petzold

2015

Brain Research

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This review on the role of glial fibrillary acidic protein (GFAP) as a biomarker for astroglial pathology in neurological diseases provides background to protein synthesis, assembly, function and degeneration. Qualitative and quantitative analytical techniques for the investigation of human tissue and biological fluid samples are discussed including partial lack of parallelism and multiplexing capabilities. Pathological implications are reviewed in view of immunocytochemical, cell-culture and genetic findings. Particular emphasis is given to neurodegeneration related to autoimmune astrocytopathies and to genetic gain of function mutations. The current literature on body fluid levels of GFAP in human disease is summarised and illustrated by disease specific meta-analyses. In addition to the role of GFAP as a diagnostic biomarker for chronic disease, there are important data on the prognostic value for acute conditions. The published evidence permits to classify the dominant GFAP signatures in biological fluids. This classification may serve as a template for supporting diagnostic criteria of autoimmune astrocytopathies, monitoring disease progression in toxic gain of function mutations, clinical treatment trials (secondary outcome and toxicity biomarker) and provide prognostic information in neurocritical care if used within well defined time-frames.

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Section: Mass-spectrometrymentioning

confidence: 99%

Glial fibrillary acidic protein is a body fluid biomarker for glial pathology in human disease

Petzold

2015

Brain Research

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“…48 Despite tissue heterogeneity, the protein expression in the disk might not be representative for the entire tumor. 49 These new technologies have been used successfully to quantitatively and qualitatively characterize existing cancer markers in prostate cancer 50 and to detect several disease-associated proteins in tissue samples 51 or complex biological specimens, such as serum, 52 cerebrospinal fluid, 51 nipple aspirates, 53 pancreatic juice, 54 saliva, 55 and urine. 56 Although these technologies have demonstrated their suitability, they still provide only limited information about the spatial variability of the cancer proteome.…”

Section: Pathogenesismentioning

confidence: 99%

Head and neck cancer

Rezende

Freire

Franco

2010

Cancer

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Tumors of the head and neck comprise an important neoplasia group, the incidence of which is increasing in many parts of the world. Recent advances in diagnostic and therapeutic techniques for these lesions have yielded novel molecular targets, uncovered signal pathway dominance, and advanced early cancer detection. Proteomics is a powerful tool for investigating the distribution of proteins and small molecules within biological systems through the analysis of different types of samples. The proteomic profiles of different types of cancer have been studied, and this has provided remarkable advances in cancer understanding. This review covers recent advances for head and neck cancer; it encompasses the risk factors, pathogenesis, proteomic tools that can help in understanding cancer, and new proteomic findings in this type of cancer. Cancer 2010;116:4914-25.

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“…For each sample, a volume corresponding to 100 mg total protein (determined by Bradford protein assay) was aliquoted, dried down and labeled with iTRAQ TM 114-117 as described previously [24]. After iTRAQ TM labeling, equal volumes of the four samples were combined and 50 mL of the sample mixture was dried down under vacuum.…”

Section: Labeling Human Vcsf Samplesmentioning

confidence: 99%

“…This setup was used for the quantification of protein standards as well as in a case study to identify relative changes in proteome profiles in a set of ventricular cerebrospinal fluid (vCSF) samples collected from a patient recovering from traumatic brain injury (TBI). In a parallel study an evaluation of nanoLC-MALDI-TOF/TOF MS and iTRAQ TM labeling of potential protein biomarkers in vCSF have been performed [24]. PolyE-323 modified capillaries in CE [25] respectively, using the following procedure: The samples were redissolved in 20 mL dissolution buffer, 1 mL 1 M urea solution (instead of SDS as suggested in the standard protocol) for protein denaturation.…”

Section: Introductionmentioning

confidence: 99%

CE MALDI‐TOF/TOF MS for multiplexed quantification of proteins in human ventricular cerebrospinal fluid

et al. 2009

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CE, interfaced off-line to MALDI-TOF/TOF MS, was for the first time used to quantitatively monitor the protein content in complex biological and clinical samples with iTRAQ labeling. The usefulness and advantage of iTRAQ labeling, in combination, with CE MALDI-TOF/TOF MS is demonstrated on mixtures of protein standards and by a case study on human ventricular cerebrospinal fluid samples collected from a patient with traumatic brain injury during patient recovery. Mixtures of five standard proteins were initially analyzed to optimize the experimental conditions for the CE MALDI-MS and MS/MS analysis. The interactions of proteins and peptides with the capillary inner wall during CE separation were minimized using PolyE-323 modified capillaries. The analysis of the ventricular cerebrospinal fluid samples yielded 43 significantly (p < 0.05 MudPIT scoring) identified proteins that could be quantitatively monitored over time. The identified changes in protein levels for several of these proteins are well in line with the reports from previous studies on protein patterns that could be related to the post-traumatic processes of traumatic brain injury. This study shows that the presented approach, combining isobaric tags with CE MALDI-TOF/TOF MS, is a useful choice for quantitative proteomic analysis.

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Temporally resolved differential proteomic analysis of human ventricular CSF for monitoring traumatic brain injury biomarker candidates

Cited by 63 publications

References 44 publications

Glial fibrillary acidic protein is a body fluid biomarker for glial pathology in human disease

Glial fibrillary acidic protein is a body fluid biomarker for glial pathology in human disease

Head and neck cancer

CE MALDI‐TOF/TOF MS for multiplexed quantification of proteins in human ventricular cerebrospinal fluid

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