Assessment of protein stability in cerebrospinal fluid using surface-enhanced laser desorption/ionization time-of-flight mass spectrometry protein profiling

Ranganathan, Srikanth; Polshyna, Anna; Nicholl, Georgina C.B.; Lyons‐Weiler, James; Bowser, Robert

doi:10.1385/cp:2:1:91

Cited by 17 publications

(16 citation statements)

References 22 publications

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“…The ratio of males to females in the living subject cohort was 1.8:1 and in the autopsy cohort was 1.5:1. Acquisition of CSF and processing was performed as previously described (14).…”

Section: Study Populationmentioning

confidence: 99%

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Comparative proteomic profiling of cerebrospinal fluid between living and post mortem ALS and control subjects

Ranganathan

Nicholl

Henry

et al. 2007

Amyotrophic Lateral Sclerosis

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Neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), lack definitive diagnostic tests or biomarkers of disease progression. Most studies that investigate protein abnormalities in ALS have used biofluids such as blood or cerebrospinal fluid (CSF), while some have used post mortem tissue or CSF samples. Since ALS disease progression and post mortem effects probably induce significant alterations to protein modifications or proteolysis, we directly examined the CSF proteome from ALS subjects at various lengths of time from symptom onset and at autopsy by mass spectrometry based proteomics. CSF was also obtained from both healthy agematched control subjects and at autopsy from healthy and Alzheimer's disease (AD) controls. We identified significant differences in the CSF proteome between living and post mortem ALS subjects, as well as living and post mortem control subjects. We also noted differences in the CSF proteome of ALS subjects that have exhibited symptoms for varying lengths of time and between ALS and AD subjects at end-stage of disease. This is the first study describing differences in the CSF proteome from post mortem and living ALS subjects using a mass spectrometric approach. These differences highlight the importance of utilizing CSF from living ALS subjects near the time of symptom onset for the identification of early protein biomarkers, although some protein alterations that occur early in the disease process are maintained throughout the course of disease and in post mortem samples.

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“…The ratio of males to females in the living subject cohort was 1.8:1 and in the autopsy cohort was 1.5:1. Acquisition of CSF and processing was performed as previously described (14).…”

Section: Study Populationmentioning

confidence: 99%

“…We recently reported standard procedures to properly acquire and store human CSF samples to maintain proteome stability as assessed by mass spectrometry (14). We have used this CSF protocol to uncover a panel of protein biomarkers in the CSF of patients recently diagnosed with ALS (7).…”

Section: Introductionmentioning

confidence: 99%

Comparative proteomic profiling of cerebrospinal fluid between living and post mortem ALS and control subjects

Ranganathan

Nicholl

Henry

et al. 2007

Amyotrophic Lateral Sclerosis

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“…Samples analysed in this study were left over specimens following normal microbiology and chemistry laboratory procedures. There is lacking data for the samples on the time taken from collection during lumbar puncture to storage at -80°C and therefore there is possibility that proteome changes occurred during that period 49 . Label-free proteomics are cost-efficient, offer higher proteome coverage and a higher dynamic range.…”

Section: Discussionmentioning

confidence: 99%

“…The authors need to say more on how the samples were originally collected, how long it took before they were stored and at what temperature. They may also need to add this as a limitation in the Discussion section bearing in mind that the stability of CSF proteins is compromised if kept under different temperatures for some time (Ranganathan et al , 2006 2 ). Definition of CM: although archive CSF samples were used, i have strong reservation with the criteria used in defining CM cases.…”

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confidence: 99%

Cerebrospinal fluid markers to distinguish bacterial meningitis from cerebral malaria in children

Njunge¹,

Oyaro²,

Kibinge³

et al. 2017

Wellcome Open Res

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Background . Few hospitals in high malaria endemic countries in Africa have the diagnostic capacity for clinically distinguishing acute bacterial meningitis (ABM) from cerebral malaria (CM). As a result, empirical use of antibiotics is necessary. A biochemical marker of ABM would facilitate precise clinical diagnosis and management of these infections and enable rational use of antibiotics. Methods. We used label-free protein quantification by mass spectrometry to identify cerebrospinal fluid (CSF) markers that distinguish ABM (n=37) from CM (n=22) in Kenyan children. Fold change (FC) and false discovery rates (FDR) were used to identify differentially expressed proteins. Subsequently, potential biomarkers were assessed for their ability to discriminate between ABM and CM using receiver operating characteristic (ROC) curves. Results. The host CSF proteome response to ABM ( Haemophilus influenza and Streptococcus pneumoniae) is significantly different to CM. Fifty two proteins were differentially expressed (FDR<0.01, Log FC≥2), of which 83% (43/52) were upregulated in ABM compared to CM. Myeloperoxidase and lactotransferrin were present in 37 (100%) and 36 (97%) of ABM cases, respectively, but absent in CM (n=22). Area under the ROC curve (AUC), sensitivity, and specificity were assessed for myeloperoxidase (1, 1, and 1; 95% CI, 1-1) and lactotransferrin (0.98, 0.97, and 1; 95% CI, 0.96-1). Conclusion. Myeloperoxidase and lactotransferrin have a high potential to distinguish ABM from CM and thereby improve clinical management. Their validation requires a larger cohort of samples that includes other bacterial aetiologies of ABM.

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“…While most acknowledge that standard operating procedures for the collection and storage of clinical samples are required for clinical proteomic biomarker discovery and validation efforts,46 few individual studies have carefully defined such standard operating procedures 35, 47. Additional standard operating procedures must be developed for any sample processing step necessary to enrich the biomarker prior to analysis as well as the methods for data capture, normalization, and statistical analysis.…”

Section: Necessary Diagnostic Assay Validation Steps Required To Impamentioning

confidence: 99%

Applying proteomics to the diagnosis and treatment of ALS and related diseases

Bowser

Lacomis

2009

Muscle and Nerve

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Protein-based biomarkers for amyotrophic lateral sclerosis (ALS) and other motor neuron diseases (MNDs) have many potential clinical utilities, including diagnostic, prognostic, and drug development indications. During the past decade a number of potential protein biomarkers have been proposed for MNDs. Further verification studies, followed by large validation and qualification studies, are required to advance these initial discoveries toward clinical use. Study of additional patient populations, including disease mimics, is required during the validation phase of biomarker development. Important regulatory issues are discussed that will affect the timing and strategy for biomarker assay development in ALS and other MNDs. The continued development of protein biomarkers for MNDs requires extensive collaboration between academic clinicians and scientists in conjunction with the biotechnology and pharmaceutical industries.

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Assessment of protein stability in cerebrospinal fluid using surface-enhanced laser desorption/ionization time-of-flight mass spectrometry protein profiling

Cited by 17 publications

References 22 publications

Comparative proteomic profiling of cerebrospinal fluid between living and post mortem ALS and control subjects

Comparative proteomic profiling of cerebrospinal fluid between living and post mortem ALS and control subjects

Cerebrospinal fluid markers to distinguish bacterial meningitis from cerebral malaria in children

Applying proteomics to the diagnosis and treatment of ALS and related diseases

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