Composition of the peptide fraction in human blood plasma: database of circulating human peptides

Richter, Rudolf; Schulz‐Knappe, Peter; Schrader, Michael; Ständker, Ludger; Jürgens, Michael; Tammen, Harald; Forssmann, Wolf‐Georg

doi:10.1016/s0378-4347(99)00012-2

Cited by 184 publications

(153 citation statements)

References 26 publications

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“…Developments in mass spectrometry, particularly in SELDI-TOF and, more recently, in high-resolution mass spectrometry, offer several substantial advantages over traditional biomarker discovery tools such as 2-dimensional gels (27,28). First, mass spectrometry is the preferred approach to the detection of low molecular weight protein fragments, peptides, and metabolites that are smaller than 10,000 daltons (7,29,30).…”

Section: Discussionmentioning

confidence: 99%

A serum proteomic approach to gauging the state of remission in Wegener's granulomatosis

Stone

Rajapakse

Hoffman

et al. 2005

Arthritis & Rheumatism

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Objective. To identify serum ion patterns that distinguish remission from active disease in patients with Wegener's granulomatosis (WG).Methods. Using sera collected in the WG Etanercept Trial, we selected samples from patients who either were undergoing a period of extended disease remission or had recent flares of active WG. Unfractionated samples were randomized into sets for training and testing, such that remission sera and active disease sera could be analyzed without batch bias. Molecular species within the sera were ionized by high-resolution, matrixassisted laser desorption ionization time-of-flight mass spectrometry. We then used a bioinformatics patternrecognition tool to identify optimal combinations of ions. During the training stage, the clinical data (remission versus active disease) were provided in association with the spectral data from each sample. In the testing stage, we performed blinded testing on a previously unexamined set of samples.Results Conclusion. This serum proteomic profiling approach appears to be useful in distinguishing between states of stable clinical remission and active disease.

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Section: Discussionmentioning

confidence: 99%

A serum proteomic approach to gauging the state of remission in Wegener's granulomatosis

Stone

Rajapakse

Hoffman

et al. 2005

Arthritis & Rheumatism

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“…Inversely, many peptides, absent in plasma but detectable in serum, can be identified after coagulation. It is therefore of importance to have good preanalytical conditions when mining the proteome of plasma, and more particularly its "peptidome", in which about 5000 peptides have been revealed [22]. Over 10 000 different proteins have been estimated to be commonly present in the plasma, most of which are at very low relative abundances [23].…”

Section: Overviewmentioning

confidence: 99%

“…These proteins included six known substrates for the protease and nine potential ones. Such an approach, combined with the study of plasma peptidome [102] will be interesting to evaluate other proteases as well as the effect on plasma proteins of systemic fibrinolytic treatments that are currently used to treat patients after cardiovascular events such as heart infarction [103]. "Degradomics" and "peptidomics" will be certainly also useful to restudy the coagulation cascade, the activation either of the complement or of the fibrinolytic pathways.…”

Section: Degradomics and Peptidomicsmentioning

confidence: 99%

Recent advances in blood‐related proteomics

et al. 2005

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Service régional vaudois de transfusion sanguine, Lausanne, SwitzerlandBlood is divided in two compartments, namely, plasma and cells. The latter contain red blood cells, leukocytes, and platelets. From a descriptive medical discipline, hematology has evolved towards a pioneering discipline where molecular biology has permitted the development of prognostic and diagnostic indicators for disease. The recent advance in MS and protein separation now allows similar progress in the analysis of proteins. Proteomics offers great promise for the study of proteins in plasma/serum, indeed a number of proteomics databases for plasma/ serum have been established. This is a very complex body fluid containing lipids, carbohydrates, amino acids, vitamins, nucleic acids, hormones, and proteins. About 1500 different proteins have recently been identified, and a number of potential new markers of diseases have been characterized. Here, examples of the enormous promise of plasma/serum proteomic analysis for diagnostic/prognostic markers and information on disease mechanism are given. Within the blood are also a large number of different blood cell types that potentially hold similar information. Proteomics of red blood cells, until now, has not improved our knowledge of these cells, in contrast to the major progresses achieved while studying platelets and leukocytes. In the future, proteomics will change several aspects of hematology.

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“…On the other hand, some proteases in the urine still keep their activity at pH 2.7, thus still capable of degrading other proteins into fragments. It was reported that urine and other body fluid samples were acidified to pH 2.7 with hydrochloric acid immediately to prevent bacterial growth before analysis [6,30,46]. To check whether adjusting of the pH would affect the stability of the peptides in urine, the peptides in native state urine sample and acidified urine sample (pH 2.7) were extracted using the same procedure.…”

Section: Extraction Of the Peptides From Urinementioning

confidence: 99%

Analysis of the human urine endogenous peptides by nanoparticle extraction and mass spectrometry identification

Yang

et al. 2014

Analytica Chimica Acta

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Composition of the peptide fraction in human blood plasma: database of circulating human peptides

Cited by 184 publications

References 26 publications

A serum proteomic approach to gauging the state of remission in Wegener's granulomatosis

A serum proteomic approach to gauging the state of remission in Wegener's granulomatosis

Recent advances in blood‐related proteomics

Analysis of the human urine endogenous peptides by nanoparticle extraction and mass spectrometry identification

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