دورية أكاديمية
أعرض في EDS

Differential denaturation of serum proteome reveals a significant amount of hidden information in complex mixtures of proteins.

التفاصيل البيبلوغرافية
العنوان: Differential denaturation of serum proteome reveals a significant amount of hidden information in complex mixtures of proteins.
المؤلفون: Verdoliva V; Dip. Ematologia, Oncologia e Medicina Molecolare, Istituto Superiore di Sanità, Roma, Italy., Senatore C, Polci ML, Rossi S, Cordella M, Carlucci G, Marchetti P, Antonini-Cappellini G, Facchiano A, D'Arcangelo D, Facchiano F
المصدر: PloS one [PLoS One] 2013; Vol. 8 (3), pp. e57104. Date of Electronic Publication: 2013 Mar 22.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Blood Proteins/*chemistry , Blood Proteins/*metabolism , Proteomics/*methods, Animals ; Cell Line, Tumor ; Cells, Cultured ; Computational Biology ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Humans ; Male ; Mass Spectrometry ; Mice ; Mice, Inbred C57BL ; Protein Folding ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
مستخلص: Unlabelled: Recently developed proteomic technologies allow to profile thousands of proteins within a high-throughput approach towards biomarker discovery, although results are not as satisfactory as expected. In the present study we demonstrate that serum proteome denaturation is a key underestimated feature; in fact, a new differential denaturation protocol better discriminates serum proteins according to their electrophoretic mobility as compared to single-denaturation protocols. Sixty nine different denaturation treatments were tested and the 3 most discriminating ones were selected (TRIDENT analysis) and applied to human sera, showing a significant improvement of serum protein discrimination as confirmed by MALDI-TOF/MS and LC-MS/MS identification, depending on the type of denaturation applied. Thereafter sera from mice and patients carrying cutaneous melanoma were analyzed through TRIDENT. Nine and 8 protein bands were found differentially expressed in mice and human melanoma sera, compared to healthy controls (p<0.05); three of them were found, for the first time, significantly modulated: α2macroglobulin (down-regulated in melanoma, p<0.001), Apolipoprotein-E and Apolipoprotein-A1 (both up-regulated in melanoma, p<0.04), both in mice and humans. The modulation was confirmed by immunological methods. Other less abundant proteins (e.g. gelsolin) were found significantly modulated (p<0.05).
Conclusions: i) serum proteome contains a large amount of information, still neglected, related to proteins folding; ii) a careful serum denaturation may significantly improve analytical procedures involving complex protein mixtures; iii) serum differential denaturation protocol highlights interesting proteomic differences between cancer and healthy sera.
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المشرفين على المادة: 0 (Blood Proteins)
تواريخ الأحداث: Date Created: 20130328 Date Completed: 20130911 Latest Revision: 20211021
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC3606341
DOI: 10.1371/journal.pone.0057104
PMID: 23533572
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0057104