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Quantitative Proteomic Analysis of Meningiomas for the Identification of Surrogate Protein Markers

View Article: PubMed Central - PubMed

ABSTRACT

Meningiomas are the most common non-glial tumors of the brain and spine. Pathophysiology and definite histological grading of meningiomas are frequently found to be deceptive due to their unusual morphological features and locations. Here for the first time we report a comprehensive serum proteomic analysis of different grades of meningiomas by using multiple quantitative proteomic and immunoassay-based approaches to obtain mechanistic insights about disease pathogenesis and identify grade specific protein signatures. In silico functional analysis revealed modulation of different vital physiological pathways including complement and coagulation cascades, metabolism of lipids and lipoproteins, immune signaling, cell growth and apoptosis and integrin signaling in meningiomas. ROC curve analysis demonstrated apolipoprotein E and A-I and hemopexin as efficient predictors for meningiomas. Identified proteins like vimentin, alpha-2-macroglobulin, apolipoprotein B and A-I and antithrombin-III, which exhibited a sequential increase in different malignancy grades of meningiomas, could serve as potential predictive markers.

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Differentially expressed serum proteins in different grades of meningiomas identified using 2D-DIGE.Trend of few selected differentially expressed serum proteins in different grades of meningiomas represented as standardized log abundance of spot intensity.
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f2: Differentially expressed serum proteins in different grades of meningiomas identified using 2D-DIGE.Trend of few selected differentially expressed serum proteins in different grades of meningiomas represented as standardized log abundance of spot intensity.

Mentions: In DeCyder 2D software analysis approximately 1500 protein spots were detected on each 2D-DIGE gels. Comparative serum proteome analysis of the healthy controls and different grades of meningioma patients revealed differential expression of 41 and 24 protein spots (p < 0.05) in MGI and MGII, respectively (Table S2 and Table S3). In grade I meningioma, among the 41 differentially expressed protein spots, 20 spots exhibited reduced expression, while the remaining 21 spots were up-regulated (Table S2; Figure S1A). In grade II meningioma, expression level of 14 protein spots was elevated, whereas 10 spots were found to be down-regulated (Table S3; Figure S1B). Identity of 27 and 10 protein spots in MGI and MGII, respectively, was established by the subsequent MALDI-TOF/TOF MS analysis (Table S4 and Table S5). Few spots remained unidentified due to the extremely low intensity of those spots and inadequate quantity of detectable peptides. Alpha-1-antitrypsin, Ig kappa chain, serum albumin, hemopexin and haptoglobin were identified as multiple spots in 2D-DIGE gels most likely due to the presence of multiple isoforms (Table S4 and Table S5). DIGE gel images, 3D views and graphical representation of selected protein spots in MGI and MGII are shown in Figure S1. Among the identified differentially expressed proteins, 6 candidates; hemopexin, serum albumin, haptoglobin, alpha-2-macroglobulin, apolipoprotein A-I and serotransferrin were found to be commonly altered in grade I and grade II meningiomas, however levels of differential expression (fold-changes) was found to be different (Figure 2).


Quantitative Proteomic Analysis of Meningiomas for the Identification of Surrogate Protein Markers
Differentially expressed serum proteins in different grades of meningiomas identified using 2D-DIGE.Trend of few selected differentially expressed serum proteins in different grades of meningiomas represented as standardized log abundance of spot intensity.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC5382771&req=5

f2: Differentially expressed serum proteins in different grades of meningiomas identified using 2D-DIGE.Trend of few selected differentially expressed serum proteins in different grades of meningiomas represented as standardized log abundance of spot intensity.
Mentions: In DeCyder 2D software analysis approximately 1500 protein spots were detected on each 2D-DIGE gels. Comparative serum proteome analysis of the healthy controls and different grades of meningioma patients revealed differential expression of 41 and 24 protein spots (p < 0.05) in MGI and MGII, respectively (Table S2 and Table S3). In grade I meningioma, among the 41 differentially expressed protein spots, 20 spots exhibited reduced expression, while the remaining 21 spots were up-regulated (Table S2; Figure S1A). In grade II meningioma, expression level of 14 protein spots was elevated, whereas 10 spots were found to be down-regulated (Table S3; Figure S1B). Identity of 27 and 10 protein spots in MGI and MGII, respectively, was established by the subsequent MALDI-TOF/TOF MS analysis (Table S4 and Table S5). Few spots remained unidentified due to the extremely low intensity of those spots and inadequate quantity of detectable peptides. Alpha-1-antitrypsin, Ig kappa chain, serum albumin, hemopexin and haptoglobin were identified as multiple spots in 2D-DIGE gels most likely due to the presence of multiple isoforms (Table S4 and Table S5). DIGE gel images, 3D views and graphical representation of selected protein spots in MGI and MGII are shown in Figure S1. Among the identified differentially expressed proteins, 6 candidates; hemopexin, serum albumin, haptoglobin, alpha-2-macroglobulin, apolipoprotein A-I and serotransferrin were found to be commonly altered in grade I and grade II meningiomas, however levels of differential expression (fold-changes) was found to be different (Figure 2).

View Article: PubMed Central - PubMed

ABSTRACT

Meningiomas are the most common non-glial tumors of the brain and spine. Pathophysiology and definite histological grading of meningiomas are frequently found to be deceptive due to their unusual morphological features and locations. Here for the first time we report a comprehensive serum proteomic analysis of different grades of meningiomas by using multiple quantitative proteomic and immunoassay-based approaches to obtain mechanistic insights about disease pathogenesis and identify grade specific protein signatures. In silico functional analysis revealed modulation of different vital physiological pathways including complement and coagulation cascades, metabolism of lipids and lipoproteins, immune signaling, cell growth and apoptosis and integrin signaling in meningiomas. ROC curve analysis demonstrated apolipoprotein E and A-I and hemopexin as efficient predictors for meningiomas. Identified proteins like vimentin, alpha-2-macroglobulin, apolipoprotein B and A-I and antithrombin-III, which exhibited a sequential increase in different malignancy grades of meningiomas, could serve as potential predictive markers.

No MeSH data available.


Related in: MedlinePlus