Protein identification and quantification from riverbank grape, Vitis riparia : Comparing SDS-PAGE and FASP-GPF techniques for shotgun proteomic analysis

PROTEOMICS ◽  
2015 ◽  
Vol 15 (17) ◽  
pp. 3061-3065 ◽  
Author(s):  
Iniga S. George ◽  
Anne Y. Fennell ◽  
Paul A. Haynes
Keyword(s):  
Proteomic Analysis ◽  
Protein Identification ◽  
Vitis Riparia ◽  
Sds Page ◽  
Identification And Quantification

scholarly journals Protocol Optimization of Proteomic Analysis of Korean Ginseng (Panax ginseng Meyer)

Separations ◽  
2021 ◽  
Vol 8 (4) ◽  
pp. 53
Author(s):  
Clarissa Braccia ◽  
Bhakti Prinsi ◽  
Mara Colzani ◽  
Alessandra A. Altomare ◽  
Luca Espen ◽  
...  
Keyword(s):  
Panax Ginseng ◽  
Proteomic Analysis ◽  
Metabolic Pathways ◽  
Extraction Procedure ◽  
Biotic Stresses ◽  
Phenol Extraction ◽  
Ms Analysis ◽  
Sds Page ◽  
Protein Properties ◽  
Korean Ginseng

The benefits of ginseng have been mainly attributed to its triterpenoids, called ginsenosides. Recent genome sequencing of the Panax ginseng has paved the way for in-depth proteomic studies of this medicinal plant. The current study was conducted to deepen the proteomic information on the root proteome of Korean ginseng. Proteomic workflow was optimized by testing two different strategies, characterized by the phenol extraction procedure, the presence or the absence of SDS-PAGE fractionation step, and nano-scale liquid chromatographic tandem mass spectrometry (nLC-MS/MS) analysis. The results highlighted an evident improvement of proteome extraction by the combination of phenol extraction with SDS-PAGE before the nLC-MS/MS analysis. In addition, a dramatic impact of the steaming process (the treatment to produce red ginseng from ginseng) on protein properties was observed. Overall, the analyses of Korean ginseng permitted the characterization of a total of 2412 proteins. A large number of identified proteins belonged to the functional categories of protein and carbon/energy metabolism (22.4% and 14.6%, respectively). The primary and secondary metabolisms are major metabolic pathways, which emerged from the proteomic analysis. In addition, a large number of proteins known to play an important role in response to (a)biotic stresses were also identified. The current proteomic study not only confirmed the previous transcriptomic and proteomic reports but also extended proteomic information, including the main metabolic pathways involved in Korean ginseng.

scholarly journals Proteomic Identification of Altered Cerebral Proteins in the Complex Regional Pain Syndrome Animal Model

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Francis Sahngun Nahm ◽  
Zee-Yong Park ◽  
Sang-Soep Nahm ◽  
Yong Chul Kim ◽  
Pyung Bok Lee
Keyword(s):  
Animal Model ◽  
Complex Regional Pain Syndrome ◽  
Proteomic Analysis ◽  
Protein Identification ◽  
Pain Syndrome ◽  
Differentially Expressed ◽  
Control Groups ◽  
Altered Expression ◽  
Rat Cerebrum ◽  
And Control

Background. Complex regional pain syndrome (CRPS) is a rare but debilitating pain disorder. Although the exact pathophysiology of CRPS is not fully understood, central and peripheral mechanisms might be involved in the development of this disorder. To reveal the central mechanism of CRPS, we conducted a proteomic analysis of rat cerebrum using the chronic postischemia pain (CPIP) model, a novel experimental model of CRPS.Materials and Methods. After generating the CPIP animal model, we performed a proteomic analysis of the rat cerebrum using a multidimensional protein identification technology, and screened the proteins differentially expressed between the CPIP and control groups.Results. A total of 155 proteins were differentially expressed between the CPIP and control groups: 125 increased and 30 decreased; expressions of proteins related to cell signaling, synaptic plasticity, regulation of cell proliferation, and cytoskeletal formation were increased in the CPIP group. However, proenkephalin A, cereblon, and neuroserpin were decreased in CPIP group.Conclusion. Altered expression of cerebral proteins in the CPIP model indicates cerebral involvement in the pathogenesis of CRPS. Further study is required to elucidate the roles of these proteins in the development and maintenance of CRPS.

Proteomic analyses of normal and malignant breast tissue—Identification of a tumor-specific protein expression profile

2006 ◽  
Vol 24 (18_suppl) ◽  
pp. 10524-10524
Author(s):  
G. Hudelist ◽  
C. Singer ◽  
K. Pischinger ◽  
K. Kaserer ◽  
M. Manavi ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Gene Expression ◽  
Protein Expression ◽  
Antineoplastic Therapy ◽  
Proteomic Analysis ◽  
Protein Identification ◽  
Traditional Approach ◽  
Specific Protein ◽  
2D Page ◽  
Malignant Breast

10524 Background: Gene expression analysis has become a promising tool in predicting the clinical course of malignant disease and the response to antineoplastic therapy. Suprisingly, only little is known about the protein expression pattern of human tumors. Recent advances in proteomic analysis allow to identify proteins of interest by their expression and/or modification pattern in 2D-PAGE rather than using the traditional approach of translating gene expression data. Methods: In order to identify a proteomic pattern that is characteristic for malignant breast epithelium, we performed differential 2D-PAGE analysis in sets of microdissected malignant breast epithelia and corresponding adjacent normal breast epithelia from 5 patients with invasive breast carcinoma. Results: Thirty-two protein spots were found to be selectively regulated in malignant epithelium, and were subjected to MALDI-TOF and/or immunoblotting for protein identification. Thirteen of the identified proteins had previously not been associated with breast cancer. The validity of these findings was confirmed by literature review and immunohistochemistry for identified proteins in an independent cohort of 50 breast cancer specimens. Conclusions: We here describe a proteomic analysis of matched normal and malignant epithelia from invasive breast carcinomas. This strategy leads to a better understanding of oncogenesis at an operational level and helps to characterize the malignant phenotype of individual tumors and thereby to identify novel targets for antineoplastic therapy. No significant financial relationships to disclose.

Differentially isotope-coded N-terminal protein sulphonation: Combining protein identification and quantification

PROTEOMICS ◽  
2006 ◽  
Vol 6 (8) ◽  
pp. 2338-2349 ◽  
Author(s):  
Elisabeth Guillaume ◽  
Alexandre Panchaud ◽  
Michael Affolter ◽  
Valérie Desvergnes ◽  
Martin Kussmann
Keyword(s):  
Protein Identification ◽  
Terminal Protein ◽  
Identification And Quantification
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