Application of LC/MS to proteomics studies: current status and future prospects

Chen, Guodong; Pramanik, Birendra N.

doi:10.1016/j.drudis.2009.02.007

Cited by 82 publications

(53 citation statements)

References 65 publications

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“…When coupled to chromatographic separations, MS is routinely used for characterization of therapeutic proteins [14][15][16][17] and in proteomics and biomarker discovery arenas for identification of low-abundance proteins across a dynamic range of 3-4 orders of magnitude in a variety of samples. 18,19 The combination of MS with two-dimensional gel electrophoresis has recently been applied for the identification of host-cell proteins co-purified with recombinant monoclonal antibodies 20 and with apolipoprotein A-I. 21 In addition, two recent reports describe the use of SELDI-TOF MS 22,23 and SDS-PAGE followed by 1D LC/MS/MS 23 for screening 22 and identification of HCPs 23 from purified recombinant proteins.…”

Section: Resultsmentioning

confidence: 99%

Analysis of host-cell proteins in biotherapeutic proteins by comprehensive online two-dimensional liquid chromatography/mass spectrometry

Doneanu

Xenopoulos

Fadgen

et al. 2012

mAbs

153

150

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Section: Resultsmentioning

confidence: 99%

Analysis of host-cell proteins in biotherapeutic proteins by comprehensive online two-dimensional liquid chromatography/mass spectrometry

Doneanu

Xenopoulos

Fadgen

et al. 2012

mAbs

153

150

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“…In addition, the technical reproducibility of high quality 2D gels is problematic for membrane proteins (Henningsen et al, 2002;Santoni et al, 2000) and, therefore, hampers the identification of low-abundance proteins of interest. Therefore, we proceeded by performing a qualitative comparison using nUPLC-ESI Q-TOF-MS/MS, an approach previously described as being highly sensitive (Chen & Pramanik, 2009;Old et al, 2005). Since it is also known that mass spectral peak intensities of peptide ions correlate well with protein abundances in complex samples (Chen & Pramanik, 2009) and since the MS search algorithm automatically analyses the most abundant proteins first, this approach appeared suitable for the analysis of differential protein expression.…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, we proceeded by performing a qualitative comparison using nUPLC-ESI Q-TOF-MS/MS, an approach previously described as being highly sensitive (Chen & Pramanik, 2009;Old et al, 2005). Since it is also known that mass spectral peak intensities of peptide ions correlate well with protein abundances in complex samples (Chen & Pramanik, 2009) and since the MS search algorithm automatically analyses the most abundant proteins first, this approach appeared suitable for the analysis of differential protein expression. It avoids the limitations of 2D gel electrophoresis in separating membrane proteins and the identification of proteins with a pI higher than 11 and a molecular mass below 15 or above 150 kDa.…”

Section: Discussionmentioning

confidence: 99%

Differential proteome analysis of Mycobacterium avium subsp. paratuberculosis grown in vitro and isolated from cases of clinical Johne's disease

Weigoldt¹,

Meens²,

Doll

et al. 2011

Microbiology

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Bovine Johne's disease (paratuberculosis), caused by Mycobacterium avium subspecies paratuberculosis, poses a significant economic problem to the beef and dairy industry worldwide. Despite its relevance, however, pathogenesis of Johne's disease is still only partially resolved. Since mycobacterial membrane proteins expressed during infection are likely to play an important role in pathogenesis, membrane-enriched fractions, namely mucosa-derived membranes (MDM) and culture-derived membranes (CDM), of M. avium subsp. paratuberculosis from three cows with clinical paratuberculosis were investigated. An initial analysis by 2D difference gel electrophoresis (2D DIGE) and MALDI-TOF-MS analysis revealed four differentially expressed proteins with only one predicted membrane protein. Due to this limited outcome, membrane preparations were subjected to a tube–gel trypsin digestion and investigated by using nanoflow-liquid-chromatography-coupled tandem MS. Based on this approach a total of 212 proteins were detected in MDM including 32 proteins of bovine origin; 275 proteins were detected in CDM; 59 % of MDM and CDM proteins were predicted to be membrane-associated. A total of 130 of the proteins were detected in both MDM and CDM and 48 predicted membrane proteins were detected in MDM from at least two cows. Four of these proteins were not detected in CDM, implying differential expression in the host. All membrane-associated proteins, especially the four identified as being differentially expressed, might be relevant targets for further analyses into the pathogenesis of bovine paratuberculosis.

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“…In typical conditions the LC is coupled on-line with mass spectrometer and the proteins/peptides eluted from an analytical column are directly injected into the mass spectrometer for identification and/or quantification [37].…”

Section: Proteomic Methods Applied For Dr Diagnosismentioning

confidence: 99%

Diabetic retinopathy: Proteomic approaches to help the differential diagnosis and to understand the underlying molecular mechanisms

Csősz

Deák

Kalló

et al. 2017

Journal of Proteomics

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a b s t r a c t a r t i c l e i n f oDiabetic retinopathy is the most common diabetic eye disease and a leading cause of blindness among patients with diabetes. The appearance and the severity of the symptoms correlate with the duration of diabetes and poor blood glucose level management. Diabetic retinopathy is also categorized as a chronic low-level inflammatory disease; the high blood glucose level promotes the accumulation of the advanced glycation end products and leads to the stimulation of monocytes and macrophages. Examination of protein level alterations in tears using state-of the art proteomics techniques have identified several proteins as possible biomarkers for the different stages of the diabetic retinopathy. Some of the differentially expressed tear proteins have a role in the barrier function of tears linking the diabetic retinopathy with another eye complication of diabetes, namely the diabetic keratopathy resulting in impaired wound healing. Understanding the molecular events leading to the eye complications caused by hyperglycemia may help the identification of novel biomarkers as well as therapeutic targets in order to improve quality of life of diabetic patients. Biological significance: Diabetic retinopathy (DR), the leading cause of blindness among diabetic patients can develop without any serious symptoms therefore the early detection is crucial. Because of the increasing prevalence there is a high need for improved screening methods able to diagnose DR as soon as possible. The non-invasive collection and the relatively high protein concentration make the tear fluid a good source for biomarker discovery helping the early diagnosis. In this work we have reviewed the administration of advanced proteomics techniques used in tear biomarker studies and the identified biomarkers with potential to improve the already existing screening methods for DR detection.

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Application of LC/MS to proteomics studies: current status and future prospects

Cited by 82 publications

References 65 publications

Analysis of host-cell proteins in biotherapeutic proteins by comprehensive online two-dimensional liquid chromatography/mass spectrometry

Analysis of host-cell proteins in biotherapeutic proteins by comprehensive online two-dimensional liquid chromatography/mass spectrometry

Differential proteome analysis of Mycobacterium avium subsp. paratuberculosis grown in vitro and isolated from cases of clinical Johne's disease

Diabetic retinopathy: Proteomic approaches to help the differential diagnosis and to understand the underlying molecular mechanisms

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