Analysis of differentially expressed proteins in cancerous and normal colonic tissues

Gam, Lay‐Harn; Leow, Chiuan Yee; Man, Che Nin; Gooi, Boon-Hui; Singh, Manjit

doi:10.3748/wjg.v12.i31.4973

Cited by 8 publications

(3 citation statements)

References 51 publications

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“…Protein spots of interest were excised from the Coomassie‐stained 2‐DE gels and processed for in‐gel digestion according to methods described before by Gam et al . (). Briefly, the gels were incubated in 100 mmol l −1 ammonium bicarbonate (NH 4 HCO 3 ) for 10 min followed by incubation in 100% acetonitrile (ACN) for 5 min.…”

Section: Methodsmentioning

confidence: 97%

Immunoproteomic analysis of antibody response to cell wall-associated proteins of Candida tropicalis

et al. 2014

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Section: Methodsmentioning

confidence: 97%

Immunoproteomic analysis of antibody response to cell wall-associated proteins of Candida tropicalis

et al. 2014

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“…In-situ protein digestion was performed as described by Gam et al [15]. In short, the proteins were reduced, alkylated and digested with trypsin.…”

Section: In-gel Protein Digestionmentioning

confidence: 99%

Proteomics and Detection of Uromodulin in First-time Renal Calculi Patients and Recurrent Renal Calculi Patients

Wai-Hoe

Wing-Seng²,

Ismail

et al. 2009

Appl Biochem Biotechnol

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Renal calculi disease or known as kidney stone disease is the most common urological disorder in both men and women, although it is more prevalent in men. The lifetime chance for an individual to develop renal calculi is~10% whereas the risk of recurrence in a 10-year period is 74%. Therefore, a diagnostic tool for screening or detecting renal calculi is greatly needed. In this study, we analyze urinary protein profiles from patients with renal calculi for the first time (RC), healthy subjects (HS), and patients with recurrent renal calculi (RRC) to identify a biomarker for detecting the disease. Urinary proteins were isolated by salt precipitation and the proteins resolved by SDS-PAGE. Target proteins were analyzed with LC/MS/MS. Thirty-two proteins were identified from healthy subjects and patients. Uromodulin was the most abundant urinary protein in HS but was a very faint band if detected at all from those that formed renal calculi for the first time (p< 0.05). Yet the excreted levels of urinary uromodulin in RRC were similar to those of the HS suggesting that uromodulin is a reliable biomarker for only RC. In addition, a few immunoglobulins that were commonly found in the urine of both RC and RRC, which include Ig alpha heavy chain 1, Ig gamma-2 c region, Ig gamma-3 heavy chain disease protein, Ig heavy chain variable region, Ig heavy constant region gamma 4, and Ig heavy chain. Ig heavy chain Fab frag and antibody a5b7 chain B may serve as potential biomarkers for renal calculi disease.

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“…Protein spots corresponding to the immunoreactive spots were manually excised from the Coomassie-stained 2-DE gels and prepared for in-gel digestion according to the method described by Gam et al (2006). Briefly, the gel pieces were first dehydrated in 100% acetonitrile (ACN) and rehydrated in 100 mmol l À1 ammonium bicarbonate (NH 4 HCO 3 ).…”

Section: In-gel Digestionmentioning

confidence: 99%

Identification of immunogenic proteins of Candida parapsilosis by serological proteome analysis

et al. 2014

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Aims Systemic candidiasis is the leading fungal bloodstream infection, and its incidence has been on the rise. Recently, Candida parapsilosis has emerged as an increasingly prevalent fungal pathogen, but little is known about its antigenic profile. Hence, the current work was performed to discover immunogenic proteins of C. parapsilosis using serological proteome analysis. Methods and Results Cell wall proteins extracted from C. parapsilosis were resolved by two‐dimensional electrophoresis followed by immunoblotting using antisera from experimentally infected mice. Mass spectrometry analysis of the 32 immunoreactive protein spots resulted in the identification of 12 distinct proteins. Among them, 11 proteins were known antigens of Candida albicans, whereas Idh2p was identified for the first time as an immunogenic protein of Candida species. Recombinant Idh2p was expressed in Escherichia coli, and its antigenicity was verified by immunoblot analysis. Conclusions An immunoproteomic approach was successfully applied to identify immunogenic proteins of C. parapsilosis, with Idh2p as a novel candidate antigen. The identified antigens may serve as potential biomarkers for development of diagnostic assay and/or vaccine for C. parapsilosis. Significance and Impact of the Study This work represents the first immunoproteomic analysis of C. parapsilosis, which provides new insights into host–pathogen interactions and pathogenesis of C. parapsilosis. The immunogenic proteins could be studied as biomarker candidates for C. parapsilosis.

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Analysis of differentially expressed proteins in cancerous and normal colonic tissues

Abstract: Many of the identified proteins have been reported to be involved in the progression of similar or other types of cancers. However, some of the identified proteins have not been reported before. In addition, a number of hypothetical proteins were also identified.

Cited by 8 publications

References 51 publications

Immunoproteomic analysis of antibody response to cell wall-associated proteins of Candida tropicalis

Immunoproteomic analysis of antibody response to cell wall-associated proteins of Candida tropicalis

Proteomics and Detection of Uromodulin in First-time Renal Calculi Patients and Recurrent Renal Calculi Patients

Identification of immunogenic proteins of Candida parapsilosis by serological proteome analysis

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