Lectin‐based electrophoretic analysis of the expression of the 35 kDa inter‐α‐trypsin inhibitor heavy chain H4 fragment in sera of patients with five different malignancies

Mohamed, Emida; Abdul‐Rahman, Puteri Shafinaz; Doustjalali, Saeid Reza; Chen, Yeng; Lim, Boon Kiong; Omar, Siti Zawiah; Bustam, Anita Zarina; Singh, Vivek Ajit; Taib, Nur Aishah Mohd; Yip, Cheng Har; Hashim, Onn Haji

doi:10.1002/elps.200700828

Cited by 43 publications

(35 citation statements)

References 17 publications

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“…Inter-alpha-trypsin inhibitor heavy chain 4, which was also identified, is a plasma glycoprotein that acts as an acute-phase protein in several species. This protein and its cleavage fragments are also candidate biomarkers associated with different malignant diseases [26,27]. Serum amyloid, transthyretin and inter-alpha-trypsin inhibitor heavy chain 4 were not detected in the urine of AAIItreated mice.…”

Section: Discussionmentioning

confidence: 99%

SELDI‐TOF as a method for biomarker discovery in the urine of aristolochic‐acid‐treated mice

et al. 2009

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Aristolochic acids (AAs) present in Aristolochia plants are substances responsible for Chinese herbs nephropathy. Recently, strong indications have also been presented, which dietary poisoning with AA is responsible for endemic (Balkan) nephropathy (EN), an enigmatic renal disease that affects rural population living in some countries in Southeastern Europe. A mouse model was applied to follow the effects of two forms of AA, AAI and AAII. SDS-PAGE and SELDI-TOF mass spectrometry with normal phase chips were used to evaluate changes in the urine of treated animals. These two methods are demonstrated to be comparable. The use of SELDI-TOF MS for rapid analysis of a large number of samples and the combination of this method with nano-LC-ESI MS/MS for protein identification were demonstrated. Biomarker discovery after analysis of large cohort of EN patients will be the final aim of these investigations.

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Section: Discussionmentioning

confidence: 99%

SELDI‐TOF as a method for biomarker discovery in the urine of aristolochic‐acid‐treated mice

et al. 2009

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“…Aside from the use of pre-cast immobilline drystrips pH 3-10 (GE Healthcare Bio-Sciences, Uppsala, Sweden), 2-DE was performed as reported previously [14,15]. Briefly, albumin and IgG-depleted pooled serum samples (30 mg) and bound fractions from the immobilized CMB affinity isolation (30 mg) were subjected to isoelectric focusing using the Multiphor Flatbed electrophoresis system (GE Healthcare Bio-Sciences).…”

Section: -Dementioning

confidence: 99%

Application of champedak mannose‐binding lectin in the glycoproteomic profiling of serum samples unmasks reduced expression of alpha‐2 macroglobulin and complement factor B in patients with nasopharyngeal carcinoma

et al. 2010

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The use of lectin affinity chromatography prior to 2-DE separation forms an alternative method to unmask the expression of targeted glycoproteins of lower abundance in serum samples. Reduced expression of alpha-2 macroglobulin (AMG) and complement factor B (CFB) was detected in sera of patients with nasopharyngeal carcinoma (NPC) when pooled serum samples of the patients and those of healthy individuals were subjected to affinity isolation using immobilized champedak mannose-binding lectin and analyzed by 2-DE and densitometry. The AMG and CFB spots were not detected in the 2-DE protein profiles when the same pooled serum samples were subjected to albumin and IgG depletion and neither were they detected when the depleted samples were analyzed by western blotting and lectin detection. Together with other acute-phase response proteins that were previously reported to be altered in expression in NPC patients, AMG and CFB may serve as useful complementary biomarkers for NPC.

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“…Heavy chain H4 of this protein has potential diagnostic value, and it has also been topic of proteomic and glycomic analysis [154]. Weber et al [155] recently described an industrial scale process for production of butyrylcholinesterase.…”

Section: Further Plasma Proteins Considered For Therapeutic Usementioning

confidence: 99%

Therapeutic plasma proteins – application of proteomics in process optimization, validation, and analysis of the final product

et al. 2011

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An overview is given on the application of proteomic technology in the monitoring of different steps during the production of therapeutic proteins from human plasma. Recent advances in this technology enable the use of proteomics as an advantageous tool for the validation of already existing processes, the development and fine tuning of new production steps, the characterization and quality control of final products, the detection of both harmful impurities and modifications of the therapeutic protein and the auditing of batch-to-batch variations. Further, use of proteomics for preclinical testing of new products, which can be either recombinant or plasma-derived, is also discussed.

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Lectin‐based electrophoretic analysis of the expression of the 35 kDa inter‐α‐trypsin inhibitor heavy chain H4 fragment in sera of patients with five different malignancies

Cited by 43 publications

References 17 publications

SELDI‐TOF as a method for biomarker discovery in the urine of aristolochic‐acid‐treated mice

SELDI‐TOF as a method for biomarker discovery in the urine of aristolochic‐acid‐treated mice

Application of champedak mannose‐binding lectin in the glycoproteomic profiling of serum samples unmasks reduced expression of alpha‐2 macroglobulin and complement factor B in patients with nasopharyngeal carcinoma

Therapeutic plasma proteins – application of proteomics in process optimization, validation, and analysis of the final product

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