Electrophoretic pattern of concentrated urine: Comparison between 24-hour collection and random samples

Bottini, P.V.; Alves, Marília; Garlipp, Célia Regina

doi:10.1053/ajkd.2002.29920

Cited by 35 publications

(20 citation statements)

References 19 publications

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“…29,30 However, the collection of samples is cumbersome and inconvenient for the patient, leading to poor compliance, [7][8][9] and the laboratory treatment of the samples varies and can be laborious. 31,32 In addition, the excretion of BJP is affected by kidney function, and electrophoretic methods for quantifying the monoclonal protein in urine from patients with plasma cell dyscrasias can be insensitive.…”

Section: Discussionmentioning

confidence: 99%

Comparison of serum free light chain and urine electrophoresis for the detection of the light chain component of monoclonal immunoglobulins in light chain and intact immunoglobulin multiple myeloma

et al. 2015

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Section: Discussionmentioning

confidence: 99%

Comparison of serum free light chain and urine electrophoresis for the detection of the light chain component of monoclonal immunoglobulins in light chain and intact immunoglobulin multiple myeloma

et al. 2015

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“…from plasma via glomerular filtration, from renal tubular epithelial cells, from shedding of whole cells or membrane fragments along the tubulus and bladder or from exosome secretion [30,34]. According to recent recommendations for urinary proteomics [33], we collected second morning urine samples and added sodium azide instantly to minimise contamination of proteins from bacteria [3], which can change the urinary proteome profile [33]. We also removed cells and debris by centrifugation, and removed salts from urine samples by dialysis against water [33].…”

Section: Discussionmentioning

confidence: 99%

Variation in protein levels obtained from human blood cells and biofluids for platelet, peripheral blood mononuclear cell, plasma, urine and saliva proteomics

et al. 2009

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Blood cells and biofluid proteomics are emerging as a valuable tool to assess effects of interventions on health and disease. This study is aimed to assess the amount and variability of proteins from platelets, peripheral blood mononuclear cells (PBMC), plasma, urine and saliva from ten healthy volunteers for proteomics analysis, and whether protein yield is affected by prolonged fasting. Volunteers provided blood, saliva and morning urine samples once a week for 4 weeks after an overnight fast. Volunteers were fasted for a further 24 h after the fourth sampling before providing their final samples. Each 10 mL whole blood provided 400-1,500 lg protein from platelets, and 100-600 lg from PBMC. 30 lL plasma depleted of albumin and IgG provided 350-650 lg protein. A sample of morning urine provided 0.9-8.6 mg protein/dL, and a sample of saliva provided 70-950 lg protein/mL. None of these yields were influenced by the degree of fasting (overnight or 36 h). In conclusion, in contrast to the yields from plasma, platelets and PBMC, the protein yields of urine and saliva samples were highly variable within and between subjects. Certain disease conditions may cause higher or lower PBMC counts and thus protein yields, or increased urinary protein levels.

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“…For absolute quantification, a 24-h urine collection would be desirable. However, it is probably impractical to carry out quantitative collections for most biomarker discovery and validation studies because of low patient compliance and a history of unreliable results (51). An appropriate alternative is to collect spot urine samples and normalize the biomarker concentration by the creatinine concentration.…”

Section: Fig 4 Diagram Of Procedures For "Non-labeling" Protein Quanmentioning

confidence: 99%

Discovery of Urinary Biomarkers

Pisitkun

Johnstone

Knepper

2006

Molecular & Cellular Proteomics

360

315

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A myriad of proteins and peptides can be identified in normal human urine. These are derived from a variety of sources including glomerular filtration of blood plasma, cell sloughing, apoptosis, proteolytic cleavage of cell surface glycosylphosphatidylinositol-linked proteins, and secretion of exosomes by epithelial cells. Mass spectrometry-based approaches to urinary protein and peptide profiling can, in principle, reveal changes in excretion rates of specific proteins/peptides that can have predictive value in the clinical arena, e.g. in the early diagnosis of disease, in classification of disease with regard to likely therapeutic responses, in assessment of prognosis, and in monitoring response to therapy. These approaches have potential value, not only in diseases of the kidney and urinary tract but also in systemic diseases that are associated with circulating small protein and peptide markers that can pass the glomerular filter. Most large scale biomarker discovery studies reported thus far have used one of two approaches to identify proteins and peptides whose excretion in urine changes in specific disease states: 1) two-dimensional electrophoresis with mass spectrometric and/or immunochemical identification of proteins and 2) top-down mass spectrometric methods (SELDI-TOF-MS and capillary electrophoresis-MS). These studies have been chiefly in the areas of nephrology, urology, and oncology. We review these applications, focusing on two areas of progress, viz.

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Electrophoretic pattern of concentrated urine: Comparison between 24-hour collection and random samples

Cited by 35 publications

References 19 publications

Comparison of serum free light chain and urine electrophoresis for the detection of the light chain component of monoclonal immunoglobulins in light chain and intact immunoglobulin multiple myeloma

Comparison of serum free light chain and urine electrophoresis for the detection of the light chain component of monoclonal immunoglobulins in light chain and intact immunoglobulin multiple myeloma

Variation in protein levels obtained from human blood cells and biofluids for platelet, peripheral blood mononuclear cell, plasma, urine and saliva proteomics

Discovery of Urinary Biomarkers

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