The Development of a Radioimmunoassay for the Measurement of Urinary Tammhorsfall Glycoprotein in the Presence of Sodium Dodecyl Sulphate

Grant, Anne M. S.; Neuberger, A.

doi:10.1042/cs0440163

Cited by 48 publications

(14 citation statements)

References 16 publications

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“…The procedure for the determination of THglycoprotein in urine was based on the method described by Grant & Neuberger (1973). These authors used a system involving antibodycoated tubes and iodinated TH-glycoprotein.…”

Section: Selection Of Radioimmunoassay Proceduresmentioning

confidence: 99%

“…In the procedure developed for the assay of TH-glycoprotein in urine (Grant & Neuberger, 1973), sodium dodecyl sulphate at 11 mg/l and overnight incubation at 37°C was used to dissociate the TH-glycoprotein. This concentration of sodium dodecyl sulphate was then reduced by dilution to 5 mg/l before assay in order to obtain optimum slope and linearity.…”

Section: Dissociation Of Th-glycoprotein In Serummentioning

confidence: 99%

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The Development of a Radioimmunoassay Procedure for the Estimation of Tamm—Horsfall Glycoprotein in Human Serum

Avis

1977

Clinical Science

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1. A quantitative radioimmunoassay was developed for the measurement of nanogram amounts of Tamm-Horsfall (TH) glycoprotein in the presence of serum proteins at concentrations above 30 mg/ml. 2. Specific anti-(TH-glycoprotein) antibodies were labelled with 125I and these were usable for a period of 8 weeks. 3. Agarose beads (Sepharose 4B), to which TH-glycoprotein had been coupled via cyanogen bromide activation of the Sepharose, were used as the solid phase in the assay. This proved stable upon storage at 4 degrees C for periods in excess of 4 months. 4. The dissociation of the glycoprotein in the presence of serum proteins that was necessary for quantification was achieved by subjecting the sample to ultrasonication. 5. Assays conducted on a small sample of normal serum produced evidence that normal serum contained amounts (50-180 ng/ml) of a substance that reacted similarly to TH-glycoprotein in the assay procedure and in a series of experiments conducted to confirm the presence of this substance in human serum.

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Section: Selection Of Radioimmunoassay Proceduresmentioning

confidence: 99%

Section: Dissociation Of Th-glycoprotein In Serummentioning

confidence: 99%

The Development of a Radioimmunoassay Procedure for the Estimation of Tamm—Horsfall Glycoprotein in Human Serum

Avis

1977

Clinical Science

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“…The glycoprotein has since become known as Tamm-Horsfall glycoprotein (THGP). THGP is the most abundant protein in normal urine, about 50 mg of it being excreted daily [4]. Immunofluorescent microscopic analysis and THGP mRNA identification have demonstrated that biosynthesis of the glycoprotein occurs exclusively in cells of the thick ascending Henle loop (TAL) [5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

N-Glycans carried by Tamm-Horsfall glycoprotein have a crucial role in the defense against urinary tract diseases

2005

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Tamm-Horsfall glycoprotein (THGP), produced exclusively by renal cells from the thick ascending limb of Henle's loop, is attached by a glycosyl-phosphatidylinositol (GPI)-anchor to the luminal face of the cells. Urinary excretion of THGP (50-100 mg/day) occurs upon proteolytic cleavage of the large ectodomain of the GPI-anchored form. N-Glycans, consisting of a large repertoire of sialylated polyantennary chains and high-mannose structures, account for approximately 30% of the weight of human urinary THGP. We describe: (i) the involvement of urinary THGP high-mannose glycans in defense against infections of the urinary tract, caused by type-1 fimbriated Escherichia coli, which recognize high-mannose structures, (ii) the role of GalNAcbeta1-4(NeuAcalpha2-3)Galbeta1-4GlcNAcbeta1-3Gal (Sd(a) determinant) carried by human THGP in protecting the distal nephron from colonization of type-S fimbriated E. coli which recognise NeuAcalpha2-3Gal, (iii) the inhibitory effect of sialylated THGP on crystal aggregation of calcium oxalate and calcium phosphate, thus preventing nephrolithiasis. Finally, we outline the importance of N-glycans in promoting the polymerization of THGP, a process resulting in the formation of homopolymers with an M(r) of several million in urine. Since THGP defense against diseases of the urinary tract mainly consists in binding damaging agents, its ability to behave as a multivalent ligand significantly enhances this protective role.

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“…However, a new ELISA kit became available in 2009 from MD Biosciences GmbH (Zürich, Switzerland). Besides ELISA, radioimmunoassay [52,92,[104][105][106][107][108] , radial immunodiffusion [109,110] and electroimmunoassay [111,112] have also been used in the past. An elegant and highly quantitative immunomethod based on the Luminex platform has been described recently [14] .…”

Section: Biochemical Analysismentioning

confidence: 99%

Uromodulin Biology and Pathophysiology – An Update

Vyleťal

Bleyer

Kmoch

2010

Kidney Blood Press Res

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Uromodulin (UMOD) is a glycoprotein expressed on the luminal surface of the apical membrane of renal tubular epithelial cells forming the thick ascending limb of Henle. Here, UMOD forms filamentous structures probably ensuring water impermeability and the countercurrent gradient. The multidomain structure, cellular topology of UMOD and clinical consequences associated with UMOD dysfunction, however, suggest that it may be involved in other biological processes such as receptor-mediated endocytosis, mechanosensation of urinary flow, Wnt-signaling, cell cycle regulation and planar cell polarity. A specific, but as yet unidentified, protease(s) releases UMOD into the urine, where it probably contributes to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and modulates formation of supersaturated salts and their crystals. UMOD expression, biosynthesis and excretion are regulated in a complex manner, and dysregulation is found in a wide range of pathological conditions. It is strongly reduced or absent in cases with mutations in UMOD, renin, HNF1B and other genetic disorders causing autosomal dominant hyperuricemic nephropathy. In contrast, elevated UMOD excretion may be associated with, and thus predictive of, chronic kidney disease. UMOD analysis is therefore of importance in all conditions with renal involvement and may be useful in the proper classification of renal diseases.

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The Development of a Radioimmunoassay for the Measurement of Urinary Tammhorsfall Glycoprotein in the Presence of Sodium Dodecyl Sulphate

Cited by 48 publications

References 16 publications

The Development of a Radioimmunoassay Procedure for the Estimation of Tamm—Horsfall Glycoprotein in Human Serum

The Development of a Radioimmunoassay Procedure for the Estimation of Tamm—Horsfall Glycoprotein in Human Serum

N-Glycans carried by Tamm-Horsfall glycoprotein have a crucial role in the defense against urinary tract diseases

Uromodulin Biology and Pathophysiology – An Update

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