Distribution of immunoreactive Tamm-Horsfall protein in various species in the vertebrate classes

Howie, Alexander J.; Lote, Christopher J.; Cunningham, A. A.; G, Zaccone; Fasulo, Salvatore

doi:10.1007/bf00327980

Cited by 18 publications

(17 citation statements)

References 11 publications

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“…Since it has been shown that THP is present in the kidney as well as in the superficial layers of the epidermis [9], it has been suggested that this protein may be an important component of epithelia, which absorb sodium and chloride ions but are impermeable to water [11]. Additionally, THP might play a protective role against urinary tract infections [10].…”

Section: Discussionmentioning

confidence: 99%

Vitamin A excreted in the urine of canines is associated with a Tamm-Horsfall like protein

Schweigert¹,

Raila²,

Haebel

2002

Vet. Res.

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-Under physiological conditions canines transport vitamin A in blood plasma primarily as retinyl esters bound to lipoproteins and excrete substantial amounts of vitamin A as retinol and retinyl esters with urine. In the aqueous environment of urine, the hydrophobic vitamin A has to be associated with a protein. This vitamin A-protein complex was purified to homogeneity, prepared by preparative ultracentrifugation (density 1.21 g/mL), native polyacrylamide gel electrophoresis (PAGE) and size exclusion chromatography. The vitamin A-protein complex has a high molecular mass of > 5 000 kDa under native conditions. SDS PAGE under reduced conditions revealed a single band with a molecular mass of about 100 kDa for the protein moiety. Peptides obtained after limited proteolysis with trypsin from the 100 kDa protein were characterised by MALDI-TOF mass spectrometry and showed amino acid sequence homology to the human Tamm-Horsfall Protein (THP). This was further confirmed by a positive immunoreaction of the isolated protein with crossreacting human THP antibodies. The localisation of THP in dog kidneys was determined by using immunohistology. The reaction was strong along the entire thick ascending limb of the Henle loop and distal convoluted tubule. Our data point to the possibility that THP functions as a novel carrier for vitamin A in the urine of canines. l'environnement aqueux de l'urine, la vitamine A hydrophobe doit être associée à une protéine. Ce complexe protéine-vitamine A a été purifié et homogénéisé, préparé par ultracentrifugation (1,21 g/mL de densité), électrophorèse sur gel de polyacrylamide natif (PAGE) et chromatographie d'exclusion de taille. Le complexe protéine-vitamine A a une masse moléculaire élevée supérieure à 5 000 kDa dans les conditions natives. Le SDS PAGE effectué dans des conditions réduites a révélé une bande unique avec une masse moléculaire d'environ 100 kDa pour la partie protéique. Les peptides obtenus à partir de la protéine de 100 kDa, après protéolyse limitée avec de la trypsine, ont été caractérisés par spectrométrie de masse MALDI-TOF et ont montré une homologie de séquence en acides aminés avec la protéine Tamm-Horsfall (PTH) humaine. Ceci a été confirmé par une immuno-réaction positive entre la protéine isolée et les anticorps présentant une réaction croisée avec la PTH humaine. La localisation de la PTH dans le rein de chien a été déterminée par immunohistologie. La réaction a été forte tout le long de la section ascendante épaisse de l'anse de Henle, et du tubule contourné distal. Nos résultats suggèrent que la PTH fonctionne comme un nouveau transporteur pour la vitamine A dans l'urine des canidés.vitamine A / canidés / rein / urine / protéine Tamm-Horsfall

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Section: Discussionmentioning

confidence: 99%

Vitamin A excreted in the urine of canines is associated with a Tamm-Horsfall like protein

Schweigert¹,

Raila²,

Haebel

2002

Vet. Res.

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“…Wallace and Nairn [12] found THP present only in the kidneys of placental mammals but not in marsupial or monotreme mammals or in other vertebrate classes including fishes, birds, amphibians and reptiles. Howie et al [13,14] found THP in the kidneys of all mammals, in the kidney and skin of the vertebrate class Amphibia, and in the skin and gills of the vertebrate classes Chondricthyes and Osteichthyes. The differences between these studies are presumably due to differences in specificity and crossreactivity of the polyvalent sera used and the sensitivity of the histological techniques.…”

Section: Resultsmentioning

confidence: 99%

Phylogeny of Tamm-Horsfall Protein

Badgett¹,

Kumar²

1998

Urol Int

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The Tamm-Horsfall protein (THP, uromodulin) is urine’s most abundant protein. The phylogenetic distribution of the gene for THP was examined in all the major vertebrate classes. Genomic DNA was obtaind from each vertebrate class and hybridized with a rat THP cDNA probe in a DNA hybridization assay. In separate experiments, a polymerase chain reaction assay was used to amplify segments of the THP gene using primers from a consensus sequence for THP among multiple mammalian species. Both methods revealed that the THP gene was present in all the vertebrate classes. These data demonstrate the evolutionary conservation of the THP gene among vertebrates and suggest a role for this protein that is common to the kidney of all vertebrates.

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“…Additionally, THP may stimulate polymorphonuclear leukocytes in the course of an inflammatory response (Horton et al, 1990). Although THP distribution in humans is limited to the kidney, immunoreactive THP-related proteins have been detected at other mucosal surfaces of several vertebrates (Howie et al, 1993). These observations suggest that THP-like proteins could also be involved in the defence(s) against infectious agents at other mucosal sites, IP: 54.213.91.117…”

Section: Introductionmentioning

confidence: 90%

“…The physiological function of THP is still unknown, but several studies have shown that it may inhibit the urothelial adherence of uropathogenic E. coli (Kuriyama & Silverblatt, 1986 ;Leeker et al, 1997 ;Orskov et al, 1980 ;Pak et al, 2001). To investigate whether a similar mechanism may apply to respiratory pathogens, and since immunoreactive THP-related proteins have been detected in a number of different mucosal surfaces of various vertebrates (Howie et al, 1993), we investigated the anti-adherence properties of THP towards B. pertussis. We found that THP is able to inhibit the adherence of B. pertussis to both renal and pulmonary epithelial cells, suggesting that THP expresses a widespectrum anti-adherence activity.…”

Section: Discussionmentioning

confidence: 99%

Interaction of human Tamm–Horsfall glycoprotein with Bordetella pertussis toxin

Menozzi¹,

Debrie²,

Tissier³

et al. 2002

Microbiology

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Tamm-Horsfall glycoprotein (THP), which is synthesized by renal tubular cells, is the most abundant protein in normal human urine. Although its physiological function remains unclear, it has been proposed that THP may act as a defence factor against urinary tract infections by inhibiting the binding of S-and P-fimbriated Escherichia coli to renal epithelial cells. Because THPrelated proteins are also found in the superficial layers of the oral mucosa, the authors investigated the ability of THP to interfere with the cytoadherence of pathogenic bacteria that colonize mucosal surfaces other than those of the urogenital tract. In this report, it is shown that THP binds to virulent Bordetella pertussis and reduces its adherence to both renal and pulmonary epithelial cells. This cytoadherence inhibitory effect was not observed with a B. pertussis mutant lacking the pertussis toxin (PTX) operon, and was dependent on the direct interaction of THP with the S2 subunit within the PTX B oligomer. The authors also show that the glycosylation moiety of THP is crucial for its binding to PTX. The THP-PTX interaction was exploited to develop an affinity chromatography method that allows a one-step purification of active PTX. These observations suggest that besides its anti-adherence activity, THP may also trap toxins produced by pathogenic bacteria that colonize mucosal surfaces.

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Distribution of immunoreactive Tamm-Horsfall protein in various species in the vertebrate classes

Cited by 18 publications

References 11 publications

Vitamin A excreted in the urine of canines is associated with a Tamm-Horsfall like protein

Vitamin A excreted in the urine of canines is associated with a Tamm-Horsfall like protein

Phylogeny of Tamm-Horsfall Protein

Interaction of human Tamm–Horsfall glycoprotein with Bordetella pertussis toxin

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