UT-B Urea Transporter Localization in the Bovine Gastrointestinal Tract

Coyle, John; McDaid, Shari; Walpole, Caragh; Stewart, Gavin

doi:10.1007/s00232-015-9850-5

Cited by 13 publications

(21 citation statements)

References 28 publications

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“…Tissue samples were excised from dorsal, ventral, and cranial sacs of adult Holstein-Friesian cattle rumen obtained in a commercial slaughterhouse within 1 h of slaughter. This was part of our ongoing, long-term study into the transport mechanisms involved in the UNS process in cattle, which has already characterized UT-B urea transporters along the gastrointestinal tract (Coyle et al, 2016). Total RNA of the rumen papillae was extracted using a commercial kit according to manufacturer instructions (RNA-STAT 60, AMS Biotechnology, Milton, UK).…”

Section: Methodsmentioning

confidence: 99%

“…2 Taken from Røjen et al, 2011. 3 Taken from Coyle et al, 2016. and probed overnight at 4°C with 1 of 2 anti-AQP3 antibodies; 1:1,000 AQP3-HPA (HPA014924, Sigma; QLMIGCHLEQPPPSNEEENVKLAHVKHKEQI target sequence of the last 31 AA in the C-terminus of human AQP3) or 1:1,000 AQP3-SAB (SAB5200111, Sigma; undisclosed target sequence within C-terminus of rat AQP3). After the primary antibody, immunoblots were washed and probed with 1:5,000 horseradish peroxidase-linked anti-rabbit secondary antibody for 1 h at room temperature.…”

Section: Genementioning

confidence: 99%

“…After another wash, detection of protein was performed using the Western Lightning Plus ECL reagents (Perkin Elmer, Waltham, MA) and an image reader (LAS4000, Fujifilm, Tokyo, Japan). Paraformaldehyde-fixed, paraffin-embedded bovine rumen (Coyle et al, 2016) and kidney sections (AMS Biotechnology) were used for immunohistochemistry experiments. After paraffin removal and rehydration in a decreasing concentration series of ethanol (100 to 70%), sections were incubated in 0.3% hydrogen peroxide in methanol to block endogenous peroxidase.…”

Section: Genementioning

confidence: 99%

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Localization of aquaporin-3 proteins in the bovine rumen

Zhong

Farrell

Stewart

2020

Journal of Dairy Science

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Urea nitrogen salvaging is a crucial mechanism that ruminants have evolved to conserve nitrogen. Facilitative urea transporter-B proteins are known to be involved in urea transport across the rumen epithelium and thus efficiently facilitate the urea nitrogen salvaging process. Recently, functional studies have suggested that aquaglyceroporin transporters might also play a significant role in ruminal urea transport and aquaporin-3 (AQP3) protein has previously been detected in rumen tissue. In this current study, we investigated the specific localization of AQP3 transporters in the bovine rumen. First, end-point reverse-transcription PCR experiments confirmed strong AQP3 expression in both bovine rumen and kidney. Immunoblotting analysis using 2 separate anti-AQP3 antibodies detected AQP3 protein signals at 25, 32, and 42-45 kDa. Further immunolocalization studies showed AQP3 protein located in all the layers of rumen epithelium, especially in the stratum basale, and in the basolateral membranes of kidney collecting duct cells. These data confirm that AQP3 transporters are highly abundant within the bovine rumen and appear to be located throughout the ruminal epithelial layers. The physiological significance of the multiple AQP3 proteins detected and their location is not yet clear, hence further investigation is required to determine their exact contribution to ruminal urea transport.

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Section: Methodsmentioning

confidence: 99%

Section: Genementioning

confidence: 99%

Section: Genementioning

confidence: 99%

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Localization of aquaporin-3 proteins in the bovine rumen

Zhong

Farrell

Stewart

2020

Journal of Dairy Science

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“…UT-B2 mRNA transcripts can be detected in the rumen of sheep and cow [11] and its expression is regulated by gastric acidity and alkalinity, rumen ammonia concentration, and the type of food consumed in the digestive system of sheep and cow. For example, consumed solid food can increase UT-B expression in cows [4] and feeding with a large amount of nitrogen and non-fiber carbohydrates also upregulates UT-B expression in the rumen of sheep [43].…”

Section: Ut-b Proteinsmentioning

confidence: 99%

Physiological functions of urea transporter B

Liu

et al. 2019

Pflugers Arch - Eur J Physiol

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Urea transporters (UTs) are membrane proteins in the urea transporter protein A (UT-A) and urea transporter protein B (UT-B) families. UT-B is mainly expressed in endothelial cell membrane of the renal medulla and in other tissues, including the brain, heart, pancreas, colon, bladder, bone marrow, and cochlea. UT-B is responsible for the maintenance of urea concentration, male reproductive function, blood pressure, bone metabolism, and brain astrocyte and cardiac functions. Its deficiency and dysfunction contribute to the pathogenesis of many diseases. Actually, UT-B deficiency increases the sensitivity of bladder epithelial cells to apoptosis triggers in mice and UT-B-null mice develop II-III atrioventricular block and depression. The expression of UT-B in the rumen of cow and sheep may participate in digestive function. However, there is no systemic review to discuss the UT-B functions. Here, we update research approaches to understanding the functions of UT-B.

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“…UT-B is important for salvaging urea nitrogen in the bovine gastrointestinal tract, especially in the rumen (47). The serosal-to-mucosal flux of urea across the isolated ruminal epithelium is mediated by UT-B, as well as aquaporins 3, 7, and 10, in Holstein calves (48).…”

Section: Ut-bmentioning

confidence: 99%

Urea transport and clinical potential of urearetics

Klein

Sands

2016

Current Opinion in Nephrology and Hypertension

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Purpose of review Urea is transported by urea transporter proteins in kidney, erythrocytes, and other tissues. Mice in which different urea transporters have been knocked-out have urine concentrating defects, which has led to the development and testing of UT-A and UT-B inhibitors as urearetics. This review summarizes the knowledge gained during the past year on urea transporter regulation and investigations into the clinical potential of urearetics. Recent findings UT-A1 undergoes several post-translational modifications that increase its function by increasing UT-A1 accumulation in the apical plasma membrane. UT-A1 is phosphorylated by PKA, Epac, PKCα, and AMPK, all at different serine residues. UT-A1 is also regulated by 14-3-3, which contributes to UT-A1 removal from the membrane. UT-A1 is glycosylated with various glycan moieties in animal models of diabetes mellitus. Transgenic expression of UT-A1 into UT-A1/UT-A3 knock-out mice restores urine concentrating ability. UT-B is present in descending vasa recta and urinary bladder, and is linked to bladder cancer. Inhibitors of UT-A and UT-B have been developed that result in diuresis with fewer abnormalities in serum electrolytes than conventional diuretics. Summary Urea transporters play critical roles in the urine concentrating mechanism. Urea transport inhibitors are a promising new class of diuretic agents.

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UT-B Urea Transporter Localization in the Bovine Gastrointestinal Tract

Cited by 13 publications

References 28 publications

Localization of aquaporin-3 proteins in the bovine rumen

Localization of aquaporin-3 proteins in the bovine rumen

Physiological functions of urea transporter B

Urea transport and clinical potential of urearetics

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