ArticleAmerican journal of physiology. Renal physiology2012
Glycoforms of UT-A3 urea transporter with poly-N-acetyllactosamine glycosylation have enhanced transport activity.
Article in American journal of physiology. Renal physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- Identification of a Novel UT-B Urea Transporter in Human Urothelial Cancer.Frontiers in physiology · 2017Article
- Modulation of kidney urea transporter UT-A3 activity by alpha2,6-sialylation.Pflugers Archiv : European journal of physiology · 2016Article
- Glycosylation of solute carriers: mechanisms and functional consequences.Pflugers Archiv : European journal of physiology · 2016Review
- New advances in urea transporter UT-A1 membrane trafficking.International journal of molecular sciences · 2013Review
- Molecular mechanisms of urea transport in health and disease.Pflugers Archiv : European journal of physiology · 2012Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Urea transporters UT-A1 and UT-A3 are both expressed in the kidney inner medulla. However, the function of UT-A3 remains unclear. Here, we found that UT-A3, which comprises only the NH(2)-terminal half of UT-A1, has a higher urea transport activity than UT-A1 in the oocyte and that this difference was associated with differences in N-glycosylation. Heterologously expressed UT-A3 is fully glycosylated with two glycoforms of 65 and 45 kDa. By contrast, UT-A1 expressed in HEK293 cells and oocytes exhibits only a 97-kDa glycosylation form. We further found that N-glycans of UT-A3 contain a large amount of poly-N-acetyllactosamine. This highly glycosylated UT-A3 is more stable and is enriched in lipid raft domains on the cell membrane. Kifunensine, an inhibitor of α-mannosidase that inhibits N-glycan processing beyond high-mannose-type N-glycans, significantly reduced UT-A3 urea transport activity. We then examined the native UT-A1 and UT-A3 glycosylation states from kidney inner medulla and found the ratio of 65 to 45 kDa in UT-A3 is higher than that of 117 to 97 kDa in UT-A1. The highly stable expression of highly glycosylated UT-A3 on the cell membrane in kidney inner medulla suggests that UT-A3 may have an important function in urea reabsorption.
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