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Article ; Online: Purinergic signaling is enhanced in the absence of UT-A1 and UT-A3.

Himmel, Nathaniel J / Rogers, Richard T / Redd, Sara K / Wang, Yirong / Blount, Mitsi A

2021 Volume 9, Issue 1, Page(s) e14636

Abstract: ATP is an important paracrine regulator of renal tubular water and urea transport. The activity of ... ...

Abstract	ATP is an important paracrine regulator of renal tubular water and urea transport. The activity of P2Y
MeSH term(s)	Animals ; Disease Models, Animal ; Kidney Medulla/metabolism ; Kidney Tubules, Collecting/metabolism ; Male ; Membrane Transport Proteins/deficiency ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Osmolar Concentration ; Receptors, Purinergic P2Y2/metabolism ; Signal Transduction ; Urea/metabolism ; Urea Transporters
Chemical Substances	Membrane Transport Proteins ; Receptors, Purinergic P2Y2 ; Urea (8W8T17847W)
Language	English
Publishing date	2021-01-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2724325-4
ISSN	2051-817X ; 2051-817X
ISSN (online)	2051-817X
ISSN	2051-817X
DOI	10.14814/phy2.14636
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Article ; Online: A timely characterization of vasopressin-sensitive adenylyl cyclase isoforms in the mouse inner medullary collecting duct.

Blount, Mitsi A

American journal of physiology. Renal physiology

2009 Volume 298, Issue 4, Page(s) F857–8

MeSH term(s)	Adenylyl Cyclases/chemistry ; Adenylyl Cyclases/genetics ; Adenylyl Cyclases/metabolism ; Animals ; Antidiuretic Agents/pharmacology ; Gene Expression Regulation, Enzymologic ; Isoenzymes/chemistry ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Kidney Tubules, Collecting/drug effects ; Kidney Tubules, Collecting/enzymology ; Kidney Tubules, Collecting/metabolism ; Mice ; Vasopressins/pharmacology
Chemical Substances	Antidiuretic Agents ; Isoenzymes ; Vasopressins (11000-17-2) ; Adenylyl Cyclases (EC 4.6.1.1)
Language	English
Publishing date	2009-12-23
Publishing country	United States
Document type	Comment ; Editorial ; Research Support, N.I.H., Extramural
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.00725.2009
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Article ; Online: Metformin, an AMPK activator, stimulates the phosphorylation of aquaporin 2 and urea transporter A1 in inner medullary collecting ducts.

Klein, Janet D / Wang, Yanhua / Blount, Mitsi A / Molina, Patrick A / LaRocque, Lauren M / Ruiz, Joseph A / Sands, Jeff M

American journal of physiology. Renal physiology

2016 Volume 310, Issue 10, Page(s) F1008–12

Abstract: Nephrogenic diabetes insipidus (NDI) is characterized by production of very large quantities of dilute urine due to an inability of the kidney to respond to vasopressin. Congenital NDI results from mutations in the type 2 vasopressin receptor (V2R) in ∼ ... ...

Abstract	Nephrogenic diabetes insipidus (NDI) is characterized by production of very large quantities of dilute urine due to an inability of the kidney to respond to vasopressin. Congenital NDI results from mutations in the type 2 vasopressin receptor (V2R) in ∼90% of families. These patients do not have mutations in aquaporin-2 (AQP2) or urea transporter UT-A1 (UT-A1). We tested adenosine monophosphate kinase (AMPK) since it is known to phosphorylate another vasopressin-sensitive transporter, NKCC2 (Na-K-2Cl cotransporter). We found AMPK expressed in rat inner medulla (IM). AMPK directly phosphorylated AQP2 and UT-A1 in vitro. Metformin, an AMPK activator, increased phosphorylation of both AQP2 and UT-A1 in rat inner medullary collecting ducts (IMCDs). Metformin increased the apical plasma membrane accumulation of AQP2, but not UT-A1, in rat IM. Metformin increased both osmotic water permeability and urea permeability in perfused rat terminal IMCDs. These findings suggest that metformin increases osmotic water permeability by increasing AQP2 accumulation in the apical plasma membrane but increases urea permeability by activating UT-A1 already present in the membrane. Lastly, metformin increased urine osmolality in mice lacking a V2R, a mouse model of congenital NDI. We conclude that AMPK activation by metformin mimics many of the mechanisms by which vasopressin increases urine-concentrating ability. These findings suggest that metformin may be a novel therapeutic option for congenital NDI due to V2R mutations.
MeSH term(s)	AMP-Activated Protein Kinases/drug effects ; AMP-Activated Protein Kinases/metabolism ; Animals ; Aquaporin 2/metabolism ; Diabetes Insipidus, Nephrogenic/drug therapy ; Diabetes Insipidus, Nephrogenic/urine ; Drug Evaluation, Preclinical ; Hypoglycemic Agents/pharmacology ; Hypoglycemic Agents/therapeutic use ; Membrane Transport Proteins/metabolism ; Metformin/pharmacology ; Metformin/therapeutic use ; Phosphorylation/drug effects ; Rats, Sprague-Dawley ; Urea/metabolism ; Water/metabolism ; Urea Transporters
Chemical Substances	Aqp2 protein, rat ; Aquaporin 2 ; Hypoglycemic Agents ; Membrane Transport Proteins ; Water (059QF0KO0R) ; Urea (8W8T17847W) ; Metformin (9100L32L2N) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2016-03-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.00102.2016
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Article ; Online: Novel activators of aquaporin 2 membrane expression for the treatment of nephrogenic diabetes insipidus: less is more. Focus on "High-throughput chemical screening identifies AG-490 as a stimulator of aquaporin 2 membrane expression and urine concentration".

Sands, Jeff M / Blount, Mitsi A

American journal of physiology. Cell physiology

2014 Volume 307, Issue 7, Page(s) C595–6

MeSH term(s)	Animals ; Aquaporin 2/drug effects ; Cell Membrane/drug effects ; High-Throughput Screening Assays ; Kidney/drug effects ; Kidney Concentrating Ability/drug effects ; Tyrphostins/pharmacology ; Urological Agents/pharmacology
Chemical Substances	Aqp2 protein, rat ; Aquaporin 2 ; Tyrphostins ; Urological Agents ; alpha-cyano-(3,4-dihydroxy)-N-benzylcinnamide
Language	English
Publishing date	2014-06-18
Publishing country	United States
Document type	Editorial ; Research Support, N.I.H., Extramural ; Comment
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00184.2014
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Article: Genes and proteins of urea transporters.

Sands, Jeff M / Blount, Mitsi A

Sub-cellular biochemistry

2014 Volume 73, Page(s) 45–63

Abstract: A urea transporter protein in the kidney was first proposed in 1987. The first urea transporter cDNA was cloned in 1993. The SLC14a urea transporter family contains two major subgroups: SLC14a1, the UT-B urea transporter originally isolated from ... ...

Abstract	A urea transporter protein in the kidney was first proposed in 1987. The first urea transporter cDNA was cloned in 1993. The SLC14a urea transporter family contains two major subgroups: SLC14a1, the UT-B urea transporter originally isolated from erythrocytes; and SLC14a2, the UT-A group originally isolated from kidney inner medulla. Slc14a1, the human UT-B gene, arises from a single locus located on chromosome 18q12.1-q21.1, which is located close to Slc14a2. Slc14a1 includes 11 exons, with the coding region extending from exon 4 to exon 11, and is approximately 30 kb in length. The Slc14a2 gene is a very large gene with 24 exons, is approximately 300 kb in length, and encodes 6 different isoforms. Slc14a2 contains two promoter elements: promoter I is located in the typical position, upstream of exon 1, and drives the transcription of UT-A1, UT-A1b, UT-A3, UT-A3b, and UT-A4; while promoter II is located within intron 12 and drives the transcription of UT-A2 and UT-A2b. UT-A1 and UT-A3 are located in the inner medullary collecting duct, UT-A2 in the thin descending limb and liver, UT-A5 in testis, UT-A6 in colon, UT-B1 primarily in descending vasa recta and erythrocytes, and UT-B2 in rumen.
MeSH term(s)	Biological Transport ; Erythrocytes/metabolism ; Exons/genetics ; Gene Expression Profiling ; Humans ; Kidney Medulla/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Promoter Regions, Genetic/genetics ; Protein Isoforms ; Urea/metabolism ; Urea Transporters
Chemical Substances	Membrane Transport Proteins ; Protein Isoforms ; Urea (8W8T17847W)
Language	English
Publishing date	2014-10-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ISSN	0306-0225 ; 0096-8757
ISSN	0306-0225 ; 0096-8757
DOI	10.1007/978-94-017-9343-8_4
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Article ; Online: Transgenic Restoration of Urea Transporter A1 Confers Maximal Urinary Concentration in the Absence of Urea Transporter A3.

Klein, Janet D / Wang, Yanhua / Mistry, Abinash / LaRocque, Lauren M / Molina, Patrick A / Rogers, Richard T / Blount, Mitsi A / Sands, Jeff M

Journal of the American Society of Nephrology : JASN

2015 Volume 27, Issue 5, Page(s) 1448–1455

Abstract: Urea has a critical role in urinary concentration. Mice lacking the inner medullary collecting duct (IMCD) urea transporter A1 (UT-A1) and urea transporter A3 (UT-A3) have very low levels of urea permeability and are unable to concentrate urine. To ... ...

Abstract	Urea has a critical role in urinary concentration. Mice lacking the inner medullary collecting duct (IMCD) urea transporter A1 (UT-A1) and urea transporter A3 (UT-A3) have very low levels of urea permeability and are unable to concentrate urine. To investigate the role of UT-A1 in the concentration of urine, we transgenically expressed UT-A1 in knockout mice lacking UT-A1 and UT-A3 using a construct with a UT-A1 gene that cannot be spliced to produce UT-A3. This construct was inserted behind the original UT-A promoter to yield a mouse expressing only UT-A1 (UT-A1(+/+)/UT-A3(-/-)). Western blot analysis demonstrated UT-A1 in the inner medulla of UT-A1(+/+)/UT-A3(-/-) and wild-type mice, but not in UT-A1/UT-A3 knockout mice, and an absence of UT-A3 in UT-A1(+/+)/UT-A3(-/-) and UT-A1/UT-A3 knockout mice. Immunohistochemistry in UT-A1(+/+)/UT-A3(-/-) mice also showed negative UT-A3 staining in kidney and other tissues and positive UT-A1 staining only in the IMCD. Urea permeability in isolated perfused IMCDs showed basal permeability in the UT-A1(+/+)/UT-A3(-/-) mice was similar to levels in wild-type mice, but vasopressin stimulation of urea permeability in wild-type mice was significantly greater (100% increase) than in UT-A1(+/+)/UT-A3(-/-) mice (8% increase). Notably, basal urine osmolalities in both wild-type and UT-A1(+/+)/UT-A3(-/-) mice increased upon overnight water restriction. We conclude that transgenic expression of UT-A1 restores basal urea permeability to the level in wild-type mice but does not restore vasopressin-stimulated levels of urea permeability. This information suggests that transgenic expression of UT-A1 alone in mice lacking UT-A1 and UT-A3 is sufficient to restore urine-concentrating ability.
MeSH term(s)	Animals ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/physiology ; Mice ; Mice, Knockout ; Urea/urine ; Urinary Tract Physiological Phenomena ; Urea Transporters
Chemical Substances	Membrane Transport Proteins ; Urea (8W8T17847W)
Language	English
Publishing date	2015-09-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1085942-1
ISSN	1533-3450 ; 1046-6673
ISSN (online)	1533-3450
ISSN	1046-6673
DOI	10.1681/ASN.2014121267
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Article ; Online: Chronic lithium treatment induces novel patterns of pendrin localization and expression.

Himmel, Nathaniel J / Wang, Yirong / Rodriguez, Daniel A / Sun, Michael A / Blount, Mitsi A

American journal of physiology. Renal physiology

2018 Volume 315, Issue 2, Page(s) F313–F322

Abstract: Prolonged lithium treatment is associated with various renal side effects and is known to induce inner medullary collecting duct (IMCD) remodeling. In animals treated with lithium, the fraction of intercalated cells (ICs), which are responsible for acid- ... ...

Abstract	Prolonged lithium treatment is associated with various renal side effects and is known to induce inner medullary collecting duct (IMCD) remodeling. In animals treated with lithium, the fraction of intercalated cells (ICs), which are responsible for acid-base homeostasis, increases compared with renal principal cells (PCs). To investigate the intricacies of lithium-induced IMCD remodeling, male Sprague-Dawley rats were fed a lithium-enriched diet for 0,1, 2, 3, 6, 9, or 12 wk. Urine osmolality was decreased at 1 wk, and from 2 to 12 wk, animals were severely polyuric. After 6 wk of lithium treatment, approximately one-quarter of the cells in the initial IMCD expressed vacuolar H
MeSH term(s)	Ammonium Compounds/urine ; Animals ; Aquaporin 4/metabolism ; Cell Plasticity/drug effects ; Cell Proliferation/drug effects ; Chloride-Bicarbonate Antiporters/genetics ; Chloride-Bicarbonate Antiporters/metabolism ; Drug Administration Schedule ; Gene Expression Regulation ; Hydrogen-Ion Concentration ; Kidney Tubules, Collecting/drug effects ; Kidney Tubules, Collecting/metabolism ; Kidney Tubules, Collecting/pathology ; Lithium Carbonate/toxicity ; Male ; Osmolar Concentration ; Phenotype ; Polyuria/chemically induced ; Polyuria/pathology ; Polyuria/urine ; Rats, Sprague-Dawley ; Signal Transduction ; Sulfate Transporters/genetics ; Sulfate Transporters/metabolism ; Time Factors ; Vacuolar Proton-Translocating ATPases/metabolism
Chemical Substances	Ammonium Compounds ; Aqp4 protein, rat ; Aquaporin 4 ; Chloride-Bicarbonate Antiporters ; Slc26A4 protein, rat ; Sulfate Transporters ; Lithium Carbonate (2BMD2GNA4V) ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-)
Language	English
Publishing date	2018-04-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.00065.2018
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Article ; Online: Urea transport in the kidney.

Klein, Janet D / Blount, Mitsi A / Sands, Jeff M

Comprehensive Physiology

2013 Volume 1, Issue 2, Page(s) 699–729

Abstract: Urea transport proteins were initially proposed to exist in the kidney in the late 1980s when studies of urea permeability revealed values in excess of those predicted by simple lipid-phase diffusion and paracellular transport. Less than a decade later, ... ...

Abstract	Urea transport proteins were initially proposed to exist in the kidney in the late 1980s when studies of urea permeability revealed values in excess of those predicted by simple lipid-phase diffusion and paracellular transport. Less than a decade later, the first urea transporter was cloned. Currently, the SLC14A family of urea transporters contains two major subgroups: SLC14A1, the UT-B urea transporter originally isolated from erythrocytes; and SLC14A2, the UT-A group with six distinct isoforms described to date. In the kidney, UT-A1 and UT-A3 are found in the inner medullary collecting duct; UT-A2 is located in the thin descending limb, and UT-B is located primarily in the descending vasa recta; all are glycoproteins. These transporters are crucial to the kidney's ability to concentrate urine. UT-A1 and UT-A3 are acutely regulated by vasopressin. UT-A1 has also been shown to be regulated by hypertonicity, angiotensin II, and oxytocin. Acute regulation of these transporters is through phosphorylation. Both UT-A1 and UT-A3 rapidly accumulate in the plasma membrane in response to stimulation by vasopressin or hypertonicity. Long-term regulation involves altering protein abundance in response to changes in hydration status, low protein diets, adrenal steroids, sustained diuresis, or antidiuresis. Urea transporters have been studied using animal models of disease including diabetes mellitus, lithium intoxication, hypertension, and nephrotoxic drug responses. Exciting new animal models are being developed to study these transporters and search for active urea transporters. Here we introduce urea and describe the current knowledge of the urea transporter proteins, their regulation, and their role in the kidney.
MeSH term(s)	Animals ; Biological Transport ; Disease Models, Animal ; Humans ; Kidney/metabolism ; Membrane Transport Proteins/metabolism ; Urea/metabolism ; Urea Transporters
Chemical Substances	Membrane Transport Proteins ; Urea (8W8T17847W)
Language	English
Publishing date	2013-06-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ISSN	2040-4603
ISSN (online)	2040-4603
DOI	10.1002/cphy.c100030
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Article ; Online: Chronic use of chloroquine disrupts the urine concentration mechanism by lowering cAMP levels in the inner medulla.

von Bergen, Tobias N / Blount, Mitsi A

American journal of physiology. Renal physiology

2012 Volume 303, Issue 6, Page(s) F900–5

Abstract: Chloroquine, a widely used anti-malaria drug, has gained popularity for the treatment of rheumatoid arthritis, systemic lupus erythematosus (SLE), and human immunodeficiency virus (HIV). Unfortunately, chloroquine may also negatively impact renal ... ...

Abstract	Chloroquine, a widely used anti-malaria drug, has gained popularity for the treatment of rheumatoid arthritis, systemic lupus erythematosus (SLE), and human immunodeficiency virus (HIV). Unfortunately, chloroquine may also negatively impact renal function for patients whose fluid and electrolyte homeostasis is already compromised by diseases. Chronic administration of chloroquine also results in polyuria, which may be explained by suppression of the antidiuretic response of vasopressin. Several of the transporters responsible for concentrating urine are vasopressin-sensitive including the urea transporters UT-A1 and UT-A3, the water channel aquaporin-2 (AQP2), and the Na(+)-K(+)-2Cl(-) cotransporter (NKCC2). To examine the effect of chloroquine on these transporters, Sprague-Dawley rats received daily subcutaneous injections of 80 mg·kg(-1)·day(-1) of chloroquine for 4 days. Twenty-four hour urine output was twofold higher, and urine osmolality was decreased by twofold in chloroquine-treated rats compared with controls. Urine analysis of treated rats detected the presence chloroquine as well as decreased urine urea and cAMP levels compared with control rats. Western blot analysis showed a downregulation of AQP2 and NKCC2 transporters; however, UT-A1 and UT-A3 abundances were unaffected by chloroquine treatment. Immunohistochemistry showed a marked reduction of UT-A1 and AQP2 in the apical membrane in inner medullary collecting ducts of chloroquine-treated rats. In conclusion, chloroquine-induced polyuria likely occurs as a result of lowered cAMP production. These findings suggest that chronic chloroquine treatment would exacerbate the already compromised fluid homeostasis observed in diseases like chronic kidney disease.
MeSH term(s)	Animals ; Aquaporin 2/metabolism ; Chloroquine/adverse effects ; Chloroquine/urine ; Cyclic AMP/analysis ; Cyclic AMP/metabolism ; Down-Regulation ; Kidney/drug effects ; Kidney/pathology ; Kidney Concentrating Ability/drug effects ; Male ; Membrane Transport Proteins/metabolism ; Osmolar Concentration ; Polyuria/chemically induced ; Rats ; Sodium-Potassium-Chloride Symporters/metabolism ; Solute Carrier Family 12, Member 1 ; Urea/urine ; Urea Transporters
Chemical Substances	Aqp2 protein, rat ; Aquaporin 2 ; Membrane Transport Proteins ; SLC12A1 protein, human ; Slc12a1 protein, rat ; Sodium-Potassium-Chloride Symporters ; Solute Carrier Family 12, Member 1 ; Chloroquine (886U3H6UFF) ; Urea (8W8T17847W) ; Cyclic AMP (E0399OZS9N)
Language	English
Publishing date	2012-07-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.00547.2011
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Article ; Online: Molecular mechanisms of urea transport in health and disease.

Klein, Janet D / Blount, Mitsi A / Sands, Jeff M

Pflugers Archiv : European journal of physiology

2012 Volume 464, Issue 6, Page(s) 561–572

Abstract: In the late 1980s, urea permeability measurements produced values that could not be explained by paracellular transport or lipid phase diffusion. The existence of urea transport proteins were thus proposed and less than a decade later, the first urea ... ...

Abstract	In the late 1980s, urea permeability measurements produced values that could not be explained by paracellular transport or lipid phase diffusion. The existence of urea transport proteins were thus proposed and less than a decade later, the first urea transporter was cloned. The family of urea transporters has two major subgroups, designated SLC14A1 (or UT-B) and Slc14A2 (or UT-A). UT-B and UT-A gene products are glycoproteins located in various extra-renal tissues however, a majority of the resulting isoforms are found in the kidney. The UT-B (Slc14A1) urea transporter was originally isolated from erythrocytes and two isoforms have been reported. In kidney, UT-B is located primarily in the descending vasa recta. The UT-A (Slc14A2) urea transporter yields six distinct isoforms, of which three are found chiefly in the kidney medulla. UT-A1 and UT-A3 are found in the inner medullary collecting duct (IMCD), while UT-A2 is located in the thin descending limb. These transporters are crucial to the kidney's ability to concentrate urine. The regulation of urea transporter activity in the IMCD involves acute modification through phosphorylation and subsequent movement to the plasma membrane. UT-A1 and UT-A3 accumulate in the plasma membrane in response to stimulation by vasopressin or hypertonicity. Long-term regulation of the urea transporters in the IMCD involves altering protein abundance in response to changes in hydration status, low protein diets, or adrenal steroids. Urea transporters have been studied using animal models of disease including diabetes mellitus, lithium intoxication, hypertension, and nephrotoxic drug responses. Exciting new genetically engineered mouse models are being developed to study these transporters.
MeSH term(s)	Animals ; Biological Transport ; Humans ; Kidney Tubules, Collecting/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Urea/metabolism ; Urea Transporters
Chemical Substances	Membrane Transport Proteins ; Urea (8W8T17847W)
Language	English
Publishing date	2012-09-25
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	6380-0
ISSN	1432-2013 ; 0031-6768
ISSN (online)	1432-2013
ISSN	0031-6768
DOI	10.1007/s00424-012-1157-0
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