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Article: Uroguanylin: physiological role as a natriuretic hormone.

Forte, Leonard Ralph

Journal of the American Society of Nephrology : JASN

2005 Volume 16, Issue 2, Page(s) 291–292

MeSH term(s)	Animals ; Biomarkers/analysis ; Biomarkers/metabolism ; Humans ; Natriuretic Agents/metabolism ; Natriuretic Peptides ; Nephrotic Syndrome/metabolism ; Nephrotic Syndrome/physiopathology ; Peptides/analysis ; Peptides/metabolism ; Prognosis ; Sensitivity and Specificity ; Severity of Illness Index
Chemical Substances	Biomarkers ; Natriuretic Agents ; Natriuretic Peptides ; Peptides ; uroguanylin (152175-68-3)
Language	English
Publishing date	2005-02
Publishing country	United States
Document type	Comment ; Comparative Study ; Editorial
ZDB-ID	1085942-1
ISSN	1533-3450 ; 1046-6673
ISSN (online)	1533-3450
ISSN	1046-6673
DOI	10.1681/ASN.2004121061
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Article ; Online: Pendrin, a novel transcriptional target of the uroguanylin system.

Rozenfeld, Julia / Tal, Osnat / Kladnitsky, Orly / Adler, Lior / Efrati, Edna / Carrithers, Stephen L / Alper, Seth L / Zelikovic, Israel

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology

2013 Volume 32, Issue 7, Page(s) 221–237

Abstract: ... action at a defined heat shock element (HSE) site. Recent studies have unraveled novel roles for guanylin ... Guanylin (GN) and uroguanylin (UGN) are low-molecular-weight peptide hormones produced mainly ... water in both intestine and kidney. Thought to act as "intestinal natriuretic factors", GN and UGN ...

Abstract	Guanylin (GN) and uroguanylin (UGN) are low-molecular-weight peptide hormones produced mainly in the intestinal mucosa in response to oral salt load. GN and UGN (guanylin peptides) induce secretion of electrolytes and water in both intestine and kidney. Thought to act as "intestinal natriuretic factors", GN and UGN modulate renal salt secretion by both endocrine mechanisms (linking the digestive system and kidney) and paracrine/autocrine (intrarenal) mechanisms. The cellular function of GN and UGN in intestine and proximal tubule is mediated by guanylyl cyclase C (GC-C)-, cGMP-, and G protein-dependent pathways, whereas, in principal cells of the cortical collecting duct (CCD), these peptide hormones act via GC-C-independent signaling through phospholipase A2 (PLA2). The Cl(-)/HCO(-)3 exchanger pendrin (SLC26A4), encoded by the PDS gene, is expressed in non-α intercalated cells of the CCD. Pendrin is essential for CCD bicarbonate secretion and is also involved in NaCl balance and blood pressure regulation. Our recent studies have provided evidence that pendrin-mediated anion exchange in the CCD is regulated at the transcriptional level by UGN. UGN exerts an inhibitory effect on the pendrin gene promoter likely via heat shock factor 1 (HSF1) action at a defined heat shock element (HSE) site. Recent studies have unraveled novel roles for guanylin peptides in several organ systems including involvement in appetite regulation, olfactory function, cell proliferation and differentiation, inflammation, and reproductive function. Both the guanylin system and pendrin have also been implicated in airway function. Future molecular research into the receptors and signal transduction pathways involved in the action of guanylin peptides and the pendrin anion exchanger in the kidney and other organs, and into the links between them, may facilitate discovery of new therapies for hypertension, heart failure, hepatic failure and other fluid retention syndromes, as well as for diverse diseases such as obesity, asthma, and cancer.
MeSH term(s)	Cyclic GMP/metabolism ; Gastrointestinal Hormones/metabolism ; Guanylate Cyclase/metabolism ; Humans ; Intestinal Mucosa/metabolism ; Kidney Tubules, Collecting/metabolism ; Membrane Transport Proteins/biosynthesis ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Natriuretic Peptides/metabolism ; Signal Transduction ; Sulfate Transporters ; Transcription, Genetic
Chemical Substances	Gastrointestinal Hormones ; Membrane Transport Proteins ; Natriuretic Peptides ; SLC26A4 protein, human ; Sulfate Transporters ; guanylin (140653-38-9) ; uroguanylin (152175-68-3) ; Guanylate Cyclase (EC 4.6.1.2) ; Cyclic GMP (H2D2X058MU)
Language	English
Publishing date	2013-12-18
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	1067572-3
ISSN	1421-9778 ; 1015-8987
ISSN (online)	1421-9778
ISSN	1015-8987
DOI	10.1159/000356641
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Article ; Online: A uroguanylin-GUCY2C endocrine axis regulates feeding in mice.

Valentino, Michael A / Lin, Jieru E / Snook, Adam E / Li, Peng / Kim, Gilbert W / Marszalowicz, Glen / Magee, Michael S / Hyslop, Terry / Schulz, Stephanie / Waldman, Scott A

The Journal of clinical investigation

2011 Volume 121, Issue 9, Page(s) 3578–3588

Abstract: ... of centrally regulated feeding behavior in invertebrates, the role of this primordial signaling mechanism ... uroguanylin, which regulate epithelial cell dynamics along the crypt-villus axis. Here, we show that silencing ... This defined an appetite-regulating uroguanylin-GUCY2C endocrine axis, which we confirmed by showing ...

Abstract	Intestinal enteroendocrine cells are critical to central regulation of caloric consumption, since they activate hypothalamic circuits that decrease appetite and thereby restrict meal size by secreting hormones in response to nutrients in the gut. Although guanylyl cyclase and downstream cGMP are essential regulators of centrally regulated feeding behavior in invertebrates, the role of this primordial signaling mechanism in mammalian appetite regulation has eluded definition. In intestinal epithelial cells, guanylyl cyclase 2C (GUCY2C) is a transmembrane receptor that makes cGMP in response to the paracrine hormones guanylin and uroguanylin, which regulate epithelial cell dynamics along the crypt-villus axis. Here, we show that silencing of GUCY2C in mice disrupts satiation, resulting in hyperphagia and subsequent obesity and metabolic syndrome. This defined an appetite-regulating uroguanylin-GUCY2C endocrine axis, which we confirmed by showing that nutrient intake induces intestinal prouroguanylin secretion into the circulation. The prohormone signal is selectively decoded in the hypothalamus by proteolytic liberation of uroguanylin, inducing GUCY2C signaling and consequent activation of downstream anorexigenic pathways. Thus, evolutionary diversification of primitive guanylyl cyclase signaling pathways allows GUCY2C to coordinate endocrine regulation of central food acquisition pathways with paracrine control of intestinal homeostasis. Moreover, the uroguanylin-GUCY2C endocrine axis may provide a therapeutic target to control appetite, obesity, and metabolic syndrome.
MeSH term(s)	Animals ; Behavior, Animal/physiology ; Body Composition ; Body Weight ; Cyclic GMP/metabolism ; Eating ; Endocrine System/cytology ; Endocrine System/metabolism ; Epithelial Cells/cytology ; Epithelial Cells/immunology ; Feeding Behavior/physiology ; Female ; Hypothalamus/metabolism ; Insulin/blood ; Intestinal Mucosa/cytology ; Intestinal Mucosa/immunology ; Leptin/blood ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Natriuretic Peptides/genetics ; Natriuretic Peptides/metabolism ; Protein Precursors/genetics ; Protein Precursors/metabolism ; Receptors, Enterotoxin ; Receptors, Guanylate Cyclase-Coupled/genetics ; Receptors, Guanylate Cyclase-Coupled/metabolism ; Receptors, Peptide/genetics ; Receptors, Peptide/metabolism ; Satiation ; Second Messenger Systems/physiology
Chemical Substances	Insulin ; Leptin ; Natriuretic Peptides ; Protein Precursors ; Receptors, Peptide ; uroguanylin (152175-68-3) ; Gucy2c protein, mouse (EC 4.6.1.2) ; Receptors, Enterotoxin (EC 4.6.1.2) ; Receptors, Guanylate Cyclase-Coupled (EC 4.6.1.2) ; Cyclic GMP (H2D2X058MU)
Language	English
Publishing date	2011-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3067-3
ISSN	1558-8238 ; 0021-9738
ISSN (online)	1558-8238
ISSN	0021-9738
DOI	10.1172/JCI57925
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Article: Calorie-induced ER stress suppresses uroguanylin satiety signaling in diet-induced obesity.

Kim, G W / Lin, J E / Snook, A E / Aing, A S / Merlino, D J / Li, P / Waldman, S A

Nutrition & diabetes

2016 Volume 6, Page(s) e211

Abstract: ... calorie diets for 14 weeks. The role of endoplasmic reticulum (ER) stress in suppressing uroguanylin ... explored by dietary manipulation. The role of uroguanylin in mechanisms underlying obesity was examined ... regulating feeding, energy homeostasis, body mass and metabolism. Here, we explore a role for this axis ...

Abstract	Background/objectives: The uroguanylin-GUCY2C gut-brain axis has emerged as one component regulating feeding, energy homeostasis, body mass and metabolism. Here, we explore a role for this axis in mechanisms underlying diet-induced obesity (DIO). Subjects/methods: Intestinal uroguanylin expression and secretion, and hypothalamic GUCY2C expression and anorexigenic signaling, were quantified in mice on high-calorie diets for 14 weeks. The role of endoplasmic reticulum (ER) stress in suppressing uroguanylin in DIO was explored using tunicamycin, an inducer of ER stress, and tauroursodeoxycholic acid (TUDCA), a chemical chaperone that inhibits ER stress. The impact of consumed calories on uroguanylin expression was explored by dietary manipulation. The role of uroguanylin in mechanisms underlying obesity was examined using Camk2a-Cre-ER(T2)-Rosa-STOP(loxP/loxP)-Guca2b mice in which tamoxifen induces transgenic hormone expression in brain. Results: DIO suppressed intestinal uroguanylin expression and eliminated its postprandial secretion into the circulation. DIO suppressed uroguanylin through ER stress, an effect mimicked by tunicamycin and blocked by TUDCA. Hormone suppression by DIO reflected consumed calories, rather than the pathophysiological milieu of obesity, as a diet high in calories from carbohydrates suppressed uroguanylin in lean mice, whereas calorie restriction restored uroguanylin in obese mice. However, hypothalamic GUCY2C, enriched in the arcuate nucleus, produced anorexigenic signals mediating satiety upon exogenous agonist administration, and DIO did not impair these responses. Uroguanylin replacement by transgenic expression in brain repaired the hormone insufficiency and reconstituted satiety responses opposing DIO and its associated comorbidities, including visceral adiposity, glucose intolerance and hepatic steatosis. Conclusions: These studies reveal a novel pathophysiological mechanism contributing to obesity in which calorie-induced suppression of intestinal uroguanylin impairs hypothalamic mechanisms regulating food consumption through loss of anorexigenic endocrine signaling. The correlative therapeutic paradigm suggests that, in the context of hormone insufficiency with preservation of receptor sensitivity, obesity may be prevented or treated by GUCY2C hormone replacement.
MeSH term(s)	Animals ; Arcuate Nucleus of Hypothalamus/metabolism ; Caloric Restriction ; Diet ; Endoplasmic Reticulum Stress/physiology ; Energy Intake ; Fatty Liver/therapy ; Gene Expression Regulation ; Gene Silencing ; Glucose Intolerance/therapy ; Hormone Replacement Therapy ; Intestinal Mucosa/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Obese ; Mice, Transgenic ; Natriuretic Peptides/blood ; Natriuretic Peptides/metabolism ; Obesity/physiopathology ; Obesity/therapy ; Postprandial Period ; Receptors, Enterotoxin ; Receptors, Guanylate Cyclase-Coupled/genetics ; Receptors, Guanylate Cyclase-Coupled/metabolism ; Receptors, Peptide/genetics ; Receptors, Peptide/metabolism ; Satiation ; Signal Transduction ; Taurochenodeoxycholic Acid/pharmacology ; Tunicamycin/pharmacology
Chemical Substances	Natriuretic Peptides ; Receptors, Peptide ; Tunicamycin (11089-65-9) ; uroguanylin (152175-68-3) ; Taurochenodeoxycholic Acid (516-35-8) ; ursodoxicoltaurine (60EUX8MN5X) ; Gucy2c protein, mouse (EC 4.6.1.2) ; Receptors, Enterotoxin (EC 4.6.1.2) ; Receptors, Guanylate Cyclase-Coupled (EC 4.6.1.2)
Language	English
Publishing date	2016-05-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2609314-5
ISSN	2044-4052
ISSN	2044-4052
DOI	10.1038/nutd.2016.18
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Article ; Online: Pendrin, a Novel Transcriptional Target of the Uroguanylin System

Rozenfeld, Julia / Tal, Osnat / Kladnitsky, Orly / Adler, Lior / Efrati, Edna / Carrithers, Stephen L. / Alper, Seth L. / Zelikovic, Israel

Cellular Physiology and Biochemistry - International Journal of Experimental Cellular Physiology, Biochemistry and Pharmacology

2013 Volume 32, Issue S1, Page(s) 221–237

Abstract	Guanylin (GN) and uroguanylin (UGN) are low-molecular-weight peptide hormones produced mainly in the intestinal mucosa in response to oral salt load. GN and UGN (guanylin peptides) induce secretion of electrolytes and water in both intestine and kidney. Thought to act as “intestinal natriuretic factors”, GN and UGN modulate renal salt secretion by both endocrine mechanisms (linking the digestive system and kidney) and paracrine/autocrine (intrarenal) mechanisms. The cellular function of GN and UGN in intestine and proximal tubule is mediated by guanylyl cyclase C (GC-C)-, cGMP-, and G protein-dependent pathways, whereas, in principal cells of the cortical collecting duct (CCD), these peptide hormones act via GC-C-independent signaling through phospholipase A2 (PLA2). The Cl-/HCO-3 exchanger pendrin (SLC26A4), encoded by the PDS gene, is expressed in non-α intercalated cells of the CCD. Pendrin is essential for CCD bicarbonate secretion and is also involved in NaCl balance and blood pressure regulation. Our recent studies have provided evidence that pendrin-mediated anion exchange in the CCD is regulated at the transcriptional level by UGN. UGN exerts an inhibitory effect on the pendrin gene promoter likely via heat shock factor 1 (HSF1) action at a defined heat shock element (HSE) site. Recent studies have unraveled novel roles for guanylin peptides in several organ systems including involvement in appetite regulation, olfactory function, cell proliferation and differentiation, inflammation, and reproductive function. Both the guanylin system and pendrin have also been implicated in airway function. Future molecular research into the receptors and signal transduction pathways involved in the action of guanylin peptides and the pendrin anion exchanger in the kidney and other organs, and into the links between them, may facilitate discovery of new therapies for hypertension, heart failure, hepatic failure and other fluid retention syndromes, as well as for diverse diseases such as obesity, asthma, and cancer.© 2014 S. Karger AG, Basel
Keywords	Renal tubule ; Chloride transport ; Anion exchange ; Promoter ; Guanylin peptides ; Guanylyl cyclase C ; Heat shock factor ; Electrolyte homeostasis
Language	English
Publisher	S. Karger AG
Publishing place	Basel
Publishing country	Switzerland
Document type	Article ; Online
ISSN	1421-9778 ; 1015-8987 ; 1015-8987
ISSN (online)	1421-9778
ISSN	1015-8987
DOI	10.1159/000356641
Database	Karger publisher's database

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Article: Pendrin, a Novel Transcriptional Target of the Uroguanylin System

Rozenfeld, Julia / Tal, Osnat / Kladnitsky, Orly / Adler, Lior / Efrati, Edna / Carrithers, Stephen L. / Alper, Seth L. / Zelikovic, Israel

Cellular Physiology and Biochemistry

2013 Volume 32, Issue 1, Page(s) 221–237

Institution	Laboratory of Developmental Nephrology, Department of Physiology and Biophysics, Faculty of Medicine, Technion-Israel Institute of Technology, and Division of Pediatric Nephrology, Rambam Medical Center, Haifa, Israel Sequela, Inc. Pewee Valley, KY Renal Division, Division of Molecular and Vascular Medicine, Center for Vascular Biology Research, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA, USA
Abstract	Guanylin (GN) and uroguanylin (UGN) are low-molecular-weight peptide hormones produced mainly in the intestinal mucosa in response to oral salt load. GN and UGN (guanylin peptides) induce secretion of electrolytes and water in both intestine and kidney. Thought to act as “intestinal natriuretic factors”, GN and UGN modulate renal salt secretion by both endocrine mechanisms (linking the digestive system and kidney) and paracrine/autocrine (intrarenal) mechanisms. The cellular function of GN and UGN in intestine and proximal tubule is mediated by guanylyl cyclase C (GC-C)-, cGMP-, and G protein-dependent pathways, whereas, in principal cells of the cortical collecting duct (CCD), these peptide hormones act via GC-C-independent signaling through phospholipase A2 (PLA2). The Cl/HCO3 exchanger pendrin (SLC26A4), encoded by the PDS gene, is expressed in non-α intercalated cells of the CCD. Pendrin is essential for CCD bicarbonate secretion and is also involved in NaCl balance and blood pressure regulation. Our recent studies have provided evidence that pendrin-mediated anion exchange in the CCD is regulated at the transcriptional level by UGN. UGN exerts an inhibitory effect on the pendrin gene promoter likely via heat shock factor 1 (HSF1) action at a defined heat shock element (HSE) site. Recent studies have unraveled novel roles for guanylin peptides in several organ systems including involvement in appetite regulation, olfactory function, cell proliferation and differentiation, inflammation, and reproductive function. Both the guanylin system and pendrin have also been implicated in airway function. Future molecular research into the receptors and signal transduction pathways involved in the action of guanylin peptides and the pendrin anion exchanger in the kidney and other organs, and into the links between them, may facilitate discovery of new therapies for hypertension, heart failure, hepatic failure and other fluid retention syndromes, as well as for diverse diseases such as obesity, asthma, and cancer.
Keywords	Renal tubule ; Chloride transport ; Anion exchange ; Promoter ; Guanylin peptides ; Guanylyl cyclase C ; Heat shock factor ; Electrolyte homeostasis
Language	English
Publishing date	2013-12-18
Publisher	S. Karger AG
Publishing place	Basel, Switzerland
Document type	Article
ZDB-ID	1067572-3
ISBN	978-3-318-05402-6 ; 3-318-05402-X
ISSN	1421-9778 ; 1015-8987
ISSN (online)	1421-9778
ISSN	1015-8987
DOI	10.1159/000356641
Database	Karger publisher's database

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Article ; Online: Gastrointestinal hormones: uroguanylin-a new gut-derived weapon against obesity?

Frühbeck, Gema

Nature reviews. Endocrinology

2011 Volume 8, Issue 1, Page(s) 5–6

Abstract: A recent report has identified uroguanylin as an endocrine signal that exerts a physiological role ... several observations highlight the uroguanylin–guanylyl cyclase C pathway as a potential therapeutic target ...

Abstract	A recent report has identified uroguanylin as an endocrine signal that exerts a physiological role in energy homeostasis, adding another factor to the gut–brain axis. From a clinical point of view, several observations highlight the uroguanylin–guanylyl cyclase C pathway as a potential therapeutic target for the development of antiobesity drugs.
MeSH term(s)	Animals ; Drug Design ; Drugs, Investigational/therapeutic use ; Female ; Gastrointestinal Hormones/metabolism ; Gastrointestinal Hormones/physiology ; Gastrointestinal Hormones/therapeutic use ; Humans ; Intestinal Mucosa/metabolism ; Male ; Mice ; Models, Biological ; Natriuretic Peptides/chemistry ; Natriuretic Peptides/metabolism ; Natriuretic Peptides/physiology ; Natriuretic Peptides/therapeutic use ; Obesity/drug therapy ; Obesity/metabolism ; Satiety Response/drug effects ; Satiety Response/physiology
Chemical Substances	Drugs, Investigational ; Gastrointestinal Hormones ; Natriuretic Peptides ; uroguanylin (152175-68-3)
Language	English
Publishing date	2011-11-15
Publishing country	England
Document type	News
ZDB-ID	2489381-X
ISSN	1759-5037 ; 1759-5029
ISSN (online)	1759-5037
ISSN	1759-5029
DOI	10.1038/nrendo.2011.206
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Article: A novel role for uroguanylin in the regulation of sodium balance.

Forte, Leonard R

The Journal of clinical investigation

2003 Volume 112, Issue 8, Page(s) 1138–1141

Abstract: ... 1244). A physiological role for uroguanylin is discussed, linking the intestine and kidney ... Uroguanylin is a peptide hormone that regulates sodium excretion by the kidney when excess NaCl is ... consumed. A new study demonstrates that mice deficient in uroguanylin have blunted urinary sodium excretion ...

Abstract	Uroguanylin is a peptide hormone that regulates sodium excretion by the kidney when excess NaCl is consumed. A new study demonstrates that mice deficient in uroguanylin have blunted urinary sodium excretion responses to oral sodium loads in addition to elevated blood pressure (see related article beginning on page 1244). A physiological role for uroguanylin is discussed, linking the intestine and kidney in an endocrine axis for the maintenance of sodium balance.
MeSH term(s)	Amino Acid Sequence ; Animals ; Disease Models, Animal ; Gastrointestinal Hormones/chemistry ; Gastrointestinal Hormones/physiology ; Humans ; Mice ; Molecular Sequence Data ; Natriuretic Peptides ; Peptides/chemistry ; Peptides/physiology ; Sodium/metabolism ; Water-Electrolyte Balance
Chemical Substances	Gastrointestinal Hormones ; Natriuretic Peptides ; Peptides ; guanylin (140653-38-9) ; uroguanylin (152175-68-3) ; Sodium (9NEZ333N27)
Language	English
Publishing date	2003-10
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	3067-3
ISSN	1558-8238 ; 0021-9738
ISSN (online)	1558-8238
ISSN	0021-9738
DOI	10.1172/JCI20057
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Article: Occurrence and localization of uroguanylin in the aging human prostate.

Maake, Caroline / Auf der Maur, Franziska / Jovanovic, Katarina / Reinecke, Manfred / Hauri, Dieter / John, Hubert

Histochemistry and cell biology

2003 Volume 119, Issue 1, Page(s) 69–76

Abstract: ... pro-)uroguanylin. We hypothesize that this hormone may play a novel role in the male reproductive ... in the regulation of epithelial salt and water transport processes. Since little is known about a possible role ... Uroguanylin, a peptide hormone highly expressed in the gastrointestinal tract, is implicated ...

Abstract	Uroguanylin, a peptide hormone highly expressed in the gastrointestinal tract, is implicated in the regulation of epithelial salt and water transport processes. Since little is known about a possible role of uroguanylin in the reproductive system, we investigated for the first time the occurrence of this peptide in the human prostate using specimens of benign prostatic hyperplasia. Northern blot analyses detected a single uroguanylin transcript of approximately 600 bp in prostate RNA. The uroguanylin expression was further investigated by reverse transcriptase polymerase chain reaction of prostate RNA with uroguanylin-specific primers. Sequencing of the fragments obtained indicated the presence of a uroguanylin molecule with a sequence identical to its intestinal counterpart. Furthermore, in situ hybridization and immunohistochemistry revealed that uroguanylin mRNA and peptide are confined to epithelial cells of the prostate glands. Comparison with the distribution pattern of immunoreactivity for prostate-specific antigen (PSA) showed a high degree of colocalization of uroguanylin- and PSA-immunoreactive cells. In addition, by western blotting techniques we detected the presence of high molecular weight uroguanylin-immunoreactive material in prostatic fluid. In conclusion, our study indicates that the human prostate glands synthesize and secrete (pro-)uroguanylin. We hypothesize that this hormone may play a novel role in the male reproductive tract.
MeSH term(s)	Aged ; Aging/physiology ; Blotting, Northern ; Humans ; Immunoenzyme Techniques ; In Situ Hybridization ; Male ; Middle Aged ; Natriuretic Peptides ; Peptides/analysis ; Peptides/genetics ; Peptides/metabolism ; Prostate/chemistry ; Prostate/metabolism ; Prostate/pathology ; Prostate-Specific Antigen/analysis ; Prostate-Specific Antigen/metabolism ; Prostatic Hyperplasia/metabolism ; Prostatic Hyperplasia/pathology ; RNA, Messenger/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Analysis, RNA
Chemical Substances	Natriuretic Peptides ; Peptides ; RNA, Messenger ; uroguanylin (152175-68-3) ; Prostate-Specific Antigen (EC 3.4.21.77)
Language	English
Publishing date	2003-01
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1222930-1
ISSN	1432-119X ; 0948-6143 ; 0301-5564
ISSN (online)	1432-119X
ISSN	0948-6143 ; 0301-5564
DOI	10.1007/s00418-002-0490-3
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Article: Mechanisms of action of uroguanylin and guanylin and their role in salt handling.

Sindić, Aleksandra / Schlatter, Eberhard

Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association

2006 Volume 21, Issue 11, Page(s) 3007–3012

MeSH term(s)	Animals ; Gastrointestinal Hormones/pharmacology ; Gastrointestinal Hormones/physiology ; Humans ; Natriuretic Peptides/pharmacology ; Natriuretic Peptides/physiology ; Salts/metabolism
Chemical Substances	Gastrointestinal Hormones ; Natriuretic Peptides ; Salts ; guanylin (140653-38-9) ; uroguanylin (152175-68-3)
Language	English
Publishing date	2006-11
Publishing country	England
Document type	Editorial ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	90594-x
ISSN	1460-2385 ; 0931-0509
ISSN (online)	1460-2385
ISSN	0931-0509
DOI	10.1093/ndt/gfl314
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