Distinct cellular localization of mRNAs for three subtypes of prostaglandin E receptor in kidney

1994 ◽  
Vol 266 (5) ◽  
pp. F823-F828 ◽  
Author(s):  
Y. Sugimoto ◽  
T. Namba ◽  
R. Shigemoto ◽  
M. Negishi ◽  
A. Ichikawa ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Cellular Localization ◽  
Mouse Kidney ◽  
Prostaglandin E ◽  
Outer Medulla ◽  
Multiple Functions ◽  
Collecting Ducts ◽  
Distal Tubules ◽  
Stimulation Of

Distribution of the mRNAs for three subtypes of prostaglandin E (PGE) receptors in the mouse kidney was investigated by in situ hybridization. The mRNA for EP1 subtype, which is coupled to Ca2+ mobilization, was specifically localized to the collecting ducts from the cortex to the papilla. The mRNA for EP2 subtype, which is linked to stimulation of adenylate cyclase, was localized to the glomeruli. The mRNA for EP3 subtype, which is coupled to inhibition of adenylate cyclase, was located densely in the tubules in the outer medulla and in the distal tubules in the cortex. These results exhibit distinct cellular localization of three subtypes of PGE receptor in the kidney and suggest that PGE2 exerts multiple functions via these subtypes expressed in different segments of the nephron.

Intrarenal and Cellular Localization of CLC-K2 Protein in the Mouse Kidney

2001 ◽  
Vol 12 (7) ◽  
pp. 1327-1334 ◽  
Author(s):  
KATSUKI KOBAYASHI ◽  
SHINICHI UCHIDA ◽  
SHUKI MIZUTANI ◽  
SEI SASAKI ◽  
FUMIAKI MARUMO
Keyword(s):  
Cellular Localization ◽  
Collecting Duct ◽  
Type A ◽  
Mouse Kidney ◽  
Thick Ascending Limb ◽  
Intercalated Cells ◽  
Basolateral Membranes ◽  
Nephron Segments ◽  
Henle's Loop ◽  
Distal Tubules

Abstract. CLC-K2, a kidney-specific member of the CLC chloride channel family, is thought to play an important role in the transepithelial Cl- transport in the kidney. This consensus was first reached shortly after it was demonstrated that the mutations of the human CLCNKB gene resulted in Bartter's syndrome type III. To clarify the pathogenesis, the exact intrarenal and cellular localization of CLC-K2 by immunohistochemistry of the Clcnk1-/- mouse kidney were investigated by use of an anti-CLC-K antibody that recognized both CLC-K1 and CLC-K2. CLC-K2 is expressed in the thick ascending limb of Henle's loop and distal tubules, where it is localized to the basolateral membranes. The localization of CLC-K2 to these nephron segments strongly implies that CLC-K2 confers the basolateral chloride conductance in the thick ascending limb of Henle's loop and distal tubules, where Cl- is taken up by the bumetanide-sensitive Na-K-2Cl cotransporter or the thiazide-sensitive Na-Cl cotransporter at the apical membranes. CLC-K2 expression was also shown to extend into the connecting tubule in the basolateral membrane. CLC-K2 was found in basolateral membranes of the type A intercalated cells residing along the collecting duct. This localization strongly suggests that CLC-K2 confers the basolateral conductance in the type A intercalated cells where Cl- is taken up by the anion exchanger in exchange for HCO3- at the basolateral membranes. These aspects of CLC-K2 localization suggest that CLC-K2 is important in Cl- transport in the distal nephron segments.

Cellular localization of mRNAs for prostaglandin E receptor subtypes in mouse gastrointestinal tract

1997 ◽  
Vol 272 (3) ◽  
pp. G681-G687 ◽  
Author(s):  
K. Morimoto ◽  
Y. Sugimoto ◽  
M. Katsuyama ◽  
H. Oida ◽  
K. Tsuboi ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Epithelial Cells ◽  
Cellular Localization ◽  
The Body ◽  
Prostaglandin E ◽  
Receptor Subtypes ◽  
Fundic Gland ◽  
Intestinal Functions ◽  
Myenteric Ganglia

Regional and cellular distribution of mRNAs for prostaglandin E (PGE) receptor subtypes was investigated in the mouse gastrointestinal tract by in situ hybridization. Strong signals for EP1 transcripts were detected in cells of the muscularis mucosae layer, especially in the body of the stomach. Intense signals for EP3 transcripts were detected in neurons of the myenteric ganglia throughout the tract. Moderate EP3 mRNA expression was also observed in fundic gland epithelial cells, except for surface mucous cells in the stomach. Expression of EP4 mRNA was moderate in surface epithelial cells of the corpus and in glands from the surface to the base of the antrum. Strong EP4 signals were observed in the epithelium in the duodenum, jejunum, and ileum. In the ileum, signals were only observed in the upper part of the villi. However, no or weak signals for EP2 transcripts were detected. These findings suggest that PGE2 modulates various gastric or intestinal functions via at least three different PGE receptors.

scholarly journals Stimulation of hormone-responsive adenylate cyclase activity by a factor present in the cell cytosol

1980 ◽  
Vol 188 (2) ◽  
pp. 393-400 ◽  
Author(s):  
S MacNeil ◽  
A Crawford ◽  
H Amirrasooli ◽  
S Johnson ◽  
A Pollock ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Adenylate Cyclase ◽  
Prostaglandin E1 ◽  
Enzyme Activation ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Prostaglandin E ◽  
Human Articular Cartilage ◽  
Cell Cytosol ◽  
Stimulation Of

1. Homogenates of whole tissues were shown to contain both intracellular and extracellular factors that affected particulate adenylate cyclase activity in vitro. Factors present in the extracellular fluids produced an inhibition of basal, hormone- and fluoride-stimulated enzyme activity but factors present in the cell cytosol increased hormone-stimulated activity with relatively little effect on basal or fluoride-stimulated enzyme activity. 2. The existence of this cytosol factor or factors was investigated using freshly isolated human platelets, freshly isolated rat hepatocytes, and cultured cells derived from rat osteogenic sarcoma, rat calvaria, mouse melanoma, pig aortic endothelium, human articular cartilage chondrocytes and human bronchial carcinoma (BEN) cells. 3. The stimulation of the hormone response by the cytosol factor ranged from 60 to 890% depending on the tissue of origin of the adenylate cyclase. 4. In each case the behaviour of the factor was similar to the action of GTP on that particular adenylate cyclase preparation. 5. No evidence of tissue or species specificity was found, as cytosols stimulated adenylate cyclase from their own and unrelated tissues to the same degree. 6. In the human platelet, the inclusion of the cytosol in the assay of adenylate cyclase increased the rate of enzyme activity in response to stimulation by prostaglandin E1 without affecting the amount of prostaglandin E1 required for half-maximal stimulation or the characteristics of enzyme activation by prostaglandin E.

Stimulation of prostaglandin E adenylate cyclase response in pig epidermis by hydrocortisone

1989 ◽  
Vol 281 (3) ◽  
pp. 215-217 ◽  
Author(s):  
H. Koizumi ◽  
C. Yasui ◽  
T. Shimizu ◽  
A. Ohkawara
Keyword(s):  
Adenylate Cyclase ◽  
Prostaglandin E ◽  
Stimulation Of

Parathyroid hormone stimulation of the Na+/K+ pump in rat clonal osteosarcoma cells

1986 ◽  
Vol 111 (1) ◽  
pp. 61-66 ◽  
Author(s):  
M. De Luise ◽  
M. Harker
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Osteogenic Sarcoma ◽  
Monovalent Cation ◽  
Prostaglandin E ◽  
Adenylate Cyclase System ◽  
Pump Activity ◽  
Umr 106 ◽  
Insight Into ◽  
Stimulation Of

ABSTRACT A clonal line of osteoblastic cells from a rat osteogenic sarcoma (UMR 106–06), known to possess parathyroid hormone (PTH)-responsive adenylate cyclase, has been shown to increase its rate of K+ uptake mediated by a Na+/K+ pump after exposure to the hormone. The increase in pump activity was not associated with significant changes in K+ efflux or Na+ influx and would therefore be expected to alter intracellular levels of both Na+ and K+. The maximal (75%) increase in pump activity was noted at a PTH concentration of 100 μg/l and half-maximal stimulation at 1·9 μg/l. The effect appeared to be independent of the adenylate cyclase system, since a synthetic peptide antagonist of PTH activation of adenylate cyclase failed to prevent stimulation of the Na+/K+ pump. Similarly, prostaglandin E2, an alternative agonist of adenylate cyclase in these cells, had no effect on the Na+/K+ pump. This novel action of PTH on monovalent cation transport in osteoblast-like cells should provide a clearer insight into the mechanisms of hormone-induced bone resorption. J. Endocr. (1986) 111, 61–66

Cellular localization of low-molecular-weight kininogen and bradykinin B2 receptor mRNAs in human kidney

1996 ◽  
Vol 270 (6) ◽  
pp. F919-F926 ◽  
Author(s):  
Q. Song ◽  
D. Z. Wang ◽  
R. A. Harley ◽  
L. Chao ◽  
J. Chao
Keyword(s):  
Molecular Weight ◽  
Endothelial Cells ◽  
Cellular Localization ◽  
Human Kidney ◽  
Low Molecular Weight ◽  
Bradykinin B2 Receptor ◽  
Receptor Mrna ◽  
Collecting Ducts ◽  
Distal Tubules ◽  
Receptor Mrnas

Kininogen is the precursor of the kinin peptide, which binds to kinin receptors and mediates a broad spectrum of physiological effects. To understand the function of kinin in the kidney, we have identified the cellular localization of the human low-molecular-weight (LMW) kininogen and bradykinin B2 receptor mRNAs in the human kidney by in situ hybridization histochemistry. Kininogen mRNA was found in the juxtaglomerular cells, mesangial areas, epithelium of parietal and visceral (podocytes) layers of Bowman's capsule, proximal and distal tubules, thin and thick segments of Henle's loop, collecting ducts, and the endothelial cells of the blood vessels. B2 receptor mRNA was colocalized with kininogen mRNA in the kidney except the podocytes. The most intense signals were observed in the distal tubules and collecting ducts for both kininogen and B2 receptor mRNAs. No signals were observed in the interstitial cells and macula densa. Control sections did not stain with either the kininogen or B2 receptor sense riboprobe. A Northern blot showed that the expression of LMW kininogen is in the liver and the kidney. Reverse transcription-polymerase chain reaction Southern blot showed expression of B2 receptor mRNA in the endothelial cells, renal proximal tubular cells, and kidney. Our results show the sites of action of kinin in the human kidney and provide further insight into the physiological role of the kallikrein-kinin system on renal function.

scholarly journals Cellular localization of adenine receptors in the rat kidney and their functional significance in the inner medullary collecting duct

2013 ◽  
Vol 305 (9) ◽  
pp. F1298-F1305 ◽  
Author(s):  
Bellamkonda K. Kishore ◽  
Yue Zhang ◽  
Haykanush Gevorgyan ◽  
Donald E. Kohan ◽  
Anke C. Schiedel ◽  
...  
Keyword(s):  
Cellular Localization ◽  
Ex Vivo ◽  
Collecting Duct ◽  
Rat Kidney ◽  
Apical Plasma Membrane ◽  
Renal Vasculature ◽  
Outer Medulla ◽  
Collecting Ducts ◽  
Rabbit Polyclonal Antibody ◽  
Immunofluorescence Labeling

The Gi-coupled adenine receptor (AdeR) binds adenine with high affinity and potentially reduces cellular cAMP levels. Since cAMP is an important second messenger in the renal transport of water and solutes, we localized AdeR in the rat kidney. Real-time RT-PCR showed higher relative expression of AdeR mRNA in the cortex and outer medulla compared with the inner medulla. Immunoblots using a peptide-derived and affinity-purified rabbit polyclonal antibody specific for an 18-amino acid COOH-terminal sequence of rat AdeR, which we generated, detected two bands between ∼30 and 40 kDa (molecular mass of native protein: 37 kDa) in the cortex, outer medulla, and inner medulla. These bands were ablated by preadsorption of the antibody with the immunizing peptide. Immunofluorescence labeling showed expression of AdeR protein in all regions of the kidney. Immunoperoxidase revealed strong labeling of AdeR protein in the cortical vasculature, including the glomerular arterioles, and less intense labeling in the cells of the collecting duct system. Confocal immunofluorescence imaging colocalized AdeR with aquaporin-2 protein to the apical plasma membrane in the collecting duct. Functionally, adenine (10 μM) significantly decreased ( P < 0.01) 1-deamino-8-d-arginine vasopressin (10 nM)-induced cAMP production in ex vivo preparations of inner medullary collecting ducts, which was reversed by PSB-08162 (20 μM, P < 0.01), a selective antagonist of AdeR. Thus, we demonstrated the expression of AdeR in the renal vasculature and collecting ducts and its functional relevance. This study may open a new avenue for the exploration of autocrine/paracrine regulation of renal vascular and tubular functions by the nucleobase adenine in health and disease.

scholarly journals Cholera Toxin B Subunit Activates Arachidonic Acid Metabolism

1999 ◽  
Vol 67 (2) ◽  
pp. 794-799 ◽  
Author(s):  
Johnny W. Peterson ◽  
Richard A. Finkelstein ◽  
Juan Cantu ◽  
Deborah L. Gessell ◽  
Ashok K. Chopra
Keyword(s):  
Arachidonic Acid ◽  
Adenylate Cyclase ◽  
Cholera Toxin ◽  
Prostaglandin E ◽  
Activation Process ◽  
Transferase Activity ◽  
Cholera Toxin B Subunit ◽  
Lymphoma Cells ◽  
Adp Ribosylation ◽  
Stimulation Of

ABSTRACT Cholera toxin (CT) increases intestinal secretion of water and electrolytes and modulates the mucosal immune response by stimulating cellular synthesis of arachidonic acid (AA) metabolites (e.g., prostaglandin E2), as well as the intracellular second messenger cyclic AMP (cAMP). While much is known about the mechanism of CT stimulation of adenylate cyclase, the toxin’s activation of phospholipase A2, which results in increased hydrolysis of AA from membrane phospholipids, is not well understood. To determine whether CT activation of AA metabolism requires CT’s known enzymatic activity (i.e., ADP-ribosylation of GSα), we used native CT and a mutant CT protein (CT-2*) lacking ADP-ribose transferase activity in combination with S49 wild-type (WT) and S49 cyc− murine Theta (Th)1.2-positive lymphoma cells deficient in GSα. The experimental results showed that native CT stimulated the release of [3H[AA from S49 cyc− cells at a level similar to that for S49 WT cells, indicating that GSα is not essential for this process. Further, levels of cAMP in the CT-treated cyc− cells remained the same as those in the untreated control cells. The ADP-ribosyltransferase-deficient CT-2* protein, which was incapable of increasing synthesis of cAMP, displayed about the same capacity as CT to evoke the release of [3H]AA metabolites from both S49 WT and cyc− cells. We concluded that stimulation of arachidonate metabolism in S49 murine lymphoma cells by native CT does not require enzymatically functional CT, capable of catalyzing the ADP-ribosylation reaction. These results demonstrated for the first time that stimulation of adenylate cyclase by CT and stimulation of AA metabolism by CT are not necessarily coregulated. In addition, the B subunits purified from native CT and CT-2* both simulated the release of [3H]AA from S49 cyc− cells and murine monocyte/macrophage cells (RAW 264.7), suggesting a receptor-mediated cell activation process of potential importance in enhancing immune responses to vaccine components.

scholarly journals Effects of Angiotensin II on Erythropoietin Production in the Kidney and Liver

Molecules ◽  
2021 ◽  
Vol 26 (17) ◽  
pp. 5399
Author(s):  
Yukiko Yasuoka ◽  
Yuichiro Izumi ◽  
Takashi Fukuyama ◽  
Hideki Inoue ◽  
Tomomi Oshima ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Protein Expression ◽  
Renal Cortex ◽  
The Body ◽  
Outer Medulla ◽  
Main Site ◽  
Erythropoietin Production ◽  
Collecting Ducts ◽  
Mrna And Protein Expression

The kidney is a main site of erythropoietin production in the body. We developed a new method for the detection of Epo protein by deglycosylation-coupled Western blotting. Detection of deglycosylated Epo enables the examination of small changes in Epo production. Using this method, we investigated the effects of angiotensin II (ATII) on Epo production in the kidney. ATII stimulated the plasma Epo concentration; Epo, HIF2α, and PHD2 mRNA expression in nephron segments in the renal cortex and outer medulla; and Epo protein expression in the renal cortex. In situ hybridization and immunohistochemistry revealed that ATII stimulates Epo mRNA and protein expression not only in proximal tubules but also in collecting ducts, especially in intercalated cells. These data support the regulation of Epo production in the kidney by the renin–angiotensin–aldosterone system (RAS).

scholarly journals Pulmonary and Cardiorenal Cyclooxygenase-1 (COX-1), -2 (COX-2), and Microsomal Prostaglandin E Synthase-1 (mPGES-1) and -2 (mPGES-2) Expression in a Hypertension Model

2007 ◽  
Vol 2007 ◽  
pp. 1-8 ◽  
Author(s):  
Zaher A. Radi ◽  
Robert Ostroski
Keyword(s):  
Epithelial Cells ◽  
Alveolar Macrophages ◽  
Cellular Localization ◽  
Vascular Endothelial Cells ◽  
Prostaglandin E ◽  
Human Hypertension ◽  
Collecting Ducts ◽  
Cox 2 ◽  
Convoluted Tubules ◽  
Cox 1

Hypertensive mice that express the human renin and angiotensinogen genes are used as a model for human hypertension because they develop hypertension secondary to increased renin-angiotensin system activity. Our study investigated the cellular localization and distribution of COX-1, COX-2, mPGES-1, and mPGES-2 in organ tissues from a mouse model of human hypertension. Male (n=15) and female (n=15) double transgenic mice (h-Ang 204/1 h-Ren 9) were used in the study. Lung, kidney, and heart tissues were obtained from mice at necropsy and fixed in 10%neutral buffered formalin followed by embedding in paraffin wax. Cut sections were stained immunohistochemically with antibodies to COX-1, COX-2, mPGES-1, and mPGES-2 and analyzed by light microscopy. Renal expression of COX-1 was the highest in the distal convoluted tubules, cortical collecting ducts, and medullary collecting ducts; while proximal convoluted tubules lacked COX-1 expression. Bronchial and bronchiolar epithelial cells, alveolar macrophages, and cardiac vascular endothelial cells also had strong COX-1 expression, with other renal, pulmonary, or cardiac microanatomic locations having mild-to-moderate expression. mPGES-2 expression was strong in the bronchial and bronchiolar epithelial cells, mild to moderate in various renal microanatomic locations, and absent in cardiac tissues. COX-2 expression was strong in the proximal and distal convoluted tubules, alveolar macrophages, and bronchial and bronchiolar epithelial cells. Marked mPGES-1 was present only in bronchial and bronchiolar epithelial cells; while mild-to-moderate expression was present in other pulmonary, renal, or cardiac microanatomic locations. Expression of these molecules was similar between males and females. Our work suggests that in hypertensive mice, there are (a) significant microanatomic variations in the pulmonary, renal, and cardiac distribution and cellular localization of COX-1, COX-2, mPGES-1, and mPGES-2, and (b) no differences in expression between genders.

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