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Article ; Online: Comparative genomic analysis of Genlisea (corkscrew plants-Lentibulariaceae) chloroplast genomes reveals an increasing loss of the ndh genes.

Silva, Saura R / Michael, Todd P / Meer, Elliott J / Pinheiro, Daniel G / Varani, Alessandro M / Miranda, Vitor F O

2018 Volume 13, Issue 1, Page(s) e0190321

Abstract: In the carnivorous plant family Lentibulariaceae, all three genome compartments (nuclear, chloroplast, and mitochondria) have some of the highest rates of nucleotide substitutions across angiosperms. While the genera Genlisea and Utricularia have the ... ...

Abstract	In the carnivorous plant family Lentibulariaceae, all three genome compartments (nuclear, chloroplast, and mitochondria) have some of the highest rates of nucleotide substitutions across angiosperms. While the genera Genlisea and Utricularia have the smallest known flowering plant nuclear genomes, the chloroplast genomes (cpDNA) are mostly structurally conserved except for deletion and/or pseudogenization of the NAD(P)H-dehydrogenase complex (ndh) genes known to be involved in stress conditions of low light or CO2 concentrations. In order to determine how the cpDNA are changing, and to better understand the evolutionary history within the Genlisea genus, we sequenced, assembled and analyzed complete cpDNA from six species (G. aurea, G. filiformis, G. pygmaea, G. repens, G. tuberosa and G. violacea) together with the publicly available G. margaretae cpDNA. In general, the cpDNA structure among the analyzed Genlisea species is highly similar. However, we found that the plastidial ndh genes underwent a progressive process of degradation similar to the other terrestrial Lentibulariaceae cpDNA analyzed to date, but in contrast to the aquatic species. Contrary to current thinking that the terrestrial environment is a more stressful environment and thus requiring the ndh genes, we provide evidence that in the Lentibulariaceae the terrestrial forms have progressive loss while the aquatic forms have the eleven plastidial ndh genes intact. Therefore, the Lentibulariaceae system provides an important opportunity to understand the evolutionary forces that govern the transition to an aquatic environment and may provide insight into how plants manage water stress at a genome scale.
MeSH term(s)	Chloroplasts/genetics ; Genome, Chloroplast ; Magnoliopsida/classification ; Magnoliopsida/genetics ; NADPH Dehydrogenase/genetics ; Phylogeny
Chemical Substances	NADPH Dehydrogenase (EC 1.6.99.1)
Language	English
Publishing date	2018-01-02
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0190321
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Intraspecific Variation within the

Silva, Saura R / Pinheiro, Daniel G / Penha, Helen A / Płachno, Bartosz J / Michael, Todd P / Meer, Elliott J / Miranda, Vitor F O / Varani, Alessandro M

International journal of molecular sciences

2019 Volume 20, Issue 24

Abstract: Utricularia ... ...

Abstract	Utricularia amethystina
MeSH term(s)	DNA, Chloroplast/genetics ; Evolution, Molecular ; Genome, Chloroplast ; Lamiales/genetics ; Photosynthesis/genetics ; RNA Editing
Chemical Substances	DNA, Chloroplast
Language	English
Publishing date	2019-12-05
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms20246130
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Article ; Online: Combinatorial single-cell CRISPR screens by direct guide RNA capture and targeted sequencing.

Replogle, Joseph M / Norman, Thomas M / Xu, Albert / Hussmann, Jeffrey A / Chen, Jin / Cogan, J Zachery / Meer, Elliott J / Terry, Jessica M / Riordan, Daniel P / Srinivas, Niranjan / Fiddes, Ian T / Arthur, Joseph G / Alvarado, Luigi J / Pfeiffer, Katherine A / Mikkelsen, Tarjei S / Weissman, Jonathan S / Adamson, Britt

Nature biotechnology

2020 Volume 38, Issue 8, Page(s) 954–961

Abstract: Single-cell CRISPR screens enable the exploration of mammalian gene function and genetic regulatory networks. However, use of this technology has been limited by reliance on indirect indexing of single-guide RNAs (sgRNAs). Here we present direct-capture ... ...

Abstract	Single-cell CRISPR screens enable the exploration of mammalian gene function and genetic regulatory networks. However, use of this technology has been limited by reliance on indirect indexing of single-guide RNAs (sgRNAs). Here we present direct-capture Perturb-seq, a versatile screening approach in which expressed sgRNAs are sequenced alongside single-cell transcriptomes. Direct-capture Perturb-seq enables detection of multiple distinct sgRNA sequences from individual cells and thus allows pooled single-cell CRISPR screens to be easily paired with combinatorial perturbation libraries that contain dual-guide expression vectors. We demonstrate the utility of this approach for high-throughput investigations of genetic interactions and, leveraging this ability, dissect epistatic interactions between cholesterol biogenesis and DNA repair. Using direct capture Perturb-seq, we also show that targeting individual genes with multiple sgRNAs per cell improves efficacy of CRISPR interference and activation, facilitating the use of compact, highly active CRISPR libraries for single-cell screens. Last, we show that hybridization-based target enrichment permits sensitive, specific sequencing of informative transcripts from single-cell RNA-seq experiments.
MeSH term(s)	CRISPR-Cas Systems ; Gene Expression Regulation ; Gene Targeting ; HEK293 Cells ; High-Throughput Nucleotide Sequencing ; Humans ; Nucleic Acid Amplification Techniques/methods ; RNA, Guide, CRISPR-Cas Systems/genetics ; Single-Cell Analysis ; Transcriptome
Chemical Substances	RNA, Guide, CRISPR-Cas Systems
Language	English
Publishing date	2020-03-30
Publishing country	United States
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.
ZDB-ID	1311932-1
ISSN	1546-1696 ; 1087-0156
ISSN (online)	1546-1696
ISSN	1087-0156
DOI	10.1038/s41587-020-0470-y
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Article ; Online: Identification of a cis-acting element that localizes mRNA to synapses.

Meer, Elliott J / Wang, Dan Ohtan / Kim, Sangmok / Barr, Ian / Guo, Feng / Martin, Kelsey C

Proceedings of the National Academy of Sciences of the United States of America

2012 Volume 109, Issue 12, Page(s) 4639–4644

Abstract: Messenger RNA (mRNA) localization and regulated translation can spatially restrict gene expression to each of the thousands of synaptic compartments formed by a single neuron. Although cis-acting RNA elements have been shown to direct localization of ... ...

Abstract	Messenger RNA (mRNA) localization and regulated translation can spatially restrict gene expression to each of the thousands of synaptic compartments formed by a single neuron. Although cis-acting RNA elements have been shown to direct localization of mRNAs from the soma into neuronal processes, less is known about signals that target transcripts specifically to synapses. In Aplysia sensory-motor neuronal cultures, synapse formation rapidly redistributes the mRNA encoding the peptide neurotransmitter sensorin from neuritic shafts into synapses. We find that the export of sensorin mRNA from soma to neurite and the localization to synapse are controlled by distinct signals. The 3' UTR is sufficient for export into distal neurites, whereas the 5' UTR is required for concentration of reporter mRNA at synapses. We have identified a 66-nt element in the 5' UTR of sensorin that is necessary and sufficient for synaptic mRNA localization. Mutational and chemical probing analyses are consistent with a role for secondary structure in this process.
MeSH term(s)	5' Untranslated Regions ; Animals ; Aplysia ; DNA Mutational Analysis ; Electrophysiology/methods ; Genes, Reporter ; In Situ Hybridization, Fluorescence ; Neurons/metabolism ; Neuropeptides/metabolism ; Neurotransmitter Agents/metabolism ; Nucleic Acid Conformation ; Oligonucleotides, Antisense/metabolism ; RNA, Messenger/metabolism ; Sequence Analysis, RNA ; Synapses/metabolism
Chemical Substances	5' Untranslated Regions ; Neuropeptides ; Neurotransmitter Agents ; Oligonucleotides, Antisense ; RNA, Messenger ; sensorin A protein, Aplysia
Language	English
Publishing date	2012-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1116269109
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Article: Identification of a cis-acting element that localizes mRNA to synapses

Meer, Elliott J / Wang, Dan Ohtan / Kim, Sangmok / Barr, Ian / Guo, Feng / Martin, Kelsey C

Proceedings of the National Academy of Sciences of the United States of America. 2012 Mar. 20, v. 109, no. 12

2012

Abstract	Messenger RNA (mRNA) localization and regulated translation can spatially restrict gene expression to each of the thousands of synaptic compartments formed by a single neuron. Although cis-acting RNA elements have been shown to direct localization of mRNAs from the soma into neuronal processes, less is known about signals that target transcripts specifically to synapses. In Aplysia sensory-motor neuronal cultures, synapse formation rapidly redistributes the mRNA encoding the peptide neurotransmitter sensorin from neuritic shafts into synapses. We find that the export of sensorin mRNA from soma to neurite and the localization to synapse are controlled by distinct signals. The 3' UTR is sufficient for export into distal neurites, whereas the 5' UTR is required for concentration of reporter mRNA at synapses. We have identified a 66-nt element in the 5' UTR of sensorin that is necessary and sufficient for synaptic mRNA localization. Mutational and chemical probing analyses are consistent with a role for secondary structure in this process.
Keywords	3' untranslated regions ; gene expression ; neurites ; synapse ; translation (genetics)
Language	English
Dates of publication	2012-0320
Size	p. 4639-4644.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1116269109
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Article ; Online: The macula densa prorenin receptor is essential in renin release and blood pressure control.

Riquier-Brison, Anne D M / Sipos, Arnold / Prókai, Ágnes / Vargas, Sarah L / Toma, Lldikó / Meer, Elliott J / Villanueva, Karie G / Chen, Jennifer C M / Gyarmati, Georgina / Yih, Christopher / Tang, Elaine / Nadim, Bahram / Pendekanti, Sujith / Garrelds, Ingrid M / Nguyen, Genevieve / Danser, A H Jan / Peti-Peterdi, János

American journal of physiology. Renal physiology

2018 Volume 315, Issue 3, Page(s) F521–F534

Abstract: The prorenin receptor (PRR) was originally proposed to be a member of the renin-angiotensin system (RAS); however, recent work questioned their association. The present paper describes a functional link between the PRR and RAS in the renal ... ...

Abstract	The prorenin receptor (PRR) was originally proposed to be a member of the renin-angiotensin system (RAS); however, recent work questioned their association. The present paper describes a functional link between the PRR and RAS in the renal juxtaglomerular apparatus (JGA), a classic anatomical site of the RAS. PRR expression was found in the sensory cells of the JGA, the macula densa (MD), and immunohistochemistry-localized PRR to the MD basolateral cell membrane in mouse, rat, and human kidneys. MD cell PRR activation led to MAP kinase ERK1/2 signaling and stimulation of PGE
MeSH term(s)	Angiotensin-Converting Enzyme Inhibitors/pharmacology ; Animals ; Biosensing Techniques ; Blood Pressure/drug effects ; Captopril/pharmacology ; Cyclooxygenase 2/metabolism ; Diet, Sodium-Restricted ; Dinoprostone/metabolism ; Extracellular Signal-Regulated MAP Kinases/metabolism ; HEK293 Cells ; Humans ; Juxtaglomerular Apparatus/drug effects ; Juxtaglomerular Apparatus/enzymology ; Male ; Mice, Inbred C57BL ; Mice, Knockout ; Prostaglandin-E Synthases/metabolism ; Proton-Translocating ATPases/deficiency ; Proton-Translocating ATPases/genetics ; Proton-Translocating ATPases/metabolism ; Rats, Sprague-Dawley ; Receptors, Cell Surface/deficiency ; Receptors, Cell Surface/genetics ; Receptors, Cell Surface/metabolism ; Renin/metabolism ; Renin-Angiotensin System/drug effects ; Secretory Pathway ; Signal Transduction ; Vacuolar Proton-Translocating ATPases/genetics ; Vacuolar Proton-Translocating ATPases/metabolism
Chemical Substances	ATP6AP2 protein, human ; ATP6AP2 protein, mouse ; Angiotensin-Converting Enzyme Inhibitors ; Receptors, Cell Surface ; prorenin receptor ; Captopril (9G64RSX1XD) ; Ptgs2 protein, mouse (EC 1.14.99.-) ; Cyclooxygenase 2 (EC 1.14.99.1) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; Renin (EC 3.4.23.15) ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-) ; Proton-Translocating ATPases (EC 3.6.3.14) ; Prostaglandin-E Synthases (EC 5.3.99.3) ; Ptges protein, mouse (EC 5.3.99.3) ; Dinoprostone (K7Q1JQR04M)
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.00029.2018
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Article ; Online: Activation of the succinate receptor GPR91 in macula densa cells causes renin release.

Vargas, Sarah Laurin / Toma, Ildikó / Kang, Jung Julie / Meer, Elliott James / Peti-Peterdi, János

Journal of the American Society of Nephrology : JASN

2009 Volume 20, Issue 5, Page(s) 1002–1011

Abstract: Macula densa (MD) cells of the juxtaglomerular apparatus (JGA) are salt sensors and generate paracrine signals that control renal blood flow, glomerular filtration, and release of the prohypertensive hormone renin. We hypothesized that the recently ... ...

Abstract	Macula densa (MD) cells of the juxtaglomerular apparatus (JGA) are salt sensors and generate paracrine signals that control renal blood flow, glomerular filtration, and release of the prohypertensive hormone renin. We hypothesized that the recently identified succinate receptor GPR91 is present in MD cells and regulates renin release. Using immunohistochemistry, we identified GPR91 in the apical plasma membrane of MD cells. Treatment of MD cells with succinate activated mitogen-activated protein kinases (MAPKs; p38 and extracellular signal-regulated kinases 1/2) and cyclooxygenase 2 (COX-2) and induced the synthesis and release of prostaglandin E(2), a potent vasodilator and classic paracrine mediator of renin release. Using microperfused JGA and real-time confocal fluorescence imaging of quinacrine-labeled renin granules, we detected significant renin release in response to tubular succinate (EC(50) 350 microM). Genetic deletion of GPR91 (GPR91(-/-) mice) or pharmacologic inhibition of MAPK or COX-2 blocked succinate-induced renin release. Streptozotocin-induced diabetes caused GPR91-dependent upregulation of renal cortical phospho-p38, extracellular signal-regulated kinases 1/2, COX-2, and renin content. Salt depletion for 1 wk increased plasma renin activity seven-fold in wild-type mice but only 3.4-fold in GPR91(-/-) mice. In summary, MD cells can sense alterations in local tissue metabolism via accumulation of tubular succinate and GPR91 signaling, which involves the activation of MAPKs, COX-2, and the release of prostaglandin E(2). This mechanism may be integral in the regulation of renin release and activation of the renin-angiotensin system in health and disease.
MeSH term(s)	Animals ; Arterioles/physiology ; Biomarkers/analysis ; Gene Deletion ; Immunohistochemistry ; Juxtaglomerular Apparatus/cytology ; Juxtaglomerular Apparatus/physiology ; Kidney/enzymology ; Kidney/physiology ; Kidney Tubules/physiology ; Mice ; Mice, Knockout ; Nitric Oxide Synthase Type I/analysis ; Receptors, G-Protein-Coupled/deficiency ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/physiology ; Renal Circulation/physiology ; Renin/metabolism ; Renin-Angiotensin System/physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction ; Succinates/antagonists & inhibitors ; Succinates/metabolism ; Succinates/pharmacology
Chemical Substances	Biomarkers ; GPR91 protein, mouse ; Receptors, G-Protein-Coupled ; Succinates ; Nitric Oxide Synthase Type I (EC 1.14.13.39) ; Renin (EC 3.4.23.15)
Language	English
Publishing date	2009-04-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1085942-1
ISSN	1533-3450 ; 1046-6673
ISSN (online)	1533-3450
ISSN	1046-6673
DOI	10.1681/ASN.2008070740
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Article: Succinate receptor GPR91 provides a direct link between high glucose levels and renin release in murine and rabbit kidney.

Toma, Ildikó / Kang, Jung Julie / Sipos, Arnold / Vargas, Sarah / Bansal, Eric / Hanner, Fiona / Meer, Elliott / Peti-Peterdi, János

The Journal of clinical investigation

2008 Volume 118, Issue 7, Page(s) 2526–2534

Abstract: Diabetes mellitus is the most common and rapidly growing cause of end-stage renal disease in developed countries. A classic hallmark of early diabetes mellitus includes activation of the renin-angiotensin system (RAS), which may lead to hypertension and ... ...

Abstract	Diabetes mellitus is the most common and rapidly growing cause of end-stage renal disease in developed countries. A classic hallmark of early diabetes mellitus includes activation of the renin-angiotensin system (RAS), which may lead to hypertension and renal tissue injury, but the mechanism of RAS activation is elusive. Here we identified a paracrine signaling pathway in the kidney in which high levels of glucose directly triggered the release of the prohypertensive hormone renin. The signaling cascade involved the local accumulation of succinate and activation of the kidney-specific G protein-coupled metabolic receptor, GPR91, in the glomerular endothelium as observed in rat, mouse, and rabbit kidney sections. Elements of signal transduction included endothelial Ca2+, the production of NO and prostaglandin (PGE2), and their paracrine actions on adjacent renin-producing cells. This GPR91 signaling cascade may serve to modulate kidney function and help remove metabolic waste products through renal hyperfiltration, and it could also link metabolic diseases, such as diabetes, or metabolic syndrome with RAS overactivation, systemic hypertension, and organ injury.
MeSH term(s)	Animals ; Calcium Signaling/drug effects ; Calcium Signaling/physiology ; Citrates/pharmacology ; Diabetes Mellitus, Experimental/metabolism ; Diabetes Mellitus, Experimental/urine ; Dinoprostone/antagonists & inhibitors ; Dinoprostone/metabolism ; Endothelial Cells/metabolism ; Female ; Glucose/pharmacology ; Hyperglycemia/metabolism ; Juxtaglomerular Apparatus/drug effects ; Juxtaglomerular Apparatus/metabolism ; Kidney/metabolism ; Male ; Malonates/pharmacology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mice, Transgenic ; Nitric Oxide/antagonists & inhibitors ; Nitric Oxide/metabolism ; Paracrine Communication/drug effects ; Paracrine Communication/physiology ; Rabbits ; Rats ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/physiology ; Renin/blood ; Renin/metabolism ; Succinic Acid/metabolism ; Succinic Acid/pharmacology ; Succinic Acid/urine
Chemical Substances	Citrates ; GPR91 protein, mouse ; Malonates ; Receptors, G-Protein-Coupled ; Nitric Oxide (31C4KY9ESH) ; fluorocitrate (357-89-1) ; malonic acid (9KX7ZMG0MK) ; Succinic Acid (AB6MNQ6J6L) ; Renin (EC 3.4.23.15) ; Glucose (IY9XDZ35W2) ; Dinoprostone (K7Q1JQR04M)
Language	English
Publishing date	2008-06-06
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/JCI33293
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Article ; Online: The collecting duct is the major source of prorenin in diabetes.

Kang, Jung J / Toma, Ildikó / Sipos, Arnold / Meer, Elliott J / Vargas, Sarah L / Peti-Peterdi, János

Hypertension (Dallas, Tex. : 1979)

2008 Volume 51, Issue 6, Page(s) 1597–1604

Abstract: In addition to the juxtaglomerular apparatus, renin is also synthesized in renal tubular epithelium, including the collecting duct (CD). Angiotensin (Ang) II differentially regulates the synthesis of juxtaglomerular (inhibition) and CD (stimulation) ... ...

Abstract	In addition to the juxtaglomerular apparatus, renin is also synthesized in renal tubular epithelium, including the collecting duct (CD). Angiotensin (Ang) II differentially regulates the synthesis of juxtaglomerular (inhibition) and CD (stimulation) renin. Because diabetes mellitus, a disease with high intrarenal renin-Ang system and Ang II activity, is characterized by high prorenin levels, we hypothesized that the CD is the major source of prorenin in diabetes. Renin granular content was visualized using in vivo multiphoton microscopy of the kidney in diabetic Munich-Wistar rats. Diabetes caused a 3.5-fold increase in CD renin, in contrast to less pronounced juxtaglomerular changes. Ang II type 1 receptor blockade with Olmesartan reduced CD renin to control levels but significantly increased juxtaglomerular renin. Using a fluorogenic renin assay, the prorenin component of CD renin content was measured by assessing the difference in enzymatic activity of medullary homogenates before and after trypsin activation of prorenin. Trypsinization caused no change in control renin activity but a 5-fold increase in diabetes. Studies on a CD cell line (M1) showed a 22-fold increase in renin activity after trypsinization and a further 35-fold increase with Ang II treatment. Therefore, prorenin significantly contributes to baseline CD renin. Diabetes, possibly via Ang II, greatly stimulates CD prorenin and causes hyperplasia of renin-producing connecting segments. These novel findings suggest that, in a rat model of diabetes, prorenin content and release from the CD may be more important than the juxtaglomerular apparatus in contrast to the existing paradigm.
MeSH term(s)	Angiotensin II/metabolism ; Angiotensin II/pharmacology ; Angiotensin II Type 1 Receptor Blockers/pharmacology ; Animals ; Cell Division/physiology ; Cells, Cultured ; Diabetes Mellitus, Experimental/metabolism ; Diabetic Nephropathies/metabolism ; Disease Models, Animal ; Hypertension, Renal/metabolism ; Imidazoles/pharmacology ; Immunohistochemistry ; Juxtaglomerular Apparatus/cytology ; Juxtaglomerular Apparatus/metabolism ; Kidney Tubules, Collecting/cytology ; Kidney Tubules, Collecting/metabolism ; Microscopy, Fluorescence ; Quinacrine ; Rats ; Rats, Wistar ; Renin/metabolism ; Tetrazoles/pharmacology ; Trypsin ; Vasoconstrictor Agents/metabolism ; Vasoconstrictor Agents/pharmacology
Chemical Substances	Angiotensin II Type 1 Receptor Blockers ; Imidazoles ; Tetrazoles ; Vasoconstrictor Agents ; Angiotensin II (11128-99-7) ; olmesartan (8W1IQP3U10) ; Trypsin (EC 3.4.21.4) ; Renin (EC 3.4.23.15) ; Quinacrine (H0C805XYDE)
Language	English
Publishing date	2008-04-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	423736-5
ISSN	1524-4563 ; 0194-911X ; 0362-4323
ISSN (online)	1524-4563
ISSN	0194-911X ; 0362-4323
DOI	10.1161/HYPERTENSIONAHA.107.107268
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Article: Connexin 40 and ATP-dependent intercellular calcium wave in renal glomerular endothelial cells.

Toma, Ildikó / Bansal, Eric / Meer, Elliott J / Kang, Jung Julie / Vargas, Sarah L / Peti-Peterdi, János

American journal of physiology. Regulatory, integrative and comparative physiology

2008 Volume 294, Issue 6, Page(s) R1769–76

Abstract: Endothelial intracellular calcium ([Ca(2+)](i)) plays an important role in the function of the juxtaglomerular vasculature. The present studies aimed to identify the existence and molecular elements of an endothelial calcium wave in cultured glomerular ... ...

Abstract	Endothelial intracellular calcium ([Ca(2+)](i)) plays an important role in the function of the juxtaglomerular vasculature. The present studies aimed to identify the existence and molecular elements of an endothelial calcium wave in cultured glomerular endothelial cells (GENC). GENCs on glass coverslips were loaded with Fluo-4/Fura red, and ratiometric [Ca(2+)](i) imaging was performed using fluorescence confocal microscopy. Mechanical stimulation of a single GENC caused a nine-fold increase in [Ca(2+)](i), which propagated from cell to cell throughout the monolayer (7.9 +/- 0.3 microm/s) in a regenerative manner (without decrement of amplitude, kinetics, and speed) over distances >400 microm. Inhibition of voltage-dependent calcium channels with nifedipine had no effect on the above parameters, but the removal of extracellular calcium reduced Delta[Ca(2+)](i) by 50%. Importantly, the gap junction uncoupler alpha-glycyrrhetinic acid or knockdown of connexin 40 (Cx40) by transfecting GENCs with Cx40 short interfering RNA (siRNA) almost completely eliminated Delta[Ca(2+)](i) and the calcium wave. Breakdown of extracellular ATP using a scavenger cocktail (apyrase and hexokinase) or nonselective inhibition of purinergic P2 receptors with suramin, had similar blocking effects. Scraping cells off along a line eliminated physical contact between cells but did not effect calcium wave propagation. Using an ATP biosensor technique, we detected a significant elevation in extracellular ATP (Delta = 76 +/- 2 microM) during calcium wave propagation, which was abolished by Cx40 siRNA treatment (Delta = 6 +/- 1 microM). These studies suggest that connexin 40 hemichannels and extracellular ATP are key molecular elements of the glomerular endothelial calcium wave, which may serve important juxtaglomerular functions.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Animals ; Calcium/metabolism ; Calcium Signaling/physiology ; Cell Line ; Connexins/genetics ; Connexins/metabolism ; Endothelium/cytology ; Endothelium/drug effects ; Endothelium/metabolism ; Glomerular Filtration Rate/physiology ; Glycyrrhetinic Acid/pharmacology ; Juxtaglomerular Apparatus/physiology ; Kidney Glomerulus/cytology ; Kidney Glomerulus/drug effects ; Kidney Glomerulus/metabolism ; Mice ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Purinergic P2 Receptor Antagonists ; RNA, Small Interfering/pharmacology ; Receptors, Purinergic P2/drug effects ; Receptors, Purinergic P2/metabolism ; Renin/metabolism ; Suramin/pharmacology ; Gap Junction alpha-5 Protein
Chemical Substances	Connexins ; Protein Isoforms ; Purinergic P2 Receptor Antagonists ; RNA, Small Interfering ; Receptors, Purinergic P2 ; Suramin (6032D45BEM) ; Adenosine Triphosphate (8L70Q75FXE) ; Renin (EC 3.4.23.15) ; Glycyrrhetinic Acid (P540XA09DR) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2008-04-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	603839-6
ISSN	1522-1490 ; 0363-6119
ISSN (online)	1522-1490
ISSN	0363-6119
DOI	10.1152/ajpregu.00489.2007
Database	MEDical Literature Analysis and Retrieval System OnLINE

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