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Article ; Online: Comprehensive analytical and clinical evaluation of a RNA extraction-free saliva-based molecular assay for SARS-CoV-2.

Schoeber, Joost P H / Schlaghecke, Juliëtte M / Meuwissen, Britt M J / van Heertum, Mara / van den Brule, Adriaan J C / Loonen, Anne J M

PloS one

2022 Volume 17, Issue 5, Page(s) e0268082

Abstract: Standard SARS-CoV-2 testing protocols using nasopharyngeal/throat (NP/T) swabs are invasive and require trained medical staff for reliable sampling. In addition, it has been shown that PCR is more sensitive as compared to antigen-based tests. Here we ... ...

Abstract	Standard SARS-CoV-2 testing protocols using nasopharyngeal/throat (NP/T) swabs are invasive and require trained medical staff for reliable sampling. In addition, it has been shown that PCR is more sensitive as compared to antigen-based tests. Here we describe the analytical and clinical evaluation of our in-house RNA extraction-free saliva-based molecular assay for the detection of SARS-CoV-2. Analytical sensitivity of the test was equal to the sensitivity obtained in other Dutch diagnostic laboratories that process NP/T swabs. In this study, 955 individuals participated and provided NP/T swabs for routine molecular analysis (with RNA extraction) and saliva for comparison. Our RT-qPCR resulted in a sensitivity of 82,86% and a specificity of 98,94% compared to the gold standard. A false-negative ratio of 1,9% was found. The SARS-CoV-2 detection workflow described here enables easy, economical, and reliable saliva processing, useful for repeated testing of individuals.
MeSH term(s)	COVID-19/diagnosis ; COVID-19 Testing ; Humans ; Nasopharynx ; RNA ; RNA, Viral/genetics ; SARS-CoV-2/genetics ; Saliva ; Sensitivity and Specificity ; Specimen Handling/methods
Chemical Substances	RNA, Viral ; RNA (63231-63-0)
Language	English
Publishing date	2022-05-05
Publishing country	United States
Document type	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.0268082
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Glow-in-the-Dark Infectious Disease Diagnostics Using CRISPR-Cas9-Based Split Luciferase Complementation.

van der Veer, Harmen J / van Aalen, Eva A / Michielsen, Claire M S / Hanckmann, Eva T L / Deckers, Jeroen / van Borren, Marcel M G J / Flipse, Jacky / Loonen, Anne J M / Schoeber, Joost P H / Merkx, Maarten

ACS central science

2023 Volume 9, Issue 4, Page(s) 657–667

Abstract: Nucleic acid detection methods based on CRISPR and isothermal amplification techniques show great potential for point-of-care diagnostic applications. However, most current methods rely on fluorescent or lateral flow assay readout, requiring external ... ...

Abstract	Nucleic acid detection methods based on CRISPR and isothermal amplification techniques show great potential for point-of-care diagnostic applications. However, most current methods rely on fluorescent or lateral flow assay readout, requiring external excitation or postamplification reaction transfer. Here, we developed a bioluminescent nucleic acid sensor (LUNAS) platform in which target dsDNA is sequence-specifically detected by a pair of dCas9-based probes mediating split NanoLuc luciferase complementation. LUNAS is easily integrated with recombinase polymerase amplification (RPA), providing attomolar sensitivity in a rapid one-pot assay. A calibrator luciferase is included for a robust ratiometric readout, enabling real-time monitoring of the RPA reaction using a simple digital camera. We designed an RT-RPA-LUNAS assay that allows SARS-CoV-2 RNA detection without the need for cumbersome RNA isolation and demonstrated its diagnostic performance for COVID-19 patient nasopharyngeal swab samples. Detection of SARS-CoV-2 from samples with viral RNA loads of ∼200 cp/μL was achieved within ∼20 min, showing that RPA-LUNAS is attractive for point-of-care infectious disease testing.
Language	English
Publishing date	2023-03-15
Publishing country	United States
Document type	Journal Article
ISSN	2374-7943
ISSN	2374-7943
DOI	10.1021/acscentsci.2c01467
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Article ; Online: Comprehensive analytical and clinical evaluation of a RNA extraction-free saliva-based molecular assay for SARS-CoV-2.

Joost P H Schoeber / Juliëtte M Schlaghecke / Britt M J Meuwissen / Mara van Heertum / Adriaan J C van den Brule / Anne J M Loonen

PLoS ONE, Vol 17, Iss 5, p e

2022 Volume 0268082

Abstract	Standard SARS-CoV-2 testing protocols using nasopharyngeal/throat (NP/T) swabs are invasive and require trained medical staff for reliable sampling. In addition, it has been shown that PCR is more sensitive as compared to antigen-based tests. Here we describe the analytical and clinical evaluation of our in-house RNA extraction-free saliva-based molecular assay for the detection of SARS-CoV-2. Analytical sensitivity of the test was equal to the sensitivity obtained in other Dutch diagnostic laboratories that process NP/T swabs. In this study, 955 individuals participated and provided NP/T swabs for routine molecular analysis (with RNA extraction) and saliva for comparison. Our RT-qPCR resulted in a sensitivity of 82,86% and a specificity of 98,94% compared to the gold standard. A false-negative ratio of 1,9% was found. The SARS-CoV-2 detection workflow described here enables easy, economical, and reliable saliva processing, useful for repeated testing of individuals.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2022-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Fast bioluminescent nucleic acid detection using one-pot isothermal amplification and dCas9-based split luciferase complementation

van der Veer, Harm J / van Aalen, Eva A / Michielsen, Claire M.S. / Hanckmann, Eva T.L. / Deckers, Jeroen / van Borren, Marcel M.G.J. / Flipse, Jacky / Loonen, Anne J.M. / Schoeber, Joost P.H. / Merkx, Maarten

bioRxiv

Abstract: Nucleic acid detection methods based on isothermal amplification techniques show great potential for point-of-care diagnostic applications. However, most current methods rely on fluorescent or lateral flow assay readout, requiring external excitation or ... ...

Abstract	Nucleic acid detection methods based on isothermal amplification techniques show great potential for point-of-care diagnostic applications. However, most current methods rely on fluorescent or lateral flow assay readout, requiring external excitation or post-amplification reaction transfer. Here, we developed a bioluminescent nucleic acid sensor (LUNAS) platform in which target dsDNA is sequence-specifically detected by a pair of dCas9-based probes mediating split NanoLuc luciferase complementation. Whereas LUNAS itself features a detection limit of ~1 pM for dsDNA targets, the LUNAS platform is easily integrated with recombinase polymerase amplification (RPA), providing attomolar sensitivity in a single-pot assay. We designed a one-pot RT-RPA-LUNAS assay for detecting SARS-CoV-2 RNA without the need for RNA isolation and demonstrated the diagnostic performance for COVID-19 patient nasopharyngeal swab samples using a digital camera to record the ratiometric signal. Detection of SARS-CoV-2 from samples with viral RNA loads of ~200 cp/microL was achieved within ~20 minutes, showing that RPA-LUNAS is attractive for point-of-care diagnostic applications.
Keywords	covid19
Language	English
Publishing date	2022-09-15
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2022.09.12.507659
Database	COVID19

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Article: Conditional fast expression and function of multimeric TRPV5 channels using Shield-1.

Schoeber, Joost P H / van de Graaf, Stan F J / Lee, Kyu Pil / Wittgen, Hanneke G M / Hoenderop, Joost G J / Bindels, René J M

American journal of physiology. Renal physiology

2009 Volume 296, Issue 1, Page(s) F204–11

Abstract: A recently described novel controllable method to regulate protein expression is based on a mutated FK506-binding protein-12 (mtFKBP) that is unstable and rapidly degraded in mammalian cells. This instability can be conferred to other proteins directly ... ...

Abstract	A recently described novel controllable method to regulate protein expression is based on a mutated FK506-binding protein-12 (mtFKBP) that is unstable and rapidly degraded in mammalian cells. This instability can be conferred to other proteins directly fused to mtFKBP. Binding of a synthetic cell-permeant ligand (Shield-1) to mtFKBP reverses the instability, allowing conditional expression of mtFKBP-fused proteins. We adapted this strategy to study multimeric plasma membrane proteins using the ion channel TRPV5 as model protein. mtFKBP-TRPV5 forms functional ion channels and its expression can be controlled in a time- and dose-dependent fashion using Shield-1. Moreover, in the presence of Shield-1, mtFKBP-TRPV5 formed heteromultimeric channels with untagged TRPV5, which were codegraded upon washout of Shield-1, providing a strategy to study multimeric plasma membrane protein complexes without the need to destabilize all individual subunits.
MeSH term(s)	Calcium Channels/genetics ; Calcium Channels/metabolism ; Cell Line ; Cell Membrane/metabolism ; Gene Expression Regulation/physiology ; Humans ; Kidney/cytology ; Kidney/embryology ; Kidney/metabolism ; Ligands ; Protein Engineering/methods ; Protein Multimerization ; Protein Structure, Tertiary ; Small Molecule Libraries/metabolism ; TRPV Cation Channels/genetics ; TRPV Cation Channels/metabolism ; Tacrolimus Binding Protein 1A/metabolism
Chemical Substances	Calcium Channels ; Ligands ; Small Molecule Libraries ; TRPV Cation Channels ; TRPV5 protein, human ; TRPV6 protein, human ; Tacrolimus Binding Protein 1A (EC 5.2.1.-)
Language	English
Publishing date	2009-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603837-2
ISSN	1522-1466 ; 1931-857X ; 0363-6127
ISSN (online)	1522-1466
ISSN	1931-857X ; 0363-6127
DOI	10.1152/ajprenal.90473.2008
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Article ; Online: Activation of the Ca2+-sensing receptor stimulates the activity of the epithelial Ca2+ channel TRPV5.

Topala, Catalin N / Schoeber, Joost P H / Searchfield, Lydia E / Riccardi, Daniela / Hoenderop, Joost G J / Bindels, René J M

Cell calcium

2009 Volume 45, Issue 4, Page(s) 331–339

Abstract: The extracellular Ca(2+)-sensing receptor (CaR) is a key-player in plasma Ca(2+) homeostasis. It is essentially expressed in the parathyroid glands and along the kidney nephron. The distal convoluted tubules (DCT) and connecting tubules (CNT) in the ... ...

Abstract	The extracellular Ca(2+)-sensing receptor (CaR) is a key-player in plasma Ca(2+) homeostasis. It is essentially expressed in the parathyroid glands and along the kidney nephron. The distal convoluted tubules (DCT) and connecting tubules (CNT) in the kidney are involved in active Ca(2+) reabsorption, but the function of the CaR has remained unclear in these segments. Here, the Ca(2+)-selective Transient Receptor Potential Vanilloid-subtype 5 channel (TRPV5) determines active Ca(2+) reabsorption by forming the apical entry gate. In this study we show that the CaR and TRPV5 co-localize at the luminal membrane of DCT/CNT. Furthermore, by patch-clamp and Fura-2-ratiometric measurements we demonstrate that activation of the CaR leads to elevated TRPV5-mediated currents and increases intracellular Ca(2+) concentrations in cells co-expressing TRPV5 and CaR. Activation of CaR initiated a signaling cascade that activated phorbol-12-myristate-13-acetate (PMA)-insensitive protein kinase C (PKC) isoforms. Importantly, mutation of two putative PKC phosphorylation sites, S299 and S654, in TRPV5 prevented the stimulatory effect of CaR activation on channel activity, as did a dominant negative CaR construct, CaR(R185Q). Interestingly, the activity of TRPV6, TRPV5' closest homologue, was not affected by the activated CaR. We conclude that activation of the CaR stimulates TRPV5-mediated Ca(2+) influx via a PMA-insensitive PKC isoform pathway.
MeSH term(s)	Animals ; Cell Membrane/drug effects ; Cell Membrane/metabolism ; Cell Polarity/drug effects ; Epithelial Cells/cytology ; Epithelial Cells/drug effects ; Epithelial Cells/enzymology ; Epithelial Cells/metabolism ; Humans ; Ion Channel Gating ; Isoenzymes/metabolism ; Kidney Tubules, Distal/cytology ; Kidney Tubules, Distal/drug effects ; Kidney Tubules, Distal/metabolism ; Mice ; Mutant Proteins/metabolism ; Phosphorylation/drug effects ; Protein Kinase C/metabolism ; Protein Transport/drug effects ; Rabbits ; Receptors, Calcium-Sensing/metabolism ; Signal Transduction/drug effects ; TRPV Cation Channels/metabolism ; Tetradecanoylphorbol Acetate/pharmacology
Chemical Substances	Isoenzymes ; Mutant Proteins ; Receptors, Calcium-Sensing ; TRPV Cation Channels ; TRPV5 protein, human ; Protein Kinase C (EC 2.7.11.13) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
Language	English
Publishing date	2009-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/j.ceca.2008.12.003
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Zs.A 1596: Show issues

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Article ; Online: Testosterone increases urinary calcium excretion and inhibits expression of renal calcium transport proteins.

Hsu, Yu-Juei / Dimke, Henrik / Schoeber, Joost P H / Hsu, Shih-Che / Lin, Shih-Hua / Chu, Pauling / Hoenderop, Joost G J / Bindels, René J M

Kidney international

2010 Volume 77, Issue 7, Page(s) 601–608

Abstract: Although gender differences in the renal handling of calcium have been reported, the overall contribution of androgens to these differences remains uncertain. We determined here whether testosterone affects active renal calcium reabsorption by regulating ...

Abstract	Although gender differences in the renal handling of calcium have been reported, the overall contribution of androgens to these differences remains uncertain. We determined here whether testosterone affects active renal calcium reabsorption by regulating calcium transport proteins. Male mice had higher urinary calcium excretion than female mice and their renal calcium transporters were expressed at a lower level. We also found that orchidectomized mice excreted less calcium in their urine than sham-operated control mice and that the hypocalciuria was normalized after testosterone replacement. Androgen deficiency increased the abundance of the renal mRNA and protein of both the luminal transient receptor potential vanilloid-subtype 5 (TRPV5) and intracellular calbindin-D(28K) transporters, which in turn were suppressed by testosterone treatment. There were no significant differences in serum estrogen, parathyroid hormone, or 1,25-dihydroxyvitamin D3 levels between control and orchidectomized mice with or without testosterone. Moreover, incubation of primary rabbit connecting tubule and cortical collecting duct cells with a nonaromatizable androgen, dihydrotestosterone, reduced transcellular calcium transport. Thus, our study shows that gender differences in renal calcium handling are, in part, mediated by the inhibitory actions of androgens on TRPV5-mediated active renal calcium transport.
MeSH term(s)	Androgens/metabolism ; Animals ; Calbindins ; Calcium/urine ; Calcium Channels/metabolism ; Cells, Cultured ; Dihydrotestosterone ; Female ; Kidney/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Orchiectomy ; Plasma Membrane Calcium-Transporting ATPases/metabolism ; Rabbits ; Receptors, Androgen/metabolism ; S100 Calcium Binding Protein G/metabolism ; Sex Characteristics ; Sodium-Calcium Exchanger/metabolism ; TRPV Cation Channels/metabolism ; Testosterone/metabolism
Chemical Substances	Androgens ; Calbindins ; Calcium Channels ; NCX1 protein, mouse ; Receptors, Androgen ; S100 Calcium Binding Protein G ; Sodium-Calcium Exchanger ; TRPV Cation Channels ; Trpv5 protein, mouse ; Dihydrotestosterone (08J2K08A3Y) ; Testosterone (3XMK78S47O) ; Plasma Membrane Calcium-Transporting ATPases (EC 3.6.3.8) ; Atp2b1 protein, mouse (EC 7.2.2.10) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2010-01-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120573-0
ISSN	1523-1755 ; 0085-2538
ISSN (online)	1523-1755
ISSN	0085-2538
DOI	10.1038/ki.2009.522
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Zs.A 797: Show issues

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Article ; Online: Intracellular signal transduction by the extracellular calcium-sensing receptor of Xenopus melanotrope cells.

van den Hurk, Maarten J J / Cruijsen, Peter M J M / Schoeber, Joost P H / Scheenen, Wim J J M / Roubos, Eric W / Jenks, Bruce G

General and comparative endocrinology

2008 Volume 157, Issue 2, Page(s) 156–164

Abstract: The extracellular calcium-sensing receptor (CaR) is expressed in various types of endocrine pituitary cell, but the intracellular mechanism this G protein-coupled receptor uses in these cells is not known. In the present study we investigated possible ... ...

Abstract	The extracellular calcium-sensing receptor (CaR) is expressed in various types of endocrine pituitary cell, but the intracellular mechanism this G protein-coupled receptor uses in these cells is not known. In the present study we investigated possible intracellular signal transduction pathway(s) utilized by the CaR of the endocrine melanotrope cells in the intermediate pituitary lobe of the South African-clawed toad Xenopus laevis. For this purpose, the effects of various pharmacological agents on CaR-evoked secretion of radiolabeled secretory peptides from cultured melanotrope cells were assessed. CaR-evoked secretion, induced by the potent CaR agonist L-phenylalanine (L-Phe), could not be inhibited by cholera toxin, nor by NPC-15437 and PMA, indicating that neither G(s)/PKA nor G(q)/PKC pathways are involved. However, pertussis toxin (G(i/o) protein inhibitor), genistein (inhibitor of PTKs), wortmannin/LY-294002 (PI3-K inhibitor) and U-0126 (inhibitor of extracellular signal-regulated kinase, ERK) all substantially inhibited CaR-evoked secretion, indicating that the Xenopus melanotrope cell possesses a PI3-K/MAPK system that plays some role in CaR-signaling. Since no direct effect of L-Phe on ERK phosphorylation could be shown it is concluded that CaR must act primarily through another, still unknown, signaling pathway in Xenopus melanotropes. Our results indicate that the PI3-K/MAPK system has a facilitating effect on CaR-induced secretion, possibly by sensitizing the CaR.
MeSH term(s)	Androstadienes/pharmacology ; Animals ; Blotting, Western ; Butadienes/pharmacology ; Cells, Cultured ; Cholera Toxin/pharmacology ; Cyclic AMP/metabolism ; GTP-Binding Protein alpha Subunits, Gi-Go/analysis ; GTP-Binding Protein alpha Subunits, Gi-Go/metabolism ; GTP-Binding Protein alpha Subunits, Gs/antagonists & inhibitors ; GTP-Binding Protein alpha Subunits, Gs/metabolism ; Genistein/pharmacology ; Intracellular Space/drug effects ; Intracellular Space/metabolism ; Intracellular Space/physiology ; Mitogen-Activated Protein Kinases/antagonists & inhibitors ; Mitogen-Activated Protein Kinases/metabolism ; Nitriles/pharmacology ; Pertussis Toxin/pharmacology ; Phenylalanine/pharmacology ; Phosphatidylinositol 3-Kinases/antagonists & inhibitors ; Phosphatidylinositol 3-Kinases/metabolism ; Piperidines/pharmacology ; Radioimmunoassay ; Receptors, Calcium-Sensing/antagonists & inhibitors ; Receptors, Calcium-Sensing/metabolism ; Signal Transduction/drug effects ; Signal Transduction/physiology ; Xenopus laevis/metabolism
Chemical Substances	Androstadienes ; Butadienes ; Nitriles ; Piperidines ; Receptors, Calcium-Sensing ; U 0126 ; NPC 15437 (136449-85-9) ; Phenylalanine (47E5O17Y3R) ; Cholera Toxin (9012-63-9) ; Genistein (DH2M523P0H) ; Cyclic AMP (E0399OZS9N) ; Pertussis Toxin (EC 2.4.2.31) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; GTP-Binding Protein alpha Subunits, Gi-Go (EC 3.6.5.1) ; GTP-Binding Protein alpha Subunits, Gs (EC 3.6.5.1) ; wortmannin (XVA4O219QW)
Language	English
Publishing date	2008-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	1851-x
ISSN	1095-6840 ; 0016-6480
ISSN (online)	1095-6840
ISSN	0016-6480
DOI	10.1016/j.ygcen.2008.04.005
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Article: Identification of Nipsnap1 as a novel auxiliary protein inhibiting TRPV6 activity.

Schoeber, Joost P H / Topala, Catalin N / Lee, Kyu Pil / Lambers, Tim T / Ricard, Guénola / van der Kemp, Annemiete W C M / Huynen, Martijn A / Hoenderop, Joost G J / Bindels, René J M

Pflugers Archiv : European journal of physiology

2008 Volume 457, Issue 1, Page(s) 91–101

Abstract: The transient receptor potential vanilloid channels 5 and 6 (TRPV5/6) are the most Ca(2+)-selective channels within the TRP superfamily of ion channels. These epithelial Ca(2+) channels are regulated at different intra- and extracellular sites by the ... ...

Abstract	The transient receptor potential vanilloid channels 5 and 6 (TRPV5/6) are the most Ca(2+)-selective channels within the TRP superfamily of ion channels. These epithelial Ca(2+) channels are regulated at different intra- and extracellular sites by the feedback response of Ca(2+) itself, calciotropic hormones, and by TRPV5/6-associated proteins. In the present study, bioinformatics was used to search for novel TRPV5/6-associated genes. By including pull-down assays and functional analysis, Nipsnap1-a hitherto functionally uncharacterized globular protein-was identified as a novel factor involved in the regulation of TRPV6. Electrophysiological recordings revealed that Nipsnap1 abolishes TRPV6 currents. Subsequent biotinylation assays showed that TRPV6 plasma membrane expression did not change in the presence of Nipsnap1, suggesting that TRPV6 inhibition by Nipsnap1 is independently regulated from reduced cell surface channel expression. In addition, semi-quantitative reverse transcriptase PCR and immunohistochemical labeling of Nipsnap1 indicated that Nipsnap1 is expressed in mouse intestinal tissues-where TRPV6 is predominantly expressed-but that it does not co-localize with TRPV5 in the kidney. In conclusion, this study presents the first physiological function of Nipsnap1 as an associated protein inhibiting TRPV6 activity that possibly exerts its effect directly at the plasma membrane.
MeSH term(s)	Amino Acid Sequence ; Calcium Channels/genetics ; Calcium Channels/physiology ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Cells, Cultured ; Computational Biology ; Electrophysiology ; Humans ; Immunohistochemistry ; Intercellular Signaling Peptides and Proteins ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Patch-Clamp Techniques ; Protein Binding ; Proteins/genetics ; Proteins/physiology ; Reverse Transcriptase Polymerase Chain Reaction ; TRPV Cation Channels/genetics ; TRPV Cation Channels/physiology ; Tissue Distribution
Chemical Substances	Calcium Channels ; Intercellular Signaling Peptides and Proteins ; Membrane Proteins ; NIPSNAP1 protein, human ; Proteins ; TRPV Cation Channels ; TRPV5 protein, human ; TRPV6 protein, human
Language	English
Publishing date	2008-04-08
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	6380-0
ISSN	1432-2013 ; 0031-6768
ISSN (online)	1432-2013
ISSN	0031-6768
DOI	10.1007/s00424-008-0494-5
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Article ; Online: Deficiency of either P-glycoprotein or breast cancer resistance protein protect against acute kidney injury.

Huls, Miriam / Schoeber, Joost P H / Verfaillie, Catherine M / Luttun, Aernout / Ulloa-Montoya, Fernando / Menke, Aswin L / van Bolderen, Lars R / Woestenenk, Rob M / Merkx, Gerard F M / Wetzels, Jack F M / Russel, Frans G M / Masereeuw, Rosalinde

publication RETRACTED

Cell transplantation

2010 Volume 19, Issue 9, Page(s) 1195–1208

Abstract: ... of which involves bone marrow-derived (stem) cells. The ATP binding cassette transporters, P-glycoprotein and breast ... was reconstituted by bone marrow from wild-type, P-glycoprotein- or breast cancer resistance protein ...

Abstract	The kidney has a high capacity to regenerate after ischemic injury via several mechanisms, one of which involves bone marrow-derived (stem) cells. The ATP binding cassette transporters, P-glycoprotein and breast cancer resistance protein, are determinants for the enriched stem and progenitor cell fraction in bone marrow. Because they are upregulated after acute kidney injury, we hypothesized that both efflux pumps may play a role in protecting against renal injury. Surprisingly, transporter-deficient mice were protected against ischemia-induced renal injury. To further study this, bone marrow from irradiated wild-type mice was reconstituted by bone marrow from wild-type, P-glycoprotein- or breast cancer resistance protein-deficient mice. Four weeks later, kidney injury was induced and its function evaluated. Significantly more bone marrow-derived cells were detected in kidneys grafted with transporter-deficient bone marrow. A gender mismatch study suggested that cell fusion of resident tubular cells with bone marrow cells was unlikely. Renal function analyses indicated an absence of renal damage following ischemia-reperfusion in animals transplanted with transporter-deficient bone marrow. When wild-type bone marrow was transplanted in breast cancer resistance protein-deficient mice this protection is lost. Furthermore, we demonstrate that transporter-deficient bone marrow contained significantly more monocytes, granulocytes, and early outgrowth endothelial progenitor cells.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily B, Member 1/deficiency ; ATP Binding Cassette Transporter, Subfamily B, Member 1/metabolism ; ATP Binding Cassette Transporter, Subfamily G, Member 2 ; ATP-Binding Cassette Transporters/metabolism ; Acute Kidney Injury/blood ; Acute Kidney Injury/metabolism ; Acute Kidney Injury/urine ; Animals ; Bone Marrow Cells/metabolism ; Bone Marrow Transplantation ; Female ; Humans ; Ischemia/metabolism ; Kidney/blood supply ; Kidney/metabolism ; Kidney Function Tests ; Mice ; Mice, Knockout ; Reperfusion Injury/metabolism ; Transduction, Genetic
Chemical Substances	ATP Binding Cassette Transporter, Subfamily B, Member 1 ; ATP Binding Cassette Transporter, Subfamily G, Member 2 ; ATP-Binding Cassette Transporters ; Abcg2 protein, mouse
Language	English
Publishing date	2010-05-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Retracted Publication
ZDB-ID	1135816-6
ISSN	1555-3892 ; 0963-6897
ISSN (online)	1555-3892
ISSN	0963-6897
DOI	10.3727/096368910X504478
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Inter-library loan at ZB MED

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Inter-library loan at ZB MED

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Cologne/Königswinter

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Full text online

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Cologne/Königswinter

Order via subito