LIVIVO - Suchergebnisse -

Suchergebnis

Treffer 1 - 10 von insgesamt 13

Suchoptionen

Artikel ; Online: Relevance of VEGF and nephrin expression in glomerular diseases.

Bertuccio, Claudia A

2011 Band 2011, Seite(n) 718609

Abstract: The glomerular filtration barrier is affected in a large number of acquired and inherited diseases resulting in extensive leakage of plasma albumin and larger proteins, leading to nephrotic syndrome and end-stage renal disease. Unfortunately, the ... ...

Abstract	The glomerular filtration barrier is affected in a large number of acquired and inherited diseases resulting in extensive leakage of plasma albumin and larger proteins, leading to nephrotic syndrome and end-stage renal disease. Unfortunately, the molecular mechanisms governing the development of the nephrotic syndrome remain poorly understood. Here, I give an overview of recent investigations that have focused on characterizing the interrelationships between the slit diaphragm components and podocytes-secreted VEGF, which have a significant role for maintaining the normal podocyte structure and the integrity of the filtering barrier.
Sprache	Englisch
Erscheinungsdatum	2011-07-26
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	2582328-0
ISSN	2090-1747 ; 2090-1739
ISSN (online)	2090-1747
ISSN	2090-1739
DOI	10.1155/2011/718609
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Zusatzmaterialien

Über subito bestellen

Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

Details ▾
- Kostenpflichtig bestellen

Artikel: Polycystin-1C terminus cleavage and its relation with polycystin-2, two proteins involved in polycystic kidney disease.

Bertuccio, Claudia A / Caplan, Michael J

Medicina

2013 Band 73, Heft 2, Seite(n) 155–162

Abstract: Autosomal dominant polycystic kidney disease (ADPKD), a most common genetic cause of chronic renal failure, is characterized by the progressive development and enlargement of cysts in kidneys and other organs. The cystogenic process is highly complex and ...

Abstract	Autosomal dominant polycystic kidney disease (ADPKD), a most common genetic cause of chronic renal failure, is characterized by the progressive development and enlargement of cysts in kidneys and other organs. The cystogenic process is highly complex and involves a high proliferative rate, increased apoptosis, altered protein sorting, changed secretory characteristics, and disorganization of the extracellular matrix. ADPKD is caused by mutations in the genes encoding polycystin-1 (PC-1) or polycystin-2 (PC-2). PC-1 undergoes multiple cleavages that intervene in several signaling pathways involved in cellular proliferation and differentiation mechanisms. One of these cleavages releases the cytoplasmic C-terminal tail of PC-1. In addition, the C-terminal cytoplasmic tails of PC-1 and PC-2 interact in vitro and in vivo. The purpose of this review is to summarize recent literature that suggests that PC-1 and PC-2 may function through a common signaling pathway necessary for normal tubulogenesis. We hope that a better understanding of PC-1 and PC-2 protein function will lead to progress in diagnosis and treatment for ADPKD.
Mesh-Begriff(e)	Animals ; Apoptosis/physiology ; Calcium Channels/metabolism ; Cell Nucleus/metabolism ; Cell Proliferation ; Cyclic AMP/metabolism ; Humans ; Kidney Tubules/metabolism ; Mutation ; Polycystic Kidney, Autosomal Dominant/genetics ; Polycystic Kidney, Autosomal Dominant/metabolism ; TRPP Cation Channels/metabolism
Chemische Substanzen	Calcium Channels ; TRPP Cation Channels ; polycystic kidney disease 1 protein ; polycystic kidney disease 2 protein ; Cyclic AMP (E0399OZS9N)
Sprache	Englisch
Erscheinungsdatum	2013
Erscheinungsland	Argentina
Dokumenttyp	Journal Article ; Review
ZDB-ID	411586-7
ISSN	1669-9106 ; 0025-7680 ; 0325-951X
ISSN (online)	1669-9106
ISSN	0025-7680 ; 0325-951X
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Zusatzmaterialien

Verfügbar in ZB MED Köln/Königswinter

Zs.B 163: Hefte anzeigen

Standort:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Über subito bestellen

Details ▾
- Im ZB MED-Bestand
- Kostenpflichtig bestellen

Artikel ; Online: Histone deacetylase inhibitors (HDACi) increase expression of KCa2.3 (SK3) in primary microvascular endothelial cells.

Kolski-Andreaco, Aaron / Balut, Corina M / Bertuccio, Claudia A / Wilson, Annette S / Rivers, William M / Liu, Xiaoning / Gandley, Robin E / Straub, Adam C / Butterworth, Michael B / Binion, David / Devor, Daniel C

American journal of physiology. Cell physiology

2022 Band 322, Heft 3, Seite(n) C338–C353

Abstract: The small conductance calcium-activated potassium channel (KCa2.3) has long been recognized for its role in mediating vasorelaxation through the endothelium-derived hyperpolarization (EDH) response. Histone deacetylases (HDACs) have been implicated as ... ...

Abstract	The small conductance calcium-activated potassium channel (KCa2.3) has long been recognized for its role in mediating vasorelaxation through the endothelium-derived hyperpolarization (EDH) response. Histone deacetylases (HDACs) have been implicated as potential modulators of blood pressure and histone deacetylase inhibitors (HDACi) are being explored as therapeutics for hypertension. Herein, we show that HDACi increase KCa2.3 expression when heterologously expressed in HEK cells and endogenously expressed in primary cultures of human umbilical vein endothelial cells (HUVECs) and human intestinal microvascular endothelial cells (HIMECs). When primary endothelial cells were exposed to HDACi, KCa2.3 transcripts, subunits, and functional current are increased. Quantitative RT-PCR (qPCR) demonstrated increased KCa2.3 mRNA following HDACi, confirming transcriptional regulation of KCa2.3 by HDACs. By using pharmacological agents selective for different classes of HDACs, we discriminated between cytoplasmic and epigenetic modulation of KCa2.3. Biochemical analysis revealed an association between the cytoplasmic HDAC6 and KCa2.3 in immunoprecipitation studies. Specifically inhibiting HDAC6 increases expression of KCa2.3. In addition to increasing the expression of KCa2.3, we show that nonspecific inhibition of HDACs causes an increase in the expression of the molecular chaperone Hsp70 in endothelial cells. When Hsp70 is inhibited in the presence of HDACi, the magnitude of the increase in KCa2.3 expression is diminished. Finally, we show a slower rate of endocytosis of KCa2.3 as a result of exposure of primary endothelial cells to HDACi. These data provide the first demonstrated approach to increase KCa2.3 channel number in endothelial cells and may partially account for the mechanism by which HDACi induce vasorelaxation.
Mesh-Begriff(e)	Endocytosis ; Endothelial Cells/drug effects ; Endothelial Cells/enzymology ; HEK293 Cells ; HSP70 Heat-Shock Proteins/metabolism ; Histone Deacetylase 6/antagonists & inhibitors ; Histone Deacetylase 6/metabolism ; Histone Deacetylase Inhibitors/pharmacology ; Humans ; Intestines/blood supply ; Membrane Potentials ; Microvessels/drug effects ; Microvessels/enzymology ; Small-Conductance Calcium-Activated Potassium Channels/genetics ; Small-Conductance Calcium-Activated Potassium Channels/metabolism ; Up-Regulation ; Vasodilation
Chemische Substanzen	HSP70 Heat-Shock Proteins ; Histone Deacetylase Inhibitors ; KCNN3 protein, human ; Small-Conductance Calcium-Activated Potassium Channels ; HDAC6 protein, human (EC 3.5.1.98) ; Histone Deacetylase 6 (EC 3.5.1.98)
Sprache	Englisch
Erscheinungsdatum	2022-01-19
Erscheinungsland	United States
Dokumenttyp	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	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00409.2021
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Zusatzmaterialien

Verfügbar in ZB MED Köln/Königswinter

Uc I Zs.89: Hefte anzeigen

Standort:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Über subito bestellen

Details ▾
- Im ZB MED-Bestand
- Kostenpflichtig bestellen

Artikel ; Online: Plasma membrane insertion of KCa2.3 (SK3) is dependent upon the SNARE proteins, syntaxin-4 and SNAP23.

Bertuccio, Claudia A / Wang, Tony T / Hamilton, Kirk L / Rodriguez-Gil, Diego J / Condliffe, Steven B / Devor, Daniel C

PloS one

2018 Band 13, Heft 5, Seite(n) e0196717

Abstract: We previously demonstrated endocytosis of KCa2.3 is caveolin-1-, dynamin II- and Rab5-dependent. KCa2.3 then enters Rab35/EPI64C- and RME-1-containing recycling endosomes and is returned to the plasma membrane (PM). Herein, we report on the mechanism by ... ...

Abstract	We previously demonstrated endocytosis of KCa2.3 is caveolin-1-, dynamin II- and Rab5-dependent. KCa2.3 then enters Rab35/EPI64C- and RME-1-containing recycling endosomes and is returned to the plasma membrane (PM). Herein, we report on the mechanism by which KCa2.3 is inserted into the PM during recycling and following exit from the Golgi. We demonstrate KCa2.3 colocalizes with SNAP-23 and Syntaxin-4 in the PM of HEK and endothelial cells by confocal immunofluorescence microscopy. We further show KCa2.3 can be co-immunoprecipitated with SNAP-23 and Syntaxin-4. Overexpression of either Syntaxin-4 or SNAP-23 increased PM expression of KCa2.3, whereas shRNA-mediated knockdown of these SNARE proteins significantly decreased PM KCa2.3 expression, as assessed by cell surface biotinylation. Whole-cell patch clamp studies confirmed knockdown of SNAP-23 significantly decreased the apamin sensitive, KCa2.3 current. Using standard biotinylation/stripping methods, we demonstrate shRNA mediated knockdown of SNAP-23 inhibits recycling of KCa2.3 following endocytosis, whereas scrambled shRNA had no effect. Finally, using biotin ligase acceptor peptide (BLAP)-tagged KCa2.3, coupled with ER-resident biotin ligase (BirA), channels could be biotinylated in the ER after which we evaluated their rate of insertion into the PM following Golgi exit. We demonstrate knockdown of SNAP-23 significantly slows the rate of Golgi to PM delivery of KCa2.3. The inhibition of both recycling and PM delivery of newly synthesized KCa2.3 channels likely accounts for the decreased PM expression observed following knockdown of these SNARE proteins. In total, our results suggest insertion of KCa2.3 into the PM depends upon the SNARE proteins, Syntaxin-4 and SNAP-23.
Mesh-Begriff(e)	Cell Membrane/metabolism ; Golgi Apparatus/metabolism ; HEK293 Cells ; Humans ; Microscopy, Confocal ; Qa-SNARE Proteins/metabolism ; Qb-SNARE Proteins/metabolism ; Qc-SNARE Proteins/metabolism ; RNA, Small Interfering/metabolism ; Small-Conductance Calcium-Activated Potassium Channels/metabolism
Chemische Substanzen	KCNN3 protein, human ; Qa-SNARE Proteins ; Qb-SNARE Proteins ; Qc-SNARE Proteins ; RNA, Small Interfering ; SNAP23 protein, human ; Small-Conductance Calcium-Activated Potassium Channels ; syntaxin 4, human
Sprache	Englisch
Erscheinungsdatum	2018-05-16
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0196717
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Zusatzmaterialien

Über subito bestellen

Fernleihe an ZB MED

Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

Details ▾
- Kostenpflichtig bestellen

Artikel ; Online: Polycystin-1 cleavage and the regulation of transcriptional pathways.

Merrick, David / Bertuccio, Claudia A / Chapin, Hannah C / Lal, Mark / Chauvet, Veronique / Caplan, Michael J

Pediatric nephrology (Berlin, Germany)

2013 Band 29, Heft 4, Seite(n) 505–511

Abstract: Autosomal dominant polycystic kidney disease (ADPKD) is the most common genetic cause of end-stage renal disease, affecting approximately 1 in 1,000 people. The disease is characterized by the development of numerous large fluid-filled renal cysts over ... ...

Abstract	Autosomal dominant polycystic kidney disease (ADPKD) is the most common genetic cause of end-stage renal disease, affecting approximately 1 in 1,000 people. The disease is characterized by the development of numerous large fluid-filled renal cysts over the course of decades. These cysts compress the surrounding renal parenchyma and impair its function. Mutations in two genes are responsible for ADPKD. The protein products of both of these genes, polycystin-1 and polycystin-2, localize to the primary cilium and participate in a wide variety of signaling pathways. Polycystin-1 undergoes several proteolytic cleavages that produce fragments which manifest biological activities. Recent results suggest that the production of polycystin-1 cleavage fragments is necessary and sufficient to account for at least some, although certainly not all, of the physiological functions of the parent protein.
Mesh-Begriff(e)	Animals ; Gene Expression Regulation/physiology ; Humans ; Mutation ; Polycystic Kidney, Autosomal Dominant/genetics ; Polycystic Kidney, Autosomal Dominant/metabolism ; TRPP Cation Channels/genetics ; TRPP Cation Channels/metabolism ; Transcription, Genetic
Chemische Substanzen	TRPP Cation Channels ; polycystic kidney disease 1 protein
Sprache	Englisch
Erscheinungsdatum	2013-07-04
Erscheinungsland	Germany
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	631932-4
ISSN	1432-198X ; 0931-041X
ISSN (online)	1432-198X
ISSN	0931-041X
DOI	10.1007/s00467-013-2548-y
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Volltext online

Zugriff für angemeldete ZB MED Nutzerinnen und Nutzer

Zusatzmaterialien

Verfügbar in ZB MED Köln/Königswinter

Zs.A 2196: Hefte anzeigen

Standort:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Über subito bestellen

Details ▾

Artikel ; Online: Dynamin- and Rab5-dependent endocytosis of a Ca2+ -activated K+ channel, KCa2.3.

Gao, Yajuan / Bertuccio, Claudia A / Balut, Corina M / Watkins, Simon C / Devor, Daniel C

PloS one

2012 Band 7, Heft 8, Seite(n) e44150

Abstract: Regulation of the number of ion channels at the plasma membrane is a critical component of the physiological response. We recently demonstrated that the Ca(2+)-activated K(+) channel, KCa2.3 is rapidly endocytosed and enters a Rab35- and EPI64C-dependent ...

Abstract	Regulation of the number of ion channels at the plasma membrane is a critical component of the physiological response. We recently demonstrated that the Ca(2+)-activated K(+) channel, KCa2.3 is rapidly endocytosed and enters a Rab35- and EPI64C-dependent recycling compartment. Herein, we addressed the early endocytic steps of KCa2.3 using a combination of fluorescence and biotinylation techniques. We demonstrate that KCa2.3 is localized to caveolin-rich domains of the plasma membrane using fluorescence co-localization, transmission electron microscopy and co-immunoprecipitation (co-IP). Further, in cells lacking caveolin-1, we observed an accumulation of KCa2.3 at the plasma membrane as well as a decreased rate of endocytosis, as assessed by biotinylation. We also demonstrate that KCa2.3 and dynamin II are co-localized following endocytosis as well as demonstrating they are associated by co-IP. Further, expression of K44A dynamin II resulted in a 2-fold increase in plasma membrane KCa2.3 as well as a 3-fold inhibition of endocytosis. Finally, we evaluated the role of Rab5 in the endocytosis of KCa2.3. We demonstrate that expression of a dominant active Rab5 (Q79L) results in the accumulation of newly endocytosed KCa2.3 on to the membrane of the Rab5-induced vacuoles. We confirmed this co-localization by co-IP; demonstrating that KCa2.3 and Rab5 are associated. As expected, if Rab5 is required for the endocytosis of KCa2.3, expression of a dominant negative Rab5 (S34N) resulted in an approximate 2-fold accumulation of KCa2.3 at the plasma membrane. This was confirmed by siRNA-mediated knockdown of Rab5. Expression of the dominant negative Rab5 also resulted in a decreased rate of KCa2.3 endocytosis. These results demonstrate that KCa2.3 is localized to a caveolin-rich domain within the plasma membrane and is endocytosed in a dynamin- and Rab5-dependent manner prior to entering the Rab35/EPI64C recycling compartment and returning to the plasma membrane.
Mesh-Begriff(e)	Animals ; Caveolae/drug effects ; Caveolae/metabolism ; Caveolae/ultrastructure ; Dynamins/metabolism ; Endocytosis ; Endosomes/metabolism ; Endosomes/ultrastructure ; HEK293 Cells ; Humans ; Membrane Microdomains/drug effects ; Membrane Microdomains/metabolism ; Mice ; Models, Biological ; Potassium Channels, Calcium-Activated/metabolism ; Potassium Channels, Calcium-Activated/ultrastructure ; Protein Transport ; rab5 GTP-Binding Proteins/metabolism
Chemische Substanzen	Potassium Channels, Calcium-Activated ; rab5 GTP-Binding Proteins (EC 3.6.5.2) ; Dynamins (EC 3.6.5.5)
Sprache	Englisch
Erscheinungsdatum	2012-08-28
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0044150
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Zusatzmaterialien

Über subito bestellen

Fernleihe an ZB MED

Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

Details ▾
- Kostenpflichtig bestellen

Artikel ; Online: Anterograde trafficking of KCa3.1 in polarized epithelia is Rab1- and Rab8-dependent and recycling endosome-independent.

Bertuccio, Claudia A / Lee, Shih-Liang / Wu, Guangyu / Butterworth, Michael B / Hamilton, Kirk L / Devor, Daniel C

PloS one

2014 Band 9, Heft 3, Seite(n) e92013

Abstract: The intermediate conductance, Ca2+-activated K+ channel (KCa3.1) targets to the basolateral (BL) membrane in polarized epithelia where it plays a key role in transepithelial ion transport. However, there are no studies defining the anterograde and ... ...

Abstract	The intermediate conductance, Ca2+-activated K+ channel (KCa3.1) targets to the basolateral (BL) membrane in polarized epithelia where it plays a key role in transepithelial ion transport. However, there are no studies defining the anterograde and retrograde trafficking of KCa3.1 in polarized epithelia. Herein, we utilize Biotin Ligase Acceptor Peptide (BLAP)-tagged KCa3.1 to address these trafficking steps in polarized epithelia, using MDCK, Caco-2 and FRT cells. We demonstrate that KCa3.1 is exclusively targeted to the BL membrane in these cells when grown on filter supports. Following endocytosis, KCa3.1 degradation is prevented by inhibition of lysosomal/proteosomal pathways. Further, the ubiquitylation of KCa3.1 is increased following endocytosis from the BL membrane and PR-619, a deubiquitylase inhibitor, prevents degradation, indicating KCa3.1 is targeted for degradation by ubiquitylation. We demonstrate that KCa3.1 is targeted to the BL membrane in polarized LLC-PK1 cells which lack the μ1B subunit of the AP-1 complex, indicating BL targeting of KCa3.1 is independent of μ1B. As Rabs 1, 2, 6 and 8 play roles in ER/Golgi exit and trafficking of proteins to the BL membrane, we evaluated the role of these Rabs in the trafficking of KCa3.1. In the presence of dominant negative Rab1 or Rab8, KCa3.1 cell surface expression was significantly reduced, whereas Rabs 2 and 6 had no effect. We also co-immunoprecipitated KCa3.1 with both Rab1 and Rab8. These results suggest these Rabs are necessary for the anterograde trafficking of KCa3.1. Finally, we determined whether KCa3.1 traffics directly to the BL membrane or through recycling endosomes in MDCK cells. For these studies, we used either recycling endosome ablation or dominant negative RME-1 constructs and determined that KCa3.1 is trafficked directly to the BL membrane rather than via recycling endosomes. These results are the first to describe the anterograde and retrograde trafficking of KCa3.1 in polarized epithelia cells.
Mesh-Begriff(e)	Animals ; Cell Line ; Cell Membrane/metabolism ; Cell Polarity ; Dogs ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Golgi Apparatus/metabolism ; Humans ; Intermediate-Conductance Calcium-Activated Potassium Channels/metabolism ; Protein Transport ; Ubiquitination ; rab GTP-Binding Proteins/metabolism ; rab1 GTP-Binding Proteins/metabolism
Chemische Substanzen	Intermediate-Conductance Calcium-Activated Potassium Channels ; RAB8A protein, human (EC 3.6.1.-.) ; rab GTP-Binding Proteins (EC 3.6.5.2) ; rab1 GTP-Binding Proteins (EC 3.6.5.2)
Sprache	Englisch
Erscheinungsdatum	2014-03-14
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0092013
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Zusatzmaterialien

Über subito bestellen

Fernleihe an ZB MED

Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

Details ▾
- Kostenpflichtig bestellen

Artikel ; Online: Mechanisms of PKC-dependent Na+ K+ ATPase phosphorylation in the rat kidney with chronic renal failure.

Bertuccio, Claudia A / Arrizurieta, Elvira E / Ibarra, Fernando R / Martín, Rodolfo S

Renal failure

2007 Band 29, Heft 1, Seite(n) 13–22

Abstract: The present work was designed to study Na+ K+ ATPase alpha1-subunit phosphorylation in rats with chronic renal failure (CRF) in comparison with normal rats. Na+ K+ ATPase alpha1-subunit phosphorylation degree was measured by binding the McK-1 antibody to ...

Abstract	The present work was designed to study Na+ K+ ATPase alpha1-subunit phosphorylation in rats with chronic renal failure (CRF) in comparison with normal rats. Na+ K+ ATPase alpha1-subunit phosphorylation degree was measured by binding the McK-1 antibody to dephosphorylated Ser-23 in microdissected medullary thick ascending limb of Henle (mTAL) segments. In addition, the total Na+ K+ ATPase alpha1-subunit expression and activity were also measured in the outer renal medulla homogenates and membranes. CRF rats showed a higher Na+ K+ ATPase activity, as compared with control rats (18.95 +/- 2.4 vs. 11.21 +/- 1.5 micromol Pi/mg prot/h, p < 0.05), accompanied by a higher total Na+ K+ ATPase expression (0.54 +/- 0.04 vs. 0.27 +/- 0.02 normalized arbitrary units (NU), p < 0.05). When McK-1 antibody was used, a higher immunosignal in mTAL of CRF rats was observed, as compared with controls (6.3 +/- 0.35 vs. 4.1 +/- 0.33 NU, p < 0.05). The ratio Na+ K+ ATPase alpha1-subunit phosphorylation/total Na+ K+ ATPase alpha1-subunit expression per microg protein showed a non-significant difference between CRF and control rats in microdissected mTAL segments (2.11 +/- 0.12 vs. 2.26 +/- 0.18 NU, p = NS). The PKC inhibitor RO-318220 10(-6) M increased immunosignal (lower phosphorylation degree) in mTAL of CRF rats to 128.43 +/- 7.08% (p < 0.05) but did not alter McK1 binding in control rats. Both phorbol 12-myristate 13-acetate (PMA) 10(-6) M and dopamine 10(-6) M decreased immunosignal in CRF rats, corresponding to a higher Na+ K+ ATPase alpha1-subunit phosphorylation degree at Ser-23 (55.26 +/- 11.17% and 53.27 +/- 7.12% compared with basal, p < 0.05). In mTAL of CRF rats, the calcineurin inhibitor FK-506 10(-6) M did not modify phosphorylation degree at Ser-23 of Na+ K+ ATPase alpha1-subunit (100.21 +/- 3.00% compared with basal CRF). In control rats, FK 506 10(-6) M decreased the immunosignal, which corresponds to a higher Na+ K+ ATPase alpha1-subunit phosphorylation degree at Ser-23. The data suggest that the regulation of basal Na+ K+ ATPase alpha1-subunit phosphorylation degree at Ser-23 in mTAL segments of CRF rats was primarily dependent on PKC activation rather than calcineurin dependent mechanisms.
Mesh-Begriff(e)	Animals ; Calcineurin/metabolism ; In Vitro Techniques ; Kidney Failure, Chronic/metabolism ; Loop of Henle/metabolism ; Male ; Phosphorylation ; Protein Kinase C/metabolism ; Rats ; Rats, Wistar ; Sodium-Potassium-Exchanging ATPase/metabolism
Chemische Substanzen	Protein Kinase C (EC 2.7.11.13) ; Calcineurin (EC 3.1.3.16) ; Atp1a1 protein, rat (EC 3.6.1.-) ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)
Sprache	Englisch
Erscheinungsdatum	2007
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632949-4
ISSN	1525-6049 ; 0886-022X
ISSN (online)	1525-6049
ISSN	0886-022X
DOI	10.1080/08860220601038496
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Zusatzmaterialien

Verfügbar in ZB MED Köln/Königswinter

Zs.A 1331: Hefte anzeigen

Standort:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Über subito bestellen

Details ▾
- Im ZB MED-Bestand
- Kostenpflichtig bestellen

Artikel: Polycystin-1 C-terminal Cleavage Is Modulated by Polycystin-2 Expression

Bertuccio, Claudia A / Chapin, Hannah C / Cai, Yiqiang / Mistry, Kavita / Chauvet, Veronique / Somlo, Stefan / Caplan, Michael J

Journal of biological chemistry. 2009 July 31, v. 284, no. 31

2009

Abstract: Autosomal dominant polycystic kidney disease is caused by mutations in the genes encoding polycystin-1 (PC-1) and polycystin-2 (PC-2). PC-1 cleavage releases its cytoplasmic C-terminal tail (CTT), which enters the nucleus. To determine whether PC-1 CTT ... ...

Abstract	Autosomal dominant polycystic kidney disease is caused by mutations in the genes encoding polycystin-1 (PC-1) and polycystin-2 (PC-2). PC-1 cleavage releases its cytoplasmic C-terminal tail (CTT), which enters the nucleus. To determine whether PC-1 CTT cleavage is influenced by PC-2, a quantitative cleavage assay was utilized, in which the DNA binding and activation domains of Gal4 and VP16, respectively, were appended to PC-1 downstream of its CTT domain (PKDgalvp). Cells cotransfected with the resultant PKDgalvp fusion protein and PC-2 showed an increase in luciferase activity and in CTT expression, indicating that the C-terminal tail of PC-1 is cleaved and enters the nucleus. To assess whether CTT cleavage depends upon Ca²⁺ signaling, cells transfected with PKDgalvp alone or together with PC-2 were incubated with several agents that alter intracellular Ca²⁺ concentrations. PC-2 enhancement of luciferase activity was not altered by any of these treatments. Using a series of PC-2 C-terminal truncated mutations, we identified a portion of the PC-2 protein that is required to stimulate PC-1 CTT accumulation. These data demonstrate that release of the CTT from PC-1 is influenced and stabilized by PC-2. This effect is independent of Ca²⁺ but is regulated by sequences contained within the PC-2 C-terminal tail, suggesting a mechanism through which PC-1 and PC-2 may modulate a novel signaling pathway.
Sprache	Englisch
Erscheinungsverlauf	2009-0731
Umfang	p. 21011-21026.
Erscheinungsort	American Society for Biochemistry and Molecular Biology
Dokumenttyp	Artikel
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
Datenquelle	NAL Katalog (AGRICOLA)

Zusatzmaterialien

Verfügbar in ZB MED Bonn

Z 4' 65/118: Hefte anzeigen
Z 6.2: Hefte anzeigen

Über subito bestellen

Fernleihe an ZB MED

Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

Details ▾
- Im ZB MED-Bestand
- Kostenpflichtig bestellen

Artikel ; Online: Polycystin-1 C-terminal cleavage is modulated by polycystin-2 expression.

Bertuccio, Claudia A / Chapin, Hannah C / Cai, Yiqiang / Mistry, Kavita / Chauvet, Veronique / Somlo, Stefan / Caplan, Michael J

The Journal of biological chemistry

2009 Band 284, Heft 31, Seite(n) 21011–21026

Abstract	Autosomal dominant polycystic kidney disease is caused by mutations in the genes encoding polycystin-1 (PC-1) and polycystin-2 (PC-2). PC-1 cleavage releases its cytoplasmic C-terminal tail (CTT), which enters the nucleus. To determine whether PC-1 CTT cleavage is influenced by PC-2, a quantitative cleavage assay was utilized, in which the DNA binding and activation domains of Gal4 and VP16, respectively, were appended to PC-1 downstream of its CTT domain (PKDgalvp). Cells cotransfected with the resultant PKDgalvp fusion protein and PC-2 showed an increase in luciferase activity and in CTT expression, indicating that the C-terminal tail of PC-1 is cleaved and enters the nucleus. To assess whether CTT cleavage depends upon Ca2+ signaling, cells transfected with PKDgalvp alone or together with PC-2 were incubated with several agents that alter intracellular Ca2+ concentrations. PC-2 enhancement of luciferase activity was not altered by any of these treatments. Using a series of PC-2 C-terminal truncated mutations, we identified a portion of the PC-2 protein that is required to stimulate PC-1 CTT accumulation. These data demonstrate that release of the CTT from PC-1 is influenced and stabilized by PC-2. This effect is independent of Ca2+ but is regulated by sequences contained within the PC-2 C-terminal tail, suggesting a mechanism through which PC-1 and PC-2 may modulate a novel signaling pathway.
Mesh-Begriff(e)	Amino Acid Substitution/drug effects ; Amino Acids/metabolism ; Animals ; COS Cells ; Calcium/pharmacology ; Cell Nucleus/drug effects ; Cell Nucleus/metabolism ; Chlorocebus aethiops ; Extracellular Space/drug effects ; Extracellular Space/metabolism ; Genes, Reporter ; Humans ; Intracellular Space/drug effects ; Intracellular Space/metabolism ; Mice ; Mutant Proteins/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Processing, Post-Translational/drug effects ; Protein Transport/drug effects ; Structure-Activity Relationship ; TRPP Cation Channels/chemistry ; TRPP Cation Channels/metabolism
Chemische Substanzen	Amino Acids ; Mutant Proteins ; TRPP Cation Channels ; polycystic kidney disease 1 protein ; polycystic kidney disease 2 protein ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Calcium (SY7Q814VUP)
Sprache	Englisch
Erscheinungsdatum	2009-06-02
Erscheinungsland	United States
Dokumenttyp	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	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M109.017756
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

Zusatzmaterialien

Verfügbar in ZB MED Köln/Königswinter

Uc I Zs.108: Hefte anzeigen

Standort:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Über subito bestellen

Details ▾
- Im ZB MED-Bestand
- Kostenpflichtig bestellen

Zum Seitenanfang

Ihre letzten Suchen

Zusatzmaterialien

Kategorien

Über subito bestellen

Zusatzmaterialien

Kategorien

Verfügbar in ZB MED Köln/Königswinter

Über subito bestellen

Zusatzmaterialien

Kategorien

Verfügbar in ZB MED Köln/Königswinter

Über subito bestellen

Zusatzmaterialien

Kategorien

Über subito bestellen

Fernleihe an ZB MED

Volltext online

Zusatzmaterialien

Kategorien

Verfügbar in ZB MED Köln/Königswinter

Über subito bestellen

Zusatzmaterialien

Kategorien

Über subito bestellen

Fernleihe an ZB MED

Zusatzmaterialien

Kategorien

Über subito bestellen

Fernleihe an ZB MED

Zusatzmaterialien

Kategorien

Verfügbar in ZB MED Köln/Königswinter

Über subito bestellen

Zusatzmaterialien

Kategorien

Verfügbar in ZB MED Bonn

Über subito bestellen

Fernleihe an ZB MED

Zusatzmaterialien

Kategorien

Verfügbar in ZB MED Köln/Königswinter

Über subito bestellen