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  1. Article ; Online: My, oh, MYO9A! Just how complex can regulation of the podocyte actin cytoskeleton get?

    Schlöndorff, Johannes S

    Kidney international

    2021  Volume 99, Issue 5, Page(s) 1065–1067

    Abstract: Genetics contributes significantly to the development of kidney diseases. In the case of glomerular diseases such as focal segmental glomerulosclerosis, over a dozen genes involved in maintaining and regulating the actin cytoskeleton of podocytes have ... ...

    Abstract Genetics contributes significantly to the development of kidney diseases. In the case of glomerular diseases such as focal segmental glomerulosclerosis, over a dozen genes involved in maintaining and regulating the actin cytoskeleton of podocytes have been implicated. A new study adds the atypical myosin, MYO9A, to that list using a combination of human and mouse genetics, suggesting a link to enhanced RhoA activity. Unraveling the growing web of actin regulators remains a key challenge to understanding podocytopathies.
    MeSH term(s) Actin Cytoskeleton ; Animals ; GTPase-Activating Proteins ; Glomerulosclerosis, Focal Segmental/genetics ; Mice ; Myosins/genetics ; Podocytes
    Chemical Substances GTPase-Activating Proteins ; Myosins (EC 3.6.4.1)
    Language English
    Publishing date 2021-04-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 120573-0
    ISSN 1523-1755 ; 0085-2538
    ISSN (online) 1523-1755
    ISSN 0085-2538
    DOI 10.1016/j.kint.2021.01.006
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  2. Article ; Online: Trpc6 gain-of-function disease mutation enhances phosphatidylserine exposure in murine platelets.

    Boekell, Kimber L / Brown, Brittney J / Talbot, Brianna E / Schlondorff, Johannes S

    PloS one

    2022  Volume 17, Issue 6, Page(s) e0270431

    Abstract: Platelets enhance coagulation by exposing phosphatidylserine (PS) on their cell surface in response to strong agonist activation. Transient receptor potential channels, including TRPC6, have been implicated in the calcium influx central to this process. ... ...

    Abstract Platelets enhance coagulation by exposing phosphatidylserine (PS) on their cell surface in response to strong agonist activation. Transient receptor potential channels, including TRPC6, have been implicated in the calcium influx central to this process. Here, we characterize the effect of a Trpc6 gain-of-function (GOF) disease-associated, and a dominant negative (DN), mutation on murine platelet activation. Platelets from mice harboring Trpc6E896K/E896K (GOF) and Trpc6DN/DN mutations were subject to in vitro analysis. Trpc6E896K/E896K and Trpc6DN/DN mutant platelets show enhanced and absent calcium influx, respectively, upon addition of the TRPC3/6 agonist GSK1702934A (GSK). GSK was sufficient to induce integrin αIIbβ3 activation, P-selection and PS exposure, talin cleavage, and MLC2 phosphorylation in Trpc6E896K/E896K, but not in wild-type, platelets. Thrombin-induced calcium influx and PS exposure were enhanced, and clot retraction delayed, by GOF TRPC6, while no differences were noted between wild-type and Trpc6DN/DN platelets. In contrast, Erk activation upon GSK treatment was absent in Trpc6DN/DN, and enhanced in Trpc6E896K/E896K, platelets, compared to wild-type. The positive allosteric modulator, TRPC6-PAM-C20, and fluoxetine maintained their ability to enhance and inhibit, respectively, GSK-mediated calcium influx in Trpc6E896K/E896K platelets. The data demonstrate that gain-of-function mutant TRPC6 channel can enhance platelet activation, including PS exposure, while confirming that TRPC6 is not necessary for this process. Furthermore, the results suggest that Trpc6 GOF disease mutants do not simply increase wild-type TRPC6 responses, but can affect pathways not usually modulated by TRPC6 channel activity, displaying a true gain-of-function phenotype.
    MeSH term(s) Animals ; Blood Platelets/metabolism ; Calcium/metabolism ; Gain of Function Mutation ; Mice ; Mutation ; Phosphatidylserines/metabolism ; Platelet Glycoprotein GPIIb-IIIa Complex/metabolism ; TRPC Cation Channels/genetics ; TRPC Cation Channels/metabolism ; TRPC6 Cation Channel/genetics ; TRPC6 Cation Channel/metabolism
    Chemical Substances Phosphatidylserines ; Platelet Glycoprotein GPIIb-IIIa Complex ; TRPC Cation Channels ; TRPC6 Cation Channel ; Trpc6 protein, mouse ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2022-06-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; 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.0270431
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  3. Article ; Online: Dysregulated Dynein-Mediated Trafficking of Nephrin Causes INF2-related Podocytopathy.

    Sun, Hua / Perez-Gill, Chandra / Schlöndorff, Johannes S / Subramanian, Balajikarthick / Pollak, Martin R

    Journal of the American Society of Nephrology : JASN

    2020  Volume 32, Issue 2, Page(s) 307–322

    Abstract: Background: FSGS caused by mutations in : Methods: Live cell and quantitative imaging, fluorescent and surface biotinylation-based trafficking assays in cultured podocytes, and a new puromycin aminoglycoside nephropathy model of : Results: ... ...

    Abstract Background: FSGS caused by mutations in
    Methods: Live cell and quantitative imaging, fluorescent and surface biotinylation-based trafficking assays in cultured podocytes, and a new puromycin aminoglycoside nephropathy model of
    Results: Pathogenic
    Conclusions: INF2
    MeSH term(s) Animals ; Cell Culture Techniques ; Cytoplasmic Dyneins/metabolism ; Formins/genetics ; Glomerulosclerosis, Focal Segmental/etiology ; Glomerulosclerosis, Focal Segmental/metabolism ; Glomerulosclerosis, Focal Segmental/pathology ; Membrane Proteins/metabolism ; Mice ; Mutation/genetics ; Podocytes/metabolism ; Podocytes/pathology ; Protein Transport
    Chemical Substances Formins ; INF2 protein, mouse ; Membrane Proteins ; nephrin ; Cytoplasmic Dyneins (EC 3.6.4.2) ; DYNLL1 protein, mouse (EC 3.6.4.2)
    Language English
    Publishing date 2020-12-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1085942-1
    ISSN 1533-3450 ; 1046-6673
    ISSN (online) 1533-3450
    ISSN 1046-6673
    DOI 10.1681/ASN.2020081109
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3344: Show issues Location:
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  4. Article ; Online: Gain-of-function, focal segmental glomerulosclerosis Trpc6 mutation minimally affects susceptibility to renal injury in several mouse models.

    Brown, Brittney J / Boekell, Kimber L / Stotter, Brian R / Talbot, Brianna E / Schlondorff, Johannes S

    PloS one

    2022  Volume 17, Issue 8, Page(s) e0272313

    Abstract: Mutations in TRPC6 are a cause of autosomal dominant focal segmental glomerulosclerosis in humans. Many of these mutations are known to have a gain-of-function effect on the non-specific cation channel function of TRPC6. In vitro studies have suggested ... ...

    Abstract Mutations in TRPC6 are a cause of autosomal dominant focal segmental glomerulosclerosis in humans. Many of these mutations are known to have a gain-of-function effect on the non-specific cation channel function of TRPC6. In vitro studies have suggested these mutations affect several signaling pathways, but in vivo studies have largely compared wild-type and Trpc6-deficient rodents. We developed mice carrying a gain-of-function Trpc6 mutation encoding an E896K amino acid change, corresponding to a known FSGS mutation in TRPC6. Homozygous mutant Trpc6 animals have no appreciable renal pathology, and do not develop albuminuria until very advanced age. The Trpc6E896K mutation does not impart susceptibility to PAN nephrosis. The animals show a slight delay in recovery from the albumin overload model. In response to chronic angiotensin II infusion, Trpc6E896K/E896K mice have slightly greater albuminuria initially compared to wild-type animals, an effect that is lost at later time points, and a statistically non-significant trend toward more glomerular injury. This phenotype is nearly opposite to that of Trpc6-deficient animals previously described. The Trpc6 mutation does not appreciably impact renal interstitial fibrosis in response to either angiotensin II infusion, or folate-induced kidney injury. TRPC6 protein and TRPC6-agonist induced calcium influx could not be detected in glomeruli. In sum, these findings suggest that a gain-of-function Trpc6 mutation confers only a mild susceptibility to glomerular injury in the mouse.
    MeSH term(s) Albuminuria/pathology ; Angiotensin II/pharmacology ; Animals ; Disease Models, Animal ; Gain of Function Mutation ; Glomerulosclerosis, Focal Segmental/pathology ; Humans ; Kidney/pathology ; Kidney Diseases/pathology ; Mice ; Mutation ; Podocytes/metabolism ; TRPC6 Cation Channel/genetics ; TRPC6 Cation Channel/metabolism
    Chemical Substances TRPC6 Cation Channel ; TRPC6 protein, human ; Trpc6 protein, mouse ; Angiotensin II (11128-99-7)
    Language English
    Publishing date 2022-08-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0272313
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  5. Article ; Online: Genetic evaluation of living kidney donor candidates: A review and recommendations for best practices.

    Thomas, Christie P / Daloul, Reem / Lentine, Krista L / Gohh, Reginald / Anand, Prince M / Rasouly, Hila Milo / Sharfuddin, Asif A / Schlondorff, Johannes S / Rodig, Nancy M / Freese, Margaret E / Garg, Neetika / Lee, Brian K / Caliskan, Yasar

    American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons

    2023  Volume 23, Issue 5, Page(s) 597–607

    Abstract: The growing accessibility and falling costs of genetic sequencing techniques has expanded the utilization of genetic testing in clinical practice. For living kidney donation, genetic evaluation has been increasingly used to identify genetic kidney ... ...

    Abstract The growing accessibility and falling costs of genetic sequencing techniques has expanded the utilization of genetic testing in clinical practice. For living kidney donation, genetic evaluation has been increasingly used to identify genetic kidney disease in potential candidates, especially in those of younger ages. However, genetic testing on asymptomatic living kidney donors remains fraught with many challenges and uncertainties. Not all transplant practitioners are aware of the limitations of genetic testing, are comfortable with selecting testing methods, comprehending test results, or providing counsel, and many do not have access to a renal genetic counselor or a clinical geneticist. Although genetic testing can be a valuable tool in living kidney donor evaluation, its overall benefit in donor evaluation has not been demonstrated and it can also lead to confusion, inappropriate donor exclusion, or misleading reassurance. Until more published data become available, this practice resource should provide guidance for centers and transplant practitioners on the responsible use of genetic testing in the evaluation of living kidney donor candidates.
    MeSH term(s) Humans ; Kidney Transplantation ; Living Donors ; Donor Selection ; Tissue and Organ Harvesting
    Language English
    Publishing date 2023-03-01
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2060594-8
    ISSN 1600-6143 ; 1600-6135
    ISSN (online) 1600-6143
    ISSN 1600-6135
    DOI 10.1016/j.ajt.2023.02.020
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    Zs.A 5542: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  6. Article ; Online: Gain-of-function, focal segmental glomerulosclerosis Trpc6 mutation minimally affects susceptibility to renal injury in several mouse models.

    Brittney J Brown / Kimber L Boekell / Brian R Stotter / Brianna E Talbot / Johannes S Schlondorff

    PLoS ONE, Vol 17, Iss 8, p e

    2022  Volume 0272313

    Abstract: Mutations in TRPC6 are a cause of autosomal dominant focal segmental glomerulosclerosis in humans. Many of these mutations are known to have a gain-of-function effect on the non-specific cation channel function of TRPC6. In vitro studies have suggested ... ...

    Abstract Mutations in TRPC6 are a cause of autosomal dominant focal segmental glomerulosclerosis in humans. Many of these mutations are known to have a gain-of-function effect on the non-specific cation channel function of TRPC6. In vitro studies have suggested these mutations affect several signaling pathways, but in vivo studies have largely compared wild-type and Trpc6-deficient rodents. We developed mice carrying a gain-of-function Trpc6 mutation encoding an E896K amino acid change, corresponding to a known FSGS mutation in TRPC6. Homozygous mutant Trpc6 animals have no appreciable renal pathology, and do not develop albuminuria until very advanced age. The Trpc6E896K mutation does not impart susceptibility to PAN nephrosis. The animals show a slight delay in recovery from the albumin overload model. In response to chronic angiotensin II infusion, Trpc6E896K/E896K mice have slightly greater albuminuria initially compared to wild-type animals, an effect that is lost at later time points, and a statistically non-significant trend toward more glomerular injury. This phenotype is nearly opposite to that of Trpc6-deficient animals previously described. The Trpc6 mutation does not appreciably impact renal interstitial fibrosis in response to either angiotensin II infusion, or folate-induced kidney injury. TRPC6 protein and TRPC6-agonist induced calcium influx could not be detected in glomeruli. In sum, these findings suggest that a gain-of-function Trpc6 mutation confers only a mild susceptibility to glomerular injury in the mouse.
    Keywords Medicine ; R ; Science ; Q
    Subject code 616
    Language English
    Publishing date 2022-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
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  7. Article ; Online: Gain-of-function, focal segmental glomerulosclerosis Trpc6 mutation minimally affects susceptibility to renal injury in several mouse models

    Brittney J. Brown / Kimber L. Boekell / Brian R. Stotter / Brianna E. Talbot / Johannes S. Schlondorff

    PLoS ONE, Vol 17, Iss

    2022  Volume 8

    Abstract: Mutations in TRPC6 are a cause of autosomal dominant focal segmental glomerulosclerosis in humans. Many of these mutations are known to have a gain-of-function effect on the non-specific cation channel function of TRPC6. In vitro studies have suggested ... ...

    Abstract Mutations in TRPC6 are a cause of autosomal dominant focal segmental glomerulosclerosis in humans. Many of these mutations are known to have a gain-of-function effect on the non-specific cation channel function of TRPC6. In vitro studies have suggested these mutations affect several signaling pathways, but in vivo studies have largely compared wild-type and Trpc6-deficient rodents. We developed mice carrying a gain-of-function Trpc6 mutation encoding an E896K amino acid change, corresponding to a known FSGS mutation in TRPC6. Homozygous mutant Trpc6 animals have no appreciable renal pathology, and do not develop albuminuria until very advanced age. The Trpc6E896K mutation does not impart susceptibility to PAN nephrosis. The animals show a slight delay in recovery from the albumin overload model. In response to chronic angiotensin II infusion, Trpc6E896K/E896K mice have slightly greater albuminuria initially compared to wild-type animals, an effect that is lost at later time points, and a statistically non-significant trend toward more glomerular injury. This phenotype is nearly opposite to that of Trpc6-deficient animals previously described. The Trpc6 mutation does not appreciably impact renal interstitial fibrosis in response to either angiotensin II infusion, or folate-induced kidney injury. TRPC6 protein and TRPC6-agonist induced calcium influx could not be detected in glomeruli. In sum, these findings suggest that a gain-of-function Trpc6 mutation confers only a mild susceptibility to glomerular injury in the mouse.
    Keywords Medicine ; R ; Science ; Q
    Subject code 616
    Language English
    Publishing date 2022-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
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  8. Article ; Online: Transmembrane insertases and

    Talbot, Brianna E / Vandorpe, David H / Stotter, Brian R / Alper, Seth L / Schlondorff, Johannes S

    The Journal of biological chemistry

    2019  Volume 294, Issue 34, Page(s) 12655–12669

    Abstract: Transient receptor potential cation channel subfamily C member 6 (TRPC6) is a widely expressed ion channel. Gain-of-function mutations in the human TRPC6 channel cause autosomal-dominant focal segmental glomerulosclerosis, but the molecular components ... ...

    Abstract Transient receptor potential cation channel subfamily C member 6 (TRPC6) is a widely expressed ion channel. Gain-of-function mutations in the human TRPC6 channel cause autosomal-dominant focal segmental glomerulosclerosis, but the molecular components involved in disease development remain unclear. Here, we found that overexpression of gain-of-function TRPC6 channel variants is cytotoxic in cultured cells. Exploiting this phenotype in a genome-wide CRISPR/Cas screen for genes whose inactivation rescues cells from TRPC6-associated cytotoxicity, we identified several proteins essential for TRPC6 protein expression, including the endoplasmic reticulum (ER) membrane protein complex transmembrane insertase. We also identified transmembrane protein 208 (TMEM208), a putative component of a signal recognition particle-independent (SND) ER protein-targeting pathway, as being necessary for expression of TRPC6 and several other ion channels and transporters. TRPC6 expression was also diminished by loss of the previously uncharacterized WD repeat domain 83 opposite strand (WDR83OS), which interacted with both TRPC6 and TMEM208. Additionally enriched among the screen hits were genes involved in
    MeSH term(s) CRISPR-Cas Systems/genetics ; Calcium/metabolism ; Cell Death/drug effects ; Cell Membrane/drug effects ; Cell Membrane/metabolism ; Gain of Function Mutation ; Glycosylation/drug effects ; HEK293 Cells ; Humans ; Membrane Proteins/metabolism ; N-Acetylglucosaminyltransferases/metabolism ; Podocytes/drug effects ; Podocytes/metabolism ; Protein Binding/drug effects ; RNA, Guide, CRISPR-Cas Systems/metabolism ; TRPC6 Cation Channel/metabolism
    Chemical Substances Membrane Proteins ; RNA, Guide, CRISPR-Cas Systems ; TMEM208 protein, human ; TRPC6 Cation Channel ; MGAT1 protein, human (EC 2.4.1.-) ; N-Acetylglucosaminyltransferases (EC 2.4.1.-) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2019-07-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA119.008299
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    Uc I Zs.108: Show issues Location:
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  9. Article ; Online: FSGS-Causing INF2 Mutation Impairs Cleaved INF2 N-Fragment Functions in Podocytes.

    Subramanian, Balajikarthick / Chun, Justin / Perez-Gill, Chandra / Yan, Paul / Stillman, Isaac E / Higgs, Henry N / Alper, Seth L / Schlöndorff, Johannes S / Pollak, Martin R

    Journal of the American Society of Nephrology : JASN

    2020  Volume 31, Issue 2, Page(s) 374–391

    Abstract: Background: Mutations in the gene encoding inverted formin-2 (INF2), a member of the formin family of actin regulatory proteins, are among the most common causes of autosomal dominant FSGS. INF2 is regulated by interaction between its N-terminal ... ...

    Abstract Background: Mutations in the gene encoding inverted formin-2 (INF2), a member of the formin family of actin regulatory proteins, are among the most common causes of autosomal dominant FSGS. INF2 is regulated by interaction between its N-terminal diaphanous inhibitory domain (DID) and its C-terminal diaphanous autoregulatory domain (DAD). INF2 also modulates activity of other formins, such as the mDIA subfamily, and promotes stable microtubule assembly. Why the disease-causing mutations are restricted to the N terminus and how they cause human disease has been unclear.
    Methods: We examined INF2 isoforms present in podocytes and evaluated INF2 cleavage as an explanation for immunoblot findings. We evaluated the expression of INF2 N- and C-terminal fragments in human kidney disease conditions. We also investigated the localization and functions of the DID-containing N-terminal fragment in podocytes and assessed whether the FSGS-associated R218Q mutation impairs INF2 cleavage or the function of the N-fragment.
    Results: The INF2-CAAX isoform is the predominant isoform in podocytes. INF2 is proteolytically cleaved, a process mediated by cathepsin proteases, liberating the N-terminal DID to function independently. Although the N-terminal region normally localizes to podocyte foot processes, it does not do so in the presence of FSGS-associated INF2 mutations. The C-terminal fragment localizes to the cell body irrespective of INF2 mutations. In podocytes, the N-fragment localizes to the plasma membrane, binds mDIA1, and promotes cell spreading in a cleavage-dependent way. The disease-associated R218Q mutation impairs these N-fragment functions but not INF2 cleavage.
    Conclusions: INF2 is cleaved into an N-terminal DID-containing fragment and a C-terminal DAD-containing fragment. Cleavage allows the N-terminal fragment to function independently and helps explain the clustering of FSGS-associated mutations.
    MeSH term(s) Animals ; Cathepsins/physiology ; Cells, Cultured ; Formins/genetics ; Formins/physiology ; Glomerulosclerosis, Focal Segmental/etiology ; Glomerulosclerosis, Focal Segmental/genetics ; HEK293 Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Mutation ; Peptide Fragments/physiology ; Podocytes/physiology ; Protein Isoforms
    Chemical Substances Formins ; INF2 protein, human ; Peptide Fragments ; Protein Isoforms ; Cathepsins (EC 3.4.-)
    Language English
    Publishing date 2020-01-10
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1085942-1
    ISSN 1533-3450 ; 1046-6673
    ISSN (online) 1533-3450
    ISSN 1046-6673
    DOI 10.1681/ASN.2019050443
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    Zs.A 3344: Show issues Location:
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  10. Article: TRPC6 in glomerular health and disease: what we know and what we believe.

    Schlöndorff, Johannes S / Pollak, Martin R

    Seminars in cell & developmental biology

    2006  Volume 17, Issue 6, Page(s) 667–674

    Abstract: Mutations in TRPC6, a member of the transient receptor potential (TRP) superfamily of non-selective cation channels, have been identified as causing a familial form of focal segmental glomerulosclerosis, a disease characterized by proteinuria and ... ...

    Abstract Mutations in TRPC6, a member of the transient receptor potential (TRP) superfamily of non-selective cation channels, have been identified as causing a familial form of focal segmental glomerulosclerosis, a disease characterized by proteinuria and progressive renal failure. Here we review the effect of disease-associated mutations on TRPC6 function and place TRPC6 within the context of other proteins central to glomerular and podocyte function. Finally, the known roles of TRPC6 in the kidney and other organ systems are used as a framework to discuss possible signaling pathways that TRPC6 may modulate during normal glomerular function and in disease states.
    MeSH term(s) Animals ; Humans ; Kidney Diseases/metabolism ; Kidney Diseases/physiopathology ; Kidney Glomerulus/metabolism ; Kidney Glomerulus/physiology ; Kidney Glomerulus/physiopathology ; TRPC Cation Channels/physiology ; TRPC6 Cation Channel
    Chemical Substances TRPC Cation Channels ; TRPC6 Cation Channel ; TRPC6 protein, human ; Trpc6 protein, mouse ; Trpc6 protein, rat
    Language English
    Publishing date 2006-12
    Publishing country England
    Document type Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2006.11.003
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    Zs.A 2918: Show issues Location:
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