The Experts below are selected from a list of 22509 Experts worldwide ranked by ideXlab platform
Alain Vandewalle - One of the best experts on this subject based on the ideXlab platform.
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transimmortalized proximal tubule and collecting Duct Cell lines derived from the kidneys of transgenic mice
Cell Biology and Toxicology, 2007Co-Authors: Cecilia Chassin, Marcelle Bens, Alain VandewalleAbstract:This review summarizes the strategy of Cellular immortalization based on the principle of targeted oncogenesis in transgenic mice, used to establish models of transimmortalized renal proximal tubule Cells, referred to as PKSV-PCT and PKSV-PR-Cells, and collecting Duct principal Cells, referred to as mpkCCDcl4 Cells. These Cell lines have maintained for long-term passages the main biochemical and functional properties of the parental Cells from which they were derived. Proximal tubule PKSV-PCT and PKSV-PR Cells have been proved to be suitable Cell systems for toxicological and pharmacological studies. They also permitted the establishment of a model of multidrug-resistant (MDR) renal epithelial tubule Cells, PKSV-PRcol50, which have served for the study of both MDR-dependent extrusion of chemotherapeutic drugs and inappropriate accumulation of weak base anthracyclines in intraCellular acidic organelles. The novel collecting Duct Cell line mpkCCDcl4, which has maintained the characteristics of tight epithelial Cells, in particular Na+ absorption stimulated by aldosterone, has been extensively used for pharmacological studies related to the regulation of ion transport. These Cells have permitted the identification of several aldosterone-induced proteins playing a key role in the regulation of Na+ absorption mediated by the epithelial Na+ channel ENaC. Recent studies have also provided evidence that these Cell lines represent valuable Cell systems for the study of host–pathogen interactions and the analysis of the role of renal tubule epithelial Cells in the inDuction of inflammatory response caused by uropathogens that may lead to severe renal damage.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:Abstract . This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD c14 ). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus , xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus , rat, or human α-, β-, and γ-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD(c14)). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus, xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus, rat, or human alpha-, beta-, and gamma-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
Edith Hummler - One of the best experts on this subject based on the ideXlab platform.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:Abstract . This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD c14 ). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus , xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus , rat, or human α-, β-, and γ-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD(c14)). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus, xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus, rat, or human alpha-, beta-, and gamma-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
Marcelle Bens - One of the best experts on this subject based on the ideXlab platform.
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transimmortalized proximal tubule and collecting Duct Cell lines derived from the kidneys of transgenic mice
Cell Biology and Toxicology, 2007Co-Authors: Cecilia Chassin, Marcelle Bens, Alain VandewalleAbstract:This review summarizes the strategy of Cellular immortalization based on the principle of targeted oncogenesis in transgenic mice, used to establish models of transimmortalized renal proximal tubule Cells, referred to as PKSV-PCT and PKSV-PR-Cells, and collecting Duct principal Cells, referred to as mpkCCDcl4 Cells. These Cell lines have maintained for long-term passages the main biochemical and functional properties of the parental Cells from which they were derived. Proximal tubule PKSV-PCT and PKSV-PR Cells have been proved to be suitable Cell systems for toxicological and pharmacological studies. They also permitted the establishment of a model of multidrug-resistant (MDR) renal epithelial tubule Cells, PKSV-PRcol50, which have served for the study of both MDR-dependent extrusion of chemotherapeutic drugs and inappropriate accumulation of weak base anthracyclines in intraCellular acidic organelles. The novel collecting Duct Cell line mpkCCDcl4, which has maintained the characteristics of tight epithelial Cells, in particular Na+ absorption stimulated by aldosterone, has been extensively used for pharmacological studies related to the regulation of ion transport. These Cells have permitted the identification of several aldosterone-induced proteins playing a key role in the regulation of Na+ absorption mediated by the epithelial Na+ channel ENaC. Recent studies have also provided evidence that these Cell lines represent valuable Cell systems for the study of host–pathogen interactions and the analysis of the role of renal tubule epithelial Cells in the inDuction of inflammatory response caused by uropathogens that may lead to severe renal damage.
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transcriptome of a mouse kidney cortical collecting Duct Cell line effects of aldosterone and vasopressin
Proceedings of the National Academy of Sciences of the United States of America, 2001Co-Authors: Maya Robertnicoud, Marcelle Bens, Marjorie Flahaut, Jeanmarc Elalouf, Marie Nicod, Miguel Salinas, Alain Doucet, Patrick Wincker, Francois Artiguenave, Jeandaniel HorisbergerAbstract:Aldosterone and vasopressin are responsible for the final adjustment of sodium and water reabsorption in the kidney. In principal Cells of the kidney cortical collecting Duct (CCD), the integral response to aldosterone and the long-term functional effects of vasopressin depend on transcription. In this study, we analyzed the transcriptome of a highly differentiated mouse clonal CCD principal Cell line (mpkCCD(cl4)) and the changes in the transcriptome induced by aldosterone and vasopressin. Serial analysis of gene expression (SAGE) was performed on untreated Cells and on Cells treated with either aldosterone or vasopressin for 4 h. The transcriptomes in these three experimental conditions were determined by sequencing 169,721 transcript tags from the corresponding SAGE libraries. Limiting the analysis to tags that occurred twice or more in the data set, 14,654 different transcripts were identified, 3,642 of which do not match known mouse sequences. Statistical comparison (at P < 0.05 level) of the three SAGE libraries revealed 34 AITs (aldosterone-induced transcripts), 29 ARTs (aldosterone-repressed transcripts), 48 VITs (vasopressin-induced transcripts) and 11 VRTs (vasopressin-repressed transcripts). A selection of the differentially-expressed, hormone-specific transcripts (5 VITs, 2 AITs and 1 ART) has been validated in the mpkCCD(cl4) Cell line either by Northern blot hybridization or reverse transcription-PCR. The hepatocyte nuclear transcription factor HNF-3-alpha (VIT39), the receptor activity modifying protein RAMP3 (VIT48), and the glucocorticoid-induced leucine zipper protein (GILZ) (AIT28) are candidate proteins playing a role in physiological responses of this Cell line to vasopressin and aldosterone.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:Abstract . This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD c14 ). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus , xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus , rat, or human α-, β-, and γ-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD(c14)). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus, xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus, rat, or human alpha-, beta-, and gamma-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
Gregoire Vuagniaux - One of the best experts on this subject based on the ideXlab platform.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:Abstract . This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD c14 ). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus , xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus , rat, or human α-, β-, and γ-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD(c14)). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus, xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus, rat, or human alpha-, beta-, and gamma-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
Bernard C Rossier - One of the best experts on this subject based on the ideXlab platform.
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effects of mineralocorticoid and k concentration on k secretion and romk channel expression in a mouse cortical collecting Duct Cell line
American Journal of Physiology-renal Physiology, 2009Co-Authors: Heidi Fodstad, Bernard C Rossier, Elena Gonzalezrodriguez, Sylvian Bron, Hanspeter Gaeggeler, Barbara Guisan, Jeandaniel HorisbergerAbstract:The cortical collecting Duct (CCD) plays a key role in regulated K+ secretion, which is mediated mainly through renal outer medullary K+ (ROMK) channels located in the apical membrane. However, the mechanisms of the regulation of urinary K+ excretion with regard to K+ balance are not well known. We took advantage of a recently established mouse CCD Cell line (mCCDcl1) to investigate the regulation of K+ secretion by mineralocorticoid and K+ concentration. We show that this Cell line expresses ROMK mRNA and a barium-sensitive K+ conDuctance in its apical membrane. As this conDuctance is sensitive to tertiapin-Q, with an apparent affinity of 6 nM, and to intraCellular acidification, it is probably mediated by ROMK. Overnight exposure to 100 nM aldosterone did not significantly change the K+ conDuctance, while it increased the amiloride-sensitive Na+ transport. Overnight exposure to a high K+ (7 mM) concentration produced a small but significant increase in the apical membrane barium-sensitive K+ conDuctance...
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:Abstract . This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD c14 ). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus , xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus , rat, or human α-, β-, and γ-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
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activation of the amiloride sensitive epithelial sodium channel by the serine protease mcap1 expressed in a mouse cortical collecting Duct Cell line
Journal of The American Society of Nephrology, 2000Co-Authors: Gregoire Vuagniaux, Marcelle Bens, Alain Vandewalle, Veronique Vallet, Nicole Fowler Jaeger, Corinne Pfister, Nicolette Farman, Nathalie Courtoiscoutry, Bernard C Rossier, Edith HummlerAbstract:This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial Cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting Duct Cell line (mpkCCD(c14)). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus, xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule Cells and was also expressed in intact and cultured collecting Duct Cells. Coexpression of the Xenopus, rat, or human alpha-, beta-, and gamma-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the Cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
