The Experts below are selected from a list of 3969 Experts worldwide ranked by ideXlab platform
Andrew M. Herzenberg - One of the best experts on this subject based on the ideXlab platform.
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receptor: site-specific and functional linkage to the vacuolar H+-ATPase in the kidney. Hypertension
2016Co-Authors: Andrew Advani, Darren J. Kelly, Alison J. Cox, Kathryn E. White, Suzanne L. Advani, Kerri Thai, Kim A. Connelly, Darren Yuen, Judy Trogadis, Andrew M. HerzenbergAbstract:Abstract—The (pro)renin receptor ([P]RR) is a transmembrane protein that binds both renin and prorenin with high affinity, increasing the catalytic cleavage of angiotensinogen and signaling intracellularly through mitogen-activated protein kinase activation. Although initially reported as having no homology with any known membrane protein, other studies have suggested that the (P)RR is an accessory protein, named ATP6ap2, that associates with the vacuolar H-ATPase, a key mediator of final urinary Acidification. Using in situ hybridization, immunohistochemistry, and electron microscopy, together with serial sections stained with nephron segment–specific markers, we found that (P)RR mRNA and protein were predominantly expressed in collecting ducts and in the distal nephron. Within collecting ducts, the (P)RR was most abundant in microvilli at the apical surface of A-type intercalated Cells. Dual-staining immunofluorescence demonstrated colocalization of the (P)RR with the B1/2 subunit of the vacuolar H-ATPase, the ion exchanger that secretes H ions into the urinary space and that associates with an accessory subunit homologous to the (P)RR. In collecting duct/distal tubule lineage Madin-Darby canine kidney Cells, extracellular signal–regulated kinase 1/2 phosphorylation, induced by either renin or prorenin, was attenuated by the selective vacuolar H-ATPase inhibitor bafilomycin. The predominant expression of the (P)RR at the apex of Acid-Secreting Cells in the collecting duct, along with its colocalization and homology with an accessory protein of the vacuolar H-ATPase, suggests that the (P)RR may function primarily in distal nephron H transport, recently noted to be, at least in part, an angiotensi
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the pro renin receptor site specific and functional linkage to the vacuolar h atpase in the kidney
Hypertension, 2009Co-Authors: Andrew Advani, Darren J. Kelly, Alison J. Cox, Suzanne L. Advani, Kerri Thai, Kim A. Connelly, Judy Trogadis, Kathryn White, Darren A Yuen, Andrew M. HerzenbergAbstract:The (pro)renin receptor ([P]RR) is a transmembrane protein that binds both renin and prorenin with high affinity, increasing the catalytic cleavage of angiotensinogen and signaling intracellularly through mitogen-activated protein kinase activation. Although initially reported as having no homology with any known membrane protein, other studies have suggested that the (P)RR is an accessory protein, named ATP6ap2, that associates with the vacuolar H(+)-ATPase, a key mediator of final urinary Acidification. Using in situ hybridization, immunohistochemistry, and electron microscopy, together with serial sections stained with nephron segment-specific markers, we found that (P)RR mRNA and protein were predominantly expressed in collecting ducts and in the distal nephron. Within collecting ducts, the (P)RR was most abundant in microvilli at the apical surface of A-type intercalated Cells. Dual-staining immunofluorescence demonstrated colocalization of the (P)RR with the B1/2 subunit of the vacuolar H(+)-ATPase, the ion exchanger that secretes H(+) ions into the urinary space and that associates with an accessory subunit homologous to the (P)RR. In collecting duct/distal tubule lineage Madin-Darby canine kidney Cells, extracellular signal-regulated kinase 1/2 phosphorylation, induced by either renin or prorenin, was attenuated by the selective vacuolar H(+)-ATPase inhibitor bafilomycin. The predominant expression of the (P)RR at the apex of Acid-Secreting Cells in the collecting duct, along with its colocalization and homology with an accessory protein of the vacuolar H(+)-ATPase, suggests that the (P)RR may function primarily in distal nephron H(+) transport, recently noted to be, at least in part, an angiotensin II-dependent phenomenon.
Ronald R Dubreuil - One of the best experts on this subject based on the ideXlab platform.
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differential effects of a labial mutation on the development structure and function of stomach Acid Secreting Cells in drosophila melanogaster larvae and adults
Cell and Tissue Research, 2001Co-Authors: Ronald R Dubreuil, Tatyana A Grushko, Otto BaumannAbstract:The differentiation of copper Cells, which secrete stomach Acid in Drosophila larvae, has been shown previously to be sensitive to the labial k3 mutation. Here we found that stomach Acid secretion in adults was insensitive to lab k3 . The basis for this stage-specific effect was elucidated by characterizing the development, structure, and function of the adult midgut. First, we demonstrated by copper-dependent fluorescence and morphology that copper Cells were present in the adult stomach. Fine-structure analysis of adult copper Cells led to the identification of a previously unrecognized plasma membrane domain: apicolateral contacts between copper Cells and their neighbors consisted of smooth septate junctions that were enriched in αβ-spectrin and ankyrin. Second, we demonstrated that adult copper Cells were present in lab k3 /lab vd1 (conditional/null) adults. The labial protein was expressed in adult lab k3 /lab vd1 copper Cells, but not in larvae. Thus the lab k3 mutation had a stage-specific effect on midgut labial expression, but did not appear to affect protein function. Surprisingly, stomach Acidification was dispensable during larval development, since lab k3 /lab vd1 mutant larvae that lacked midgut Acidification developed into fertile adults.
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evidence that a copper metallothionein complex is responsible for fluorescence in Acid Secreting Cells of the drosophila stomach
Cell and Tissue Research, 2001Co-Authors: Megan M Mcnulty, Michael Puljung, Greg Jefford, Ronald R DubreuilAbstract:Copper Cells were originally identified in Drosophila midgut epithelium by their striking orange fluorescence in copper-fed larvae. Here, we examined copper cell fluorescence in light of the previous observations that (1) a similar fluorescent signal in yeast is produced by a complex between copper and metallothionein, and (2) metallothionein is expressed constitutively in the copper cell region and inducibly in other regions of the Drosophila midgut. Pulse-feeding experiments with 1 mM CuCl2 revealed that fluorescence appeared rapidly in copper Cells (<5 min) and slowly in other Cells of the midgut (days), suggesting a constitutive cofactor in the former and an inducible cofactor in the latter. Fluorescence was also detected in Drosophila S2 tissue culture Cells after induction of metallothionein synthesis by addition of CuCl2 to the growth medium. Thus, fluorescence coincided spatially and temporally with the expression of metallothionein. Fluorescence was also linked to the Acid-Secreting activity of copper Cells. Fluorescence was not observed when Acid secretion was inhibited by a mutation in the α spectrin gene and Acidification was blocked in copper-fed wild-type larvae. However, Acidification was restored after a 1-day chase period in which the fluorescent signal became sequestered within a vesicular compartment. We therefore conclude that copper cell fluorescence is most probably attributable to a cytoplasmic copper-metallothionein complex, suggesting an unanticipated role for metallothionein in Acid-Secreting Cells.
Magotoshi Morii - One of the best experts on this subject based on the ideXlab platform.
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new fluorescent probes e3810 and methoxy e3810 for determining distributions of the apical membrane and the Acidic compartment of gastric Acid Secreting Cells
Japanese Journal of Physiology, 1992Co-Authors: Noriaki Takeguchi, Tsuneaki Yamanouchi, Hideki Sakai, Magotoshi MoriiAbstract:Substituted benzimidazoles such as omeprazole, E3810 and methoxy E3810 were inhibitors of gastric H+, K(+)-ATPase which is rich in the apical membrane of gastric parietal or oxyntic Cells at the Secreting state. The Acid-activated compounds of omeprazole and methoxy E3810, which have methoxy group at the 5-position in the benzimidazole ring, are fluorescent (excitation wavelength = 370 nm; emission wavelength = 560 nm). The fluorescence disappeared when the activated compounds reacted with the ATPase or glutathione. Using this fluorescence property, the distribution of the intracellular Acidic canalicular space in isolated single parietal Cells was determined. On the other hand, irradiation with ultraviolet light (335 nm) of the Acid-activated compound of E3810 which had been reacted with sulfhydryl group of the ATPase or glutathione resulted in a formation of a fluorescent compound (emission = 470 nm). Using this second fluorescence property, we determined the distribution of the apical membrane of the intracellular canaliculus of isolated single mammalian parietal Cells and also the location of the apical membrane on the external surface of newt oxyntic Cells.
Andrew Advani - One of the best experts on this subject based on the ideXlab platform.
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receptor: site-specific and functional linkage to the vacuolar H+-ATPase in the kidney. Hypertension
2016Co-Authors: Andrew Advani, Darren J. Kelly, Alison J. Cox, Kathryn E. White, Suzanne L. Advani, Kerri Thai, Kim A. Connelly, Darren Yuen, Judy Trogadis, Andrew M. HerzenbergAbstract:Abstract—The (pro)renin receptor ([P]RR) is a transmembrane protein that binds both renin and prorenin with high affinity, increasing the catalytic cleavage of angiotensinogen and signaling intracellularly through mitogen-activated protein kinase activation. Although initially reported as having no homology with any known membrane protein, other studies have suggested that the (P)RR is an accessory protein, named ATP6ap2, that associates with the vacuolar H-ATPase, a key mediator of final urinary Acidification. Using in situ hybridization, immunohistochemistry, and electron microscopy, together with serial sections stained with nephron segment–specific markers, we found that (P)RR mRNA and protein were predominantly expressed in collecting ducts and in the distal nephron. Within collecting ducts, the (P)RR was most abundant in microvilli at the apical surface of A-type intercalated Cells. Dual-staining immunofluorescence demonstrated colocalization of the (P)RR with the B1/2 subunit of the vacuolar H-ATPase, the ion exchanger that secretes H ions into the urinary space and that associates with an accessory subunit homologous to the (P)RR. In collecting duct/distal tubule lineage Madin-Darby canine kidney Cells, extracellular signal–regulated kinase 1/2 phosphorylation, induced by either renin or prorenin, was attenuated by the selective vacuolar H-ATPase inhibitor bafilomycin. The predominant expression of the (P)RR at the apex of Acid-Secreting Cells in the collecting duct, along with its colocalization and homology with an accessory protein of the vacuolar H-ATPase, suggests that the (P)RR may function primarily in distal nephron H transport, recently noted to be, at least in part, an angiotensi
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the pro renin receptor site specific and functional linkage to the vacuolar h atpase in the kidney
Hypertension, 2009Co-Authors: Andrew Advani, Darren J. Kelly, Alison J. Cox, Suzanne L. Advani, Kerri Thai, Kim A. Connelly, Judy Trogadis, Kathryn White, Darren A Yuen, Andrew M. HerzenbergAbstract:The (pro)renin receptor ([P]RR) is a transmembrane protein that binds both renin and prorenin with high affinity, increasing the catalytic cleavage of angiotensinogen and signaling intracellularly through mitogen-activated protein kinase activation. Although initially reported as having no homology with any known membrane protein, other studies have suggested that the (P)RR is an accessory protein, named ATP6ap2, that associates with the vacuolar H(+)-ATPase, a key mediator of final urinary Acidification. Using in situ hybridization, immunohistochemistry, and electron microscopy, together with serial sections stained with nephron segment-specific markers, we found that (P)RR mRNA and protein were predominantly expressed in collecting ducts and in the distal nephron. Within collecting ducts, the (P)RR was most abundant in microvilli at the apical surface of A-type intercalated Cells. Dual-staining immunofluorescence demonstrated colocalization of the (P)RR with the B1/2 subunit of the vacuolar H(+)-ATPase, the ion exchanger that secretes H(+) ions into the urinary space and that associates with an accessory subunit homologous to the (P)RR. In collecting duct/distal tubule lineage Madin-Darby canine kidney Cells, extracellular signal-regulated kinase 1/2 phosphorylation, induced by either renin or prorenin, was attenuated by the selective vacuolar H(+)-ATPase inhibitor bafilomycin. The predominant expression of the (P)RR at the apex of Acid-Secreting Cells in the collecting duct, along with its colocalization and homology with an accessory protein of the vacuolar H(+)-ATPase, suggests that the (P)RR may function primarily in distal nephron H(+) transport, recently noted to be, at least in part, an angiotensin II-dependent phenomenon.
Noriaki Takeguchi - One of the best experts on this subject based on the ideXlab platform.
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new fluorescent probes e3810 and methoxy e3810 for determining distributions of the apical membrane and the Acidic compartment of gastric Acid Secreting Cells
Japanese Journal of Physiology, 1992Co-Authors: Noriaki Takeguchi, Tsuneaki Yamanouchi, Hideki Sakai, Magotoshi MoriiAbstract:Substituted benzimidazoles such as omeprazole, E3810 and methoxy E3810 were inhibitors of gastric H+, K(+)-ATPase which is rich in the apical membrane of gastric parietal or oxyntic Cells at the Secreting state. The Acid-activated compounds of omeprazole and methoxy E3810, which have methoxy group at the 5-position in the benzimidazole ring, are fluorescent (excitation wavelength = 370 nm; emission wavelength = 560 nm). The fluorescence disappeared when the activated compounds reacted with the ATPase or glutathione. Using this fluorescence property, the distribution of the intracellular Acidic canalicular space in isolated single parietal Cells was determined. On the other hand, irradiation with ultraviolet light (335 nm) of the Acid-activated compound of E3810 which had been reacted with sulfhydryl group of the ATPase or glutathione resulted in a formation of a fluorescent compound (emission = 470 nm). Using this second fluorescence property, we determined the distribution of the apical membrane of the intracellular canaliculus of isolated single mammalian parietal Cells and also the location of the apical membrane on the external surface of newt oxyntic Cells.
