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Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells
by
Moeller, Hanne B.
, Knepper, Mark A.
, Fenton, Robert A.
in
Animals
/ Aquaporin 2 - metabolism
/ Aquaporin 2 - ultrastructure
/ aquaporin water channel
/ Biological and medical sciences
/ Cell Membrane - metabolism
/ Cell Membrane - ultrastructure
/ Clathrin-Coated Vesicles - metabolism
/ Deamino Arginine Vasopressin - metabolism
/ Deamino Arginine Vasopressin - pharmacology
/ endocytosis
/ Endosomes - metabolism
/ Endosomes - ultrastructure
/ exocytosis
/ Immunohistochemistry
/ Kidney Tubules, Collecting - cytology
/ Kidney Tubules, Collecting - metabolism
/ Kidney Tubules, Collecting - ultrastructure
/ Lysosomes - metabolism
/ Lysosomes - ultrastructure
/ Medical sciences
/ Mice
/ Mice, Inbred C57BL
/ Mice, Knockout
/ Nephrology. Urinary tract diseases
/ Peroxidase - immunology
/ Peroxidase - metabolism
/ Phosphorylation
/ Rats
/ Rats, Brattleboro
/ Rats, Wistar
/ Sensitivity and Specificity
/ Serine - metabolism
/ Time Factors
/ vasopressin
2009
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Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells
by
Moeller, Hanne B.
, Knepper, Mark A.
, Fenton, Robert A.
in
Animals
/ Aquaporin 2 - metabolism
/ Aquaporin 2 - ultrastructure
/ aquaporin water channel
/ Biological and medical sciences
/ Cell Membrane - metabolism
/ Cell Membrane - ultrastructure
/ Clathrin-Coated Vesicles - metabolism
/ Deamino Arginine Vasopressin - metabolism
/ Deamino Arginine Vasopressin - pharmacology
/ endocytosis
/ Endosomes - metabolism
/ Endosomes - ultrastructure
/ exocytosis
/ Immunohistochemistry
/ Kidney Tubules, Collecting - cytology
/ Kidney Tubules, Collecting - metabolism
/ Kidney Tubules, Collecting - ultrastructure
/ Lysosomes - metabolism
/ Lysosomes - ultrastructure
/ Medical sciences
/ Mice
/ Mice, Inbred C57BL
/ Mice, Knockout
/ Nephrology. Urinary tract diseases
/ Peroxidase - immunology
/ Peroxidase - metabolism
/ Phosphorylation
/ Rats
/ Rats, Brattleboro
/ Rats, Wistar
/ Sensitivity and Specificity
/ Serine - metabolism
/ Time Factors
/ vasopressin
2009
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Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells
by
Moeller, Hanne B.
, Knepper, Mark A.
, Fenton, Robert A.
in
Animals
/ Aquaporin 2 - metabolism
/ Aquaporin 2 - ultrastructure
/ aquaporin water channel
/ Biological and medical sciences
/ Cell Membrane - metabolism
/ Cell Membrane - ultrastructure
/ Clathrin-Coated Vesicles - metabolism
/ Deamino Arginine Vasopressin - metabolism
/ Deamino Arginine Vasopressin - pharmacology
/ endocytosis
/ Endosomes - metabolism
/ Endosomes - ultrastructure
/ exocytosis
/ Immunohistochemistry
/ Kidney Tubules, Collecting - cytology
/ Kidney Tubules, Collecting - metabolism
/ Kidney Tubules, Collecting - ultrastructure
/ Lysosomes - metabolism
/ Lysosomes - ultrastructure
/ Medical sciences
/ Mice
/ Mice, Inbred C57BL
/ Mice, Knockout
/ Nephrology. Urinary tract diseases
/ Peroxidase - immunology
/ Peroxidase - metabolism
/ Phosphorylation
/ Rats
/ Rats, Brattleboro
/ Rats, Wistar
/ Sensitivity and Specificity
/ Serine - metabolism
/ Time Factors
/ vasopressin
2009
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Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells
Journal Article
Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells
2009
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Overview
Trafficking of the water channel aquaporin-2 to the apical plasma membrane of the collecting duct is mediated by arginine vasopressin, rendering the cell permeable to water. We recently identified a novel form of aquaporin-2 that is phosphorylated at serine-269 (pS269-AQP2). Using antibodies specific for this form of the water channel, we detected rat and mouse pS269-AQP2 in the connecting tubule and throughout the collecting duct system. Using confocal immunofluorescence microscopy with organelle-specific markers and immunogold electron microscopy, we found that pS269-AQP2 was found only on the apical plasma membrane of principal cells. In vasopressin-deficient Brattleboro rats, pS269-AQP2 was undetectable but dramatically increased in abundance after these rats were treated with [deamino-Cys-1, d-Arg-8]vasopressin (dDAVP). This increase occurred only at the apical plasma membrane, even after long-term dDAVP treatment. Following dDAVP there was a time-dependent redistribution of total aquaporin-2 from predominantly intracellular vesicles to the apical plasma membrane, clathrin-coated vesicles, early endosomal compartments, and lysosomes. However, pS269-AQP2 was found only on the apical plasma membrane at any time. Our results show that S269 phosphorylated aquaporin-2 is exclusively associated with the apical plasma membrane, where it escapes endocytosis to remain at the cell surface.
Publisher
Elsevier Inc,Nature Publishing Group,Elsevier Limited
Subject
/ Aquaporin 2 - ultrastructure
/ Biological and medical sciences
/ Cell Membrane - ultrastructure
/ Clathrin-Coated Vesicles - metabolism
/ Deamino Arginine Vasopressin - metabolism
/ Deamino Arginine Vasopressin - pharmacology
/ Kidney Tubules, Collecting - cytology
/ Kidney Tubules, Collecting - metabolism
/ Kidney Tubules, Collecting - ultrastructure
/ Mice
/ Nephrology. Urinary tract diseases
/ Rats
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