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craft-ca-core-ex-dev

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T126M knock-in clearly shows that Aqp2 is an essential gene [18]. The fact that our mice survive shows either that AQP2-F204V possesses some residual water transporting ability or that there are AVP-independent pathways for water reabsorption. Residual activity of AQP2-F204V is likely, as mutant animals show some small response to dDAVP, although dDAVP-stimulated urine osmolality remains quite low. Immunostaining of kidney shows that AQP2-F204V does not efficiently transport water, because it fails to localize to the apical cell surface after dDAVP treatment. Some residual activity of AQP2 would imply that some small, undetectable portion of the mutant protein is getting to the cell surface. The surface biotinylation experiment (Figure 5D) suggests that no mutant protein gets to the surface, but this does not necessarily reflect the situation in vivo. While this small fraction of protein may not be detectable by immunofluorescence, Western blotting shows that some mutant protein does progress beyond the ER (35–45 kDa species in Figure 3A). Compared to wild-type, mutant protein is enriched in the high-mannose, core-glycosylated form (31 kDa) and deficient in nonglycosylated (29 kDa) and complex glycosylated (35–45 kDa) forms. The presence of a reduced but detectable amount of protein in the 35–45 kDa range indicates that mutant protein is transported out of the ER, but with greatly reduced efficiency. Colocalization of AQP2-F204V with the ER protein calnexin in transfected MDCK cells shows that, while most of the mutant protein is trapped in the ER, some does progress beyond the ER. Diminished response to dDAVP, diminished abundance of mature glycosylated protein in mutant animals, and the transport of a fraction of mutant protein beyond the ER in MDCK cells are all consistent with the notion that AQP2-F204V misfolding is limited and that it may retain some residual water transporting activity. Evidently this residual activity is sufficient for the viability and growth of mutant animals."}

craft-ca-core-dev

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The fact that our mice survive shows either that AQP2-F204V possesses some residual water transporting ability or that there are AVP-independent pathways for water reabsorption. Residual activity of AQP2-F204V is likely, as mutant animals show some small response to dDAVP, although dDAVP-stimulated urine osmolality remains quite low. Immunostaining of kidney shows that AQP2-F204V does not efficiently transport water, because it fails to localize to the apical cell surface after dDAVP treatment. Some residual activity of AQP2 would imply that some small, undetectable portion of the mutant protein is getting to the cell surface. The surface biotinylation experiment (Figure 5D) suggests that no mutant protein gets to the surface, but this does not necessarily reflect the situation in vivo. While this small fraction of protein may not be detectable by immunofluorescence, Western blotting shows that some mutant protein does progress beyond the ER (35–45 kDa species in Figure 3A). Compared to wild-type, mutant protein is enriched in the high-mannose, core-glycosylated form (31 kDa) and deficient in nonglycosylated (29 kDa) and complex glycosylated (35–45 kDa) forms. The presence of a reduced but detectable amount of protein in the 35–45 kDa range indicates that mutant protein is transported out of the ER, but with greatly reduced efficiency. Colocalization of AQP2-F204V with the ER protein calnexin in transfected MDCK cells shows that, while most of the mutant protein is trapped in the ER, some does progress beyond the ER. Diminished response to dDAVP, diminished abundance of mature glycosylated protein in mutant animals, and the transport of a fraction of mutant protein beyond the ER in MDCK cells are all consistent with the notion that AQP2-F204V misfolding is limited and that it may retain some residual water transporting activity. Evidently this residual activity is sufficient for the viability and growth of mutant animals."}

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T126M knock-in clearly shows that Aqp2 is an essential gene [18]. The fact that our mice survive shows either that AQP2-F204V possesses some residual water transporting ability or that there are AVP-independent pathways for water reabsorption. Residual activity of AQP2-F204V is likely, as mutant animals show some small response to dDAVP, although dDAVP-stimulated urine osmolality remains quite low. Immunostaining of kidney shows that AQP2-F204V does not efficiently transport water, because it fails to localize to the apical cell surface after dDAVP treatment. Some residual activity of AQP2 would imply that some small, undetectable portion of the mutant protein is getting to the cell surface. The surface biotinylation experiment (Figure 5D) suggests that no mutant protein gets to the surface, but this does not necessarily reflect the situation in vivo. While this small fraction of protein may not be detectable by immunofluorescence, Western blotting shows that some mutant protein does progress beyond the ER (35–45 kDa species in Figure 3A). Compared to wild-type, mutant protein is enriched in the high-mannose, core-glycosylated form (31 kDa) and deficient in nonglycosylated (29 kDa) and complex glycosylated (35–45 kDa) forms. The presence of a reduced but detectable amount of protein in the 35–45 kDa range indicates that mutant protein is transported out of the ER, but with greatly reduced efficiency. Colocalization of AQP2-F204V with the ER protein calnexin in transfected MDCK cells shows that, while most of the mutant protein is trapped in the ER, some does progress beyond the ER. Diminished response to dDAVP, diminished abundance of mature glycosylated protein in mutant animals, and the transport of a fraction of mutant protein beyond the ER in MDCK cells are all consistent with the notion that AQP2-F204V misfolding is limited and that it may retain some residual water transporting activity. Evidently this residual activity is sufficient for the viability and growth of mutant animals."}

2_test

{"project":"2_test","denotations":[{"id":"16121255-11035038-85587803","span":{"begin":65,"end":67},"obj":"11035038"},{"id":"T96150","span":{"begin":65,"end":67},"obj":"11035038"}],"text":"The T126M knock-in clearly shows that Aqp2 is an essential gene [18]. The fact that our mice survive shows either that AQP2-F204V possesses some residual water transporting ability or that there are AVP-independent pathways for water reabsorption. Residual activity of AQP2-F204V is likely, as mutant animals show some small response to dDAVP, although dDAVP-stimulated urine osmolality remains quite low. Immunostaining of kidney shows that AQP2-F204V does not efficiently transport water, because it fails to localize to the apical cell surface after dDAVP treatment. Some residual activity of AQP2 would imply that some small, undetectable portion of the mutant protein is getting to the cell surface. The surface biotinylation experiment (Figure 5D) suggests that no mutant protein gets to the surface, but this does not necessarily reflect the situation in vivo. While this small fraction of protein may not be detectable by immunofluorescence, Western blotting shows that some mutant protein does progress beyond the ER (35–45 kDa species in Figure 3A). Compared to wild-type, mutant protein is enriched in the high-mannose, core-glycosylated form (31 kDa) and deficient in nonglycosylated (29 kDa) and complex glycosylated (35–45 kDa) forms. The presence of a reduced but detectable amount of protein in the 35–45 kDa range indicates that mutant protein is transported out of the ER, but with greatly reduced efficiency. Colocalization of AQP2-F204V with the ER protein calnexin in transfected MDCK cells shows that, while most of the mutant protein is trapped in the ER, some does progress beyond the ER. Diminished response to dDAVP, diminished abundance of mature glycosylated protein in mutant animals, and the transport of a fraction of mutant protein beyond the ER in MDCK cells are all consistent with the notion that AQP2-F204V misfolding is limited and that it may retain some residual water transporting activity. Evidently this residual activity is sufficient for the viability and growth of mutant animals."}