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as well as others, have proposed Abcg5/sterolin-1 and Abcg8/sterolin-2 to function as obligate heterodimers. Thus knocking out Abcg8/sterolin-2 alone is equivalent to a functional loss of both sterolins. It has been shown that Abcg8/sterolin-2 expression is required for correct apical trafficking of Abcg5/sterolin-1 to the apical surface in a polarized cell line and more recently in vivo by over-expression experiments [18,19]. In experiments shown here, using three separately developed anti-Abcg5/sterolin-1 antibodies, we have obtained inconsistent data regarding the trafficking of Abcg5/sterolin-1 in Abcg8-/- mice. Based upon classical N-glycosylation maturation it would appear that Abcg5/sterolin-1, in the Abcg8-/- mice, does not exit the endoplasmic reticulum. However, by immunohistochemistry it appears that Abcg5/sterolin-1 is apically expressed in the Abcg8-deficient mice regardless of the anti-Abcg5/sterolin-1 antibody used. Interestingly, in a report of Abcg5/Abcg8 localization in canine gallbladder epithelial cells, these two proteins were found intracellularly under baseline conditions [44]. But when given liver X receptor alpha (LXRα) agonist, Abcg5/sterolin-1 and Abcg8/sterolin-2 appeared to be expressed at the apical surface. In these studies the UTSW anti-Abcg5/sterolin-1 antibody was used. It is apparent with these conflicting data that the trafficking of these transporters is not as clear-cut. In a recent paper, Mangrivite et al. showed that the apical sorting of rat SPNT in polarized renal epithelial cells was independent of N-glycosylation [45]. Therefore, at this time, we can neither exclude the possibility that Abcg5/sterolin-1 expression is functional in our Abcg8/sterolin-2 deficient mice nor can we rule it out. We have no functional assay for these proteins at present. More extensive fractionation experiments are underway to better determine the exact compartmental location of Abcg5/sterolin-1 in the Abcg8-/- mice. In this context, Plösch et al. have described an Abcg5/sterolin-1 deficient mouse that maintains the ability to secrete biliary cholesterol to the same extent as the wild-type mice and, when fed a LXR agonist, had higher Abcg8 mRNA expression and tended to secrete more biliary cholesterol than wild-type mice [46]. It has been argued that Abcg5/sterolin-1 and Abcg8/sterolin-2 are dependent upon each other for secretion of hepatic sterols into bile [19]. Given the data presented here and from the Abcg5-deficient mouse this does not appear to be the case. Perhaps in the previously published model a non-physiologic state has been made that generates these data. Taken together, these animal models suggest that Abcg5/sterolin-1 and Abcg8/sterolin-2 have independent function in vivo or that there are proteins other than the sterolins that can secrete biliary sterols."}

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as well as others, have proposed Abcg5/sterolin-1 and Abcg8/sterolin-2 to function as obligate heterodimers. Thus knocking out Abcg8/sterolin-2 alone is equivalent to a functional loss of both sterolins. It has been shown that Abcg8/sterolin-2 expression is required for correct apical trafficking of Abcg5/sterolin-1 to the apical surface in a polarized cell line and more recently in vivo by over-expression experiments [18,19]. In experiments shown here, using three separately developed anti-Abcg5/sterolin-1 antibodies, we have obtained inconsistent data regarding the trafficking of Abcg5/sterolin-1 in Abcg8-/- mice. Based upon classical N-glycosylation maturation it would appear that Abcg5/sterolin-1, in the Abcg8-/- mice, does not exit the endoplasmic reticulum. However, by immunohistochemistry it appears that Abcg5/sterolin-1 is apically expressed in the Abcg8-deficient mice regardless of the anti-Abcg5/sterolin-1 antibody used. Interestingly, in a report of Abcg5/Abcg8 localization in canine gallbladder epithelial cells, these two proteins were found intracellularly under baseline conditions [44]. But when given liver X receptor alpha (LXRα) agonist, Abcg5/sterolin-1 and Abcg8/sterolin-2 appeared to be expressed at the apical surface. In these studies the UTSW anti-Abcg5/sterolin-1 antibody was used. It is apparent with these conflicting data that the trafficking of these transporters is not as clear-cut. In a recent paper, Mangrivite et al. showed that the apical sorting of rat SPNT in polarized renal epithelial cells was independent of N-glycosylation [45]. Therefore, at this time, we can neither exclude the possibility that Abcg5/sterolin-1 expression is functional in our Abcg8/sterolin-2 deficient mice nor can we rule it out. We have no functional assay for these proteins at present. More extensive fractionation experiments are underway to better determine the exact compartmental location of Abcg5/sterolin-1 in the Abcg8-/- mice. In this context, Plösch et al. have described an Abcg5/sterolin-1 deficient mouse that maintains the ability to secrete biliary cholesterol to the same extent as the wild-type mice and, when fed a LXR agonist, had higher Abcg8 mRNA expression and tended to secrete more biliary cholesterol than wild-type mice [46]. It has been argued that Abcg5/sterolin-1 and Abcg8/sterolin-2 are dependent upon each other for secretion of hepatic sterols into bile [19]. Given the data presented here and from the Abcg5-deficient mouse this does not appear to be the case. Perhaps in the previously published model a non-physiologic state has been made that generates these data. Taken together, these animal models suggest that Abcg5/sterolin-1 and Abcg8/sterolin-2 have independent function in vivo or that there are proteins other than the sterolins that can secrete biliary sterols."}

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as well as others, have proposed Abcg5/sterolin-1 and Abcg8/sterolin-2 to function as obligate heterodimers. Thus knocking out Abcg8/sterolin-2 alone is equivalent to a functional loss of both sterolins. It has been shown that Abcg8/sterolin-2 expression is required for correct apical trafficking of Abcg5/sterolin-1 to the apical surface in a polarized cell line and more recently in vivo by over-expression experiments [18,19]. In experiments shown here, using three separately developed anti-Abcg5/sterolin-1 antibodies, we have obtained inconsistent data regarding the trafficking of Abcg5/sterolin-1 in Abcg8-/- mice. Based upon classical N-glycosylation maturation it would appear that Abcg5/sterolin-1, in the Abcg8-/- mice, does not exit the endoplasmic reticulum. However, by immunohistochemistry it appears that Abcg5/sterolin-1 is apically expressed in the Abcg8-deficient mice regardless of the anti-Abcg5/sterolin-1 antibody used. Interestingly, in a report of Abcg5/Abcg8 localization in canine gallbladder epithelial cells, these two proteins were found intracellularly under baseline conditions [44]. But when given liver X receptor alpha (LXRα) agonist, Abcg5/sterolin-1 and Abcg8/sterolin-2 appeared to be expressed at the apical surface. In these studies the UTSW anti-Abcg5/sterolin-1 antibody was used. It is apparent with these conflicting data that the trafficking of these transporters is not as clear-cut. In a recent paper, Mangrivite et al. showed that the apical sorting of rat SPNT in polarized renal epithelial cells was independent of N-glycosylation [45]. Therefore, at this time, we can neither exclude the possibility that Abcg5/sterolin-1 expression is functional in our Abcg8/sterolin-2 deficient mice nor can we rule it out. We have no functional assay for these proteins at present. More extensive fractionation experiments are underway to better determine the exact compartmental location of Abcg5/sterolin-1 in the Abcg8-/- mice. In this context, Plösch et al. have described an Abcg5/sterolin-1 deficient mouse that maintains the ability to secrete biliary cholesterol to the same extent as the wild-type mice and, when fed a LXR agonist, had higher Abcg8 mRNA expression and tended to secrete more biliary cholesterol than wild-type mice [46]. It has been argued that Abcg5/sterolin-1 and Abcg8/sterolin-2 are dependent upon each other for secretion of hepatic sterols into bile [19]. Given the data presented here and from the Abcg5-deficient mouse this does not appear to be the case. Perhaps in the previously published model a non-physiologic state has been made that generates these data. Taken together, these animal models suggest that Abcg5/sterolin-1 and Abcg8/sterolin-2 have independent function in vivo or that there are proteins other than the sterolins that can secrete biliary sterols."}

{"project":"2_test","denotations":[{"id":"15040800-12208867-12037323","span":{"begin":427,"end":429},"obj":"12208867"},{"id":"15040800-14504269-12037324","span":{"begin":430,"end":432},"obj":"14504269"},{"id":"15040800-12878214-12037325","span":{"begin":1117,"end":1119},"obj":"12878214"},{"id":"15040800-12636174-12037326","span":{"begin":1588,"end":1590},"obj":"12636174"},{"id":"15040800-14699507-12037327","span":{"begin":2286,"end":2288},"obj":"14699507"},{"id":"15040800-14504269-12037328","span":{"begin":2427,"end":2429},"obj":"14504269"}],"text":"We, as well as others, have proposed Abcg5/sterolin-1 and Abcg8/sterolin-2 to function as obligate heterodimers. Thus knocking out Abcg8/sterolin-2 alone is equivalent to a functional loss of both sterolins. It has been shown that Abcg8/sterolin-2 expression is required for correct apical trafficking of Abcg5/sterolin-1 to the apical surface in a polarized cell line and more recently in vivo by over-expression experiments [18,19]. In experiments shown here, using three separately developed anti-Abcg5/sterolin-1 antibodies, we have obtained inconsistent data regarding the trafficking of Abcg5/sterolin-1 in Abcg8-/- mice. Based upon classical N-glycosylation maturation it would appear that Abcg5/sterolin-1, in the Abcg8-/- mice, does not exit the endoplasmic reticulum. However, by immunohistochemistry it appears that Abcg5/sterolin-1 is apically expressed in the Abcg8-deficient mice regardless of the anti-Abcg5/sterolin-1 antibody used. Interestingly, in a report of Abcg5/Abcg8 localization in canine gallbladder epithelial cells, these two proteins were found intracellularly under baseline conditions [44]. But when given liver X receptor alpha (LXRα) agonist, Abcg5/sterolin-1 and Abcg8/sterolin-2 appeared to be expressed at the apical surface. In these studies the UTSW anti-Abcg5/sterolin-1 antibody was used. It is apparent with these conflicting data that the trafficking of these transporters is not as clear-cut. In a recent paper, Mangrivite et al. showed that the apical sorting of rat SPNT in polarized renal epithelial cells was independent of N-glycosylation [45]. Therefore, at this time, we can neither exclude the possibility that Abcg5/sterolin-1 expression is functional in our Abcg8/sterolin-2 deficient mice nor can we rule it out. We have no functional assay for these proteins at present. More extensive fractionation experiments are underway to better determine the exact compartmental location of Abcg5/sterolin-1 in the Abcg8-/- mice. In this context, Plösch et al. have described an Abcg5/sterolin-1 deficient mouse that maintains the ability to secrete biliary cholesterol to the same extent as the wild-type mice and, when fed a LXR agonist, had higher Abcg8 mRNA expression and tended to secrete more biliary cholesterol than wild-type mice [46]. It has been argued that Abcg5/sterolin-1 and Abcg8/sterolin-2 are dependent upon each other for secretion of hepatic sterols into bile [19]. Given the data presented here and from the Abcg5-deficient mouse this does not appear to be the case. Perhaps in the previously published model a non-physiologic state has been made that generates these data. Taken together, these animal models suggest that Abcg5/sterolin-1 and Abcg8/sterolin-2 have independent function in vivo or that there are proteins other than the sterolins that can secrete biliary sterols."}