Novel roles for erythroid Ankyrin-1 revealed through an ENU-induced null mouse mutant

Rank, Gerhard; Sutton, Rosemary; Marshall, Vikki M.; Lundie, Rachel J.; Caddy, Jacinta; Romeo, Tony; Fernandez, Kate Marie; McCormack, Matthew P.; Cooke, Brian M.; Foote, Simon J.; Crabb, Brendan S.; Curtis, David J.; Hilton, Douglas J.; Kile, Benjamin T.; Jane, Stephen M.

doi:10.1182/blood-2008-08-172841

Cited by 44 publications

(69 citation statements)

References 44 publications

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“…Interestingly, miR-486 is located within the last intron of the ankyrin gene (ANK-1), an integral red cell-membrane cytoskeletal protein. 25 Previous studies have shown that GATA-1 binds and regulates the ANK-1 promoter. 26 Although not directly shown, these findings suggest that miR-486 may be regulated by GATA1 binding to the ANK-1 promoter.…”

Section: Discussionmentioning

confidence: 99%

MicroRNA-486 regulates normal erythropoiesis and enhances growth and modulates drug response in CML progenitors

Wang

et al. 2015

Blood

131

101

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Section: Discussionmentioning

confidence: 99%

MicroRNA-486 regulates normal erythropoiesis and enhances growth and modulates drug response in CML progenitors

Wang

et al. 2015

Blood

131

101

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“…Reduced expression of the ankyrin binding proteins band 3 and protein 4.2 has been noted in these patients, [13][14][15] and in murine models of ankyrin deficient HS, secondary protein deficiencies of GPA, protein 4.2 and Rh, but not band 3 or GPC, were observed. 16 However, more extensive characterization of the membrane protein composition in humans, including the effect on RhAG and other putative ankyrin associated proteins, is so far lacking.…”

Section: Introductionmentioning

confidence: 99%

Severe Ankyrin-R deficiency results in impaired surface retention and lysosomal degradation of RhAG in human erythroblasts

et al. 2016

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“…40,41 However, an earlier simultaneous expression profile is in keeping with the known dependence of protein 4.2 on band 3 expression. 8,[10][11][12] The level and association of band 3 and protein 4.2 remains constant after 72h (normoblast stage) suggesting that the majority of protein 4.2 may already be associated with band 3 early in differentiation.…”

Section: Protein 42 Is Expressed Simultaneous To Band 3 During Erythmentioning

confidence: 99%

Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2)

Akker¹,

Satchwell²,

Pellegrin³

et al. 2010

Haematologica

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The online version of this article has a Supplementary Appendix. BackgroundProtein 4.2 deficiency caused by mutations in the EPB42 gene results in hereditary spherocytosis with characteristic alterations of CD47, CD44 and RhAG. We decided to investigate at which stage of erythropoiesis these hallmarks of protein 4.2 deficiency arise in a novel protein 4.2 patient and whether they cause disruption to the band 3 macrocomplex. Design and MethodsWe used immunoprecipitations and detergent extractability to assess the strength of protein associations within the band 3 macrocomplex and with the cytoskeleton in erythrocytes. Patient erythroblasts were cultured from peripheral blood mononuclear cells to study the effects of protein 4.2 deficiency during erythropoiesis. ResultsWe report a patient with two novel mutations in EPB42 resulting in complete protein 4.2 deficiency. Immunoprecipitations revealed a weakened ankyrin-1-band 3 interaction in erythrocytes resulting in increased band 3 detergent extractability. CD44 abundance and its association with the cytoskeleton were increased. Erythroblast differentiation revealed that protein 4.2 and band 3 appear simultaneously and associate early in differentiation. Protein 4.2 deficiency results in lower CD47, higher CD44 expression and increased RhAG glycosylation starting from the basophilic stage. The normal downregulation of CD44 expression was not seen during protein 4.2(-) erythroblast differentiation. Knockdown of CD47 did not increase CD44 expression, arguing against a direct reciprocal relationship. ConclusionsWe have established that the characteristic changes caused by protein 4.2 deficiency occur early during erythropoiesis. We postulate that weakening of the ankyrin-1-band 3 association during protein 4.2 deficiency is compensated, in part, by increased CD44-cytoskeleton binding.

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Novel roles for erythroid Ankyrin-1 revealed through an ENU-induced null mouse mutant

Cited by 44 publications

References 44 publications

MicroRNA-486 regulates normal erythropoiesis and enhances growth and modulates drug response in CML progenitors

MicroRNA-486 regulates normal erythropoiesis and enhances growth and modulates drug response in CML progenitors

Severe Ankyrin-R deficiency results in impaired surface retention and lysosomal degradation of RhAG in human erythroblasts

Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2)

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