Tubulin is retained throughout the human hematopoietic/erythroid cell differentiation process and plays a structural role in sedimentable fraction of mature erythrocytes

Nigra, Ayelén D.; Santander, Verónica S.; Dircio-Maldonado, Roberto; Amaiden, Marina R.; Monesterolo, Noelia E.; Flores-Guzmán, Patricia; Muhlberger, Tamara; Rivelli, Juan F.; Campetelli, Alexis N.; Mayani, Héctor; Casale, César H.

doi:10.1016/j.biocel.2017.08.012

Cited by 6 publications

(13 citation statements)

References 30 publications

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“…Fluorescence corresponding to tubulin was observed in these cells in the form of a thin peripheral ring, because the cells were small, with very low activity and little cytoplasm. Hemoglobin was absent at this stage [34]. No distinction was made in this work between BFU-E or CFU-E (Table 1).…”

Section: Erythrocytementioning

confidence: 54%

“…In steady-state erythropoiesis, differentiation of erythroid progenitors involves the synthesis and expression of major cytoskeletal proteins found in the human erythrocyte membrane. These changes are progressive and can be [29], [30], [31], [34].…”

Section: Erythropoiesis and Changes In The Skeleton Componentsmentioning

confidence: 99%

“…Pro-erythroblast Low levels of components of the membrane skeleton, αand βspectrin, adducin, and tropomodulin. High levels of actin and presence of a well-defined typical microtubule network [30], [34], [41], [42].…”

Section: Erythropoiesis and Changes In The Skeleton Componentsmentioning

confidence: 99%

“…As in the case of progenitors, few studies have reported on the presence and function of cytoskeleton tubulin in erythroblasts. Nigra et al [34] reported that 1 3 tubulin undergoes rearrangements during erythropoiesis in proerythroblasts, which have an active metabolism. Tubulin was observed as a well-defined typical microtubule network, but while differentiation continued, the microtubules were restructured.…”

Section: Erythrocytementioning

confidence: 99%

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Human erythrocytes: cytoskeleton and its origin

Nigra

Casale

Santander

2019

Cell. Mol. Life Sci.

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Section: Erythrocytementioning

confidence: 54%

Section: Erythropoiesis and Changes In The Skeleton Componentsmentioning

confidence: 99%

Section: Erythropoiesis and Changes In The Skeleton Componentsmentioning

confidence: 99%

Section: Erythrocytementioning

confidence: 99%

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Human erythrocytes: cytoskeleton and its origin

Nigra

Casale

Santander

2019

Cell. Mol. Life Sci.

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“…Specialized tissue processing and fixation requirements for microtubule visualization precluded confirmatory studies on patient marrow samples. However, prior studies have shown that freshly obtained human peripheral red blood cells (RBC) retain remnant microtubule fragments that are disrupted by the microtubule destabilizer nocodazole [30][31][32][33] . IF for β-tubulin on RBC from non-anemic control patients confirmed the previously described pancellular stippling in the majority (>80%) of cells.…”

Section: Resultsmentioning

confidence: 99%

Iron control of erythroid microtubule cytoskeleton as a potential target in treatment of iron-restricted anemia

et al. 2021

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Anemias of chronic disease and inflammation (ACDI) result from restricted iron delivery to erythroid progenitors. The current studies reveal an organellar response in erythroid iron restriction consisting of disassembly of the microtubule cytoskeleton and associated Golgi disruption. Isocitrate supplementation, known to abrogate the erythroid iron restriction response, induces reassembly of microtubules and Golgi in iron deprived progenitors. Ferritin, based on proteomic profiles, regulation by iron and isocitrate, and putative interaction with microtubules, is assessed as a candidate mediator. Knockdown of ferritin heavy chain (FTH1) in iron replete progenitors induces microtubule collapse and erythropoietic blockade; conversely, enforced ferritin expression rescues erythroid differentiation under conditions of iron restriction. Fumarate, a known ferritin inducer, synergizes with isocitrate in reversing molecular and cellular defects of iron restriction and in oral remediation of murine anemia. These findings identify a cytoskeletal component of erythroid iron restriction and demonstrate potential for its therapeutic targeting in ACDI.

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