“…63 Studies of definitive erythroid progenitors have shown that cytoskeletal components such as actin and spectrin [64][65][66] are partitioned into reticulocytes after the vimentin-based microfilaments are degraded, allowing the nucleus to move freely about the cell. 64 The expelled nuclei are encapsulated by a thin membrane into which cell-surface molecules such as glycophorin A and phosphatidylserine are selectively partitioned.…”
Section: Enucleation Of Eryp Is Accompanied By Changes In Surface Antmentioning
“…63 Studies of definitive erythroid progenitors have shown that cytoskeletal components such as actin and spectrin [64][65][66] are partitioned into reticulocytes after the vimentin-based microfilaments are degraded, allowing the nucleus to move freely about the cell. 64 The expelled nuclei are encapsulated by a thin membrane into which cell-surface molecules such as glycophorin A and phosphatidylserine are selectively partitioned.…”
Section: Enucleation Of Eryp Is Accompanied By Changes In Surface Antmentioning
“…F-actin is a major component of the cytoskeleton of every cell type and it also has specific functions in erythroid cells, forming the basis of the contractile ring that mediates erythroid cell enucleation 31,32 and the basis of the mature RBC cytoskeleton. The enucleation and mature cytoskeleton defect of Sox6 Ϫ/Ϫ erythroid cells therefore prompted us to test whether these cells were F-actin deficient.…”
Section: Sox6 Facilitates Erythroid Cell Maturation At Least In Part mentioning
“…Precise identification of each band was not possible. Immunohistochemical study was carried out using a Vectastain ABC kit PK-6200 (Vector Laboratories, Burlingame, CA) as previously described [14]. The reaction was visualized with the peroxidase substrate kit DAB SK-4100 (Vector Laboratories).…”
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