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Blood, 15 September 2005, Vol. 106, No. 6, pp. 2200-2205. Prepublished online as a Blood First Edition Paper on June 2, 2005; DOI 10.1182/blood-2005-04-1357. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-04-1357v1 106/6/2200    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Krauss, S. W. Articles by Chasis, J. A. Search for Related Content PubMed PubMed Citation Articles by Krauss, S. W. Articles by Chasis, J. A. Related Collections Hematopoiesis and Stem Cells Red Cells Apoptosis Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS Nuclear substructure reorganization during late-stage erythropoiesis is selective and does not involve caspase cleavage of major nuclear substructural proteins Sharon Wald Krauss, Annie J. Lo, Sarah A. Short, Mark J. Koury, Narla Mohandas, and Joel Anne Chasis From the Life Sciences Division, University of California Lawrence Berkeley National Laboratory, Berkeley CA; the Vanderbilt University, VA Tennessee Valley Healthcare System, Nashville, TN; and The New York Blood Center, New York, NY. Enucleation, a rare feature of mammalian differentiation, occurs in 3 cell types: erythroblasts, lens epithelium, and keratinocytes. Previous investigations suggest that caspase activation functions in lens epithelial and keratinocyte enucleation, as well as in early erythropoiesis encompassing erythroid burst-forming unit (BFU-E) differentiation to proerythroblast. To determine whether caspase activation contributes to later erythropoiesis and whether nuclear substructures other than chromatin reorganize, we analyzed distributions of nuclear subcompartment proteins and assayed for caspase-induced cleavage of subcompartmental target proteins in mouse erythroblasts. We found that patterns of lamin B in the filamentous network interacting with both the nuclear envelope and DNA, nuclear matrix protein NuMA (Nuclear mitotic apparatus), and splicing factors Sm and SC35 persisted during nuclear condensation, consistent with effective transcription of genes expressed late in differentiation. Thus, nuclear reorganization prior to enucleation is selective, allowing maintenance of critical transcriptional processes independent of extensive chromosomal reorganization. Consistent with these data, we found no evidence for caspase-induced cleavage of major nuclear subcompartment proteins during late erythropoiesis, in contrast to what has been observed in early erythropoiesis and in lens epithelial and keratinocyte differentiation. These findings imply that nuclear condensation and extrusion during terminal erythroid differentiation involve novel mechanisms that do not entail major activation of apoptotic machinery. (Blood. 2005;106:2200-2205) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: To condense is not to die James Palis Blood 2005 106: 1900. [Full Text] [PDF] This article has been cited by other articles: Y. E. Choi, M. Butterworth, S. Malladi, C. S. Duckett, G. M. Cohen, and S. B. 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