Hinssen, Horst and Vandekerckhove, Joel and Lazarides, Elias (1987) Gelsolin is expressed in early erythroid progenitor cells and negatively regulated during erythropoiesis. Journal of Cell Biology, 105 (3). pp. 1425-1433. ISSN 0021-9525. http://resolver.caltech.edu/CaltechAUTHORS:HINjcb87
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We have identified an approximately 85-kD protein in chicken erythrocytes which is immunologically, structurally, and functionally related to the gelsolin found in many muscle and nonmuscle cell types. Cell fractionation reveals a Ca2+-dependent partitioning of gelsolin into the soluble cytoplasm and the membrane-associated cytoskeleton of differentiating or mature erythrocytes. Depending on either the presence of Ca2+ during cell lysis or on the preincubation of the intact cells with the Ca2+-ionophore A23187, up to 40% of the total cellular gelsolin is found associated with the membrane skeleton. Expression of gelsolin shows a strong negative regulation during erythroid differentiation. From quantitations of its steady-state molar ratio to actin, gelsolin is abundant in early progenitor cells as revealed from avian erythroblastosis virus- and S13 virus-transformed cells which are arrested at the colony forming unit erythroid (CFU-e) stage of erythroid development. In these cells, which have a rudimentary and unstable membrane skeleton, gelsolin remains quantitatively cytoplasmic, irrespective of the Ca2+ concentration. During chicken embryo development and maturation, the expression of gelsolin decreases by a factor of approximately 10(3) in erythroid cells. This down regulation is independent from that of actin, which is considerably less, and is observed also when S13-transformed erythroid progenitor cells are induced to differentiate under conditions where the actin content of these cells does not change. In mature erythrocytes of the adult the amount of gelsolin is low, and significantly less than required for potentially capping of all membrane-associated actin filaments. We suggest that the gelsolin in erythroid cells is involved in the assembly of the actin filaments present in the membrane skeleton, and that it may provide for a mechanism, by means of its severing action on actin filaments, to extend the meshwork of the spectrin-actin-based membrane skeleton in erythroid cells during erythropoiesis.
|Additional Information:||Copyright © 1987 by The Rockefeller University Press. RUP grants the public the non-exclusive right to copy, distribute, or display the Work under a Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ and http://creativecommons.org/licenses/by-nc-sa/3.0/legalcode. Received for publication 25 March 1987, and in revised form 5 May 1987. We are grateful to Dr. Peter K. Vogt, Department of Microbiology, University of Southern California School of Medicine, for providing us with the AEV cells and S13 virus-transformed cells. We are also grateful to Chantal Champagne for determining the site of homology between this protein and human plasma gelsolin. This work was supported by grants from the National Institutes of Health (AG 06078A and HL 35801A) and Muscular Dystrophy Association. H. Hinssen was supported by a Heisenberg Fellowship from the Deutsche Forschungsgemeinschaft.|
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