A Caltech Library Service

Synemin and Vimentin are Components of Intermediate Filaments in Avian Erythrocytes

Granger, Bruce L. and Repasky, Elizabeth A. and Lazarides, Elias (1982) Synemin and Vimentin are Components of Intermediate Filaments in Avian Erythrocytes. Journal of Cell Biology, 92 (2). pp. 299-312. ISSN 0021-9525. PMCID PMC2112073. doi:10.1083/jcb.92.2.299.

PDF - Published Version
See Usage Policy.


Use this Persistent URL to link to this item:


Synemin, a high-molecular-weight protein associated with intermediate filaments in muscle, and vimentin, an intermediate-filament subunit found in many different cell types, have been identified by immunologic and electrophoretic criteria as components of intermediate filaments in mature avian erythrocytes. Desmin, the predominant subunit of intermediate filaments in muscle, has not been detected in these cells. Two dimensional immunoautoradiography of proteolytic fragments of synemin and vimentin demonstates that the erythrocyte proteins are highly homologous, if not identical, to their muscle counterparts. Double immunoflurorescence reaveals that erythrocyte synemin and vimentin co-localize in a cytoplasmic network of sinuous filaments that extends from the nucleus to the plasma membrane and resists aggregation by colcemid. Erythrocytes that are attached to glass cover slips can be sonicated to remove nuclei and nonadherent regions of the plasma membrane; this leaves elliptical patches of adherent membrane that retain mats of vimentin- and synemin-containing intermediate filaments, as seen by immunofluorescence and rotary shadowing. Similarly, mechanical enucleation of erythrocyte ghosts in suspension allows isolation of plasma membranes that retain a significant fraction of the synemin and vimentin, as assayed by electrophoresis, and intermediate filaments, as seen in thin sections. Both synemin and vimentin remain insoluble along with spectrin and actin, in solutions containing nonionic detergent and high salt. However, brief exposure of isolated membrane to distilled water releases the synemin and vimentin together in nearly pure form, before the release of significant amounts of spectrin and actin. These data suggest that avian erythrocyte intermeditate filaments are somehow anchored to the plasma membrane; erythrocytes may thus provide a simple system for the study of intermediate filaments and their mode of interaction with membranes. In addition, these data, in conjunction with previous data from muscle, indicate that synemin is capable of associating with either desmin or vimentin and may thus perform a special role in the structure or function of intermediate filaments in erythrocytes as well as muscle.

Item Type:Article
Related URLs:
URLURL TypeDescription CentralArticle
Additional Information:© 1982 Rockefeller University Press. Received for publication 13 July 1981, and in revised form 5 October 1981. We thank David L. Gard for his helpful comments on the manuscript, and Dr. Jean-Paul Revel and Mr. Patrick F. Koen for their help with the electron microscopy. This work was supported by grants from the National Institutes of Health (NIH) (GM 06965), National Science Foundation, Muscular Dystrophy Association of America, and a Biomedical Research Support Grant to the Division of Biology, California Institute of Technology. B. L. Granger was also supported by a Predoctoral Training Grant from the NIH (GM 07616), and E. A. Repasky by a Postdoctoral Fellowship from the NIH (GM 07401). E. Lazarides is the recipient of a Research Career Development Award from the NIH.
Funding AgencyGrant Number
NIHGM 06965
Muscular Dystrophy Association of AmericaUNSPECIFIED
NIH Predoctoral FellowshipGM 07616
NIH Postdoctoral FellowshipGM 07401
Issue or Number:2
PubMed Central ID:PMC2112073
Record Number:CaltechAUTHORS:20120717-091937618
Persistent URL:
Official Citation:Synemin and vimentin are components of intermediate filaments in avian erythrocytes BL Granger, EA Repasky, and E Lazarides 92:299-312. doi:10.1083/jcb.92.2.299
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:32506
Deposited By: Ruth Sustaita
Deposited On:17 Jul 2012 16:41
Last Modified:09 Nov 2021 21:27

Repository Staff Only: item control page