A Caltech Library Service

Analysis of desmin and vimentin phosphopeptides in cultured avian myogenic cells and their modulation by 8-bromo-adenosine 3',5'-cyclic monophosphate

Gard, David L. and Lazarides, Elias (1982) Analysis of desmin and vimentin phosphopeptides in cultured avian myogenic cells and their modulation by 8-bromo-adenosine 3',5'-cyclic monophosphate. Proceedings of the National Academy of Sciences of the United States of America, 79 (22). pp. 6912-6916. ISSN 0027-8424.

PDF - Published Version
See Usage Policy.


Use this Persistent URL to link to this item:


The intermediate filament proteins desmin and vimentin are two of the major 32P phosphate acceptors in chicken myotubes differentiating in tissue culture. Analysis of the desmin and vimentin phosphopeptides by two-dimensional tryptic peptide mapping shows that both proteins are phosphorylated at multiple sites, giving rise to 5 phosphopeptides in desmin and as many as 11 in vimentin. Addition of the cAMP analogue 8-bromoadenosine 3',5'-cyclic monophosphate (8-BrcAMP) to the culture medium of mature (8-day-old) myotubes results in a 2- to 3-fold increase in PO4 incorporation into desmin and vimentin. Two-dimensional tryptic analysis of desmin and vimentin from 8-BrcAMP-treated myotubes shows increased 32PO4 incorporation into a subset of the phosphopeptides observed in control cells. Comparison of phosphopeptides from the two proteins shows the presence of at least three comigrating peptides. All three comigrating peptides exhibit cAMP-dependent increases in 32PO4 incorporation in vimentin, while only two of the three exhibit 8-BrcAMP-dependent responses in desmin. While these peptides are the only two that are sensitive to 8-BrcAMP in desmin, vimentin contains additional peptides that exhibit increased 32PO4 incorporation in response to 8-BrcAMP. This result suggests the existence of both common and distinct phosphorylation sites between desmin and vimentin that may be differentially regulated by cAMP. Thus, desmin and vimentin, even though structurally related, may be capable of responding differently to physiological stimuli.

Item Type:Article
Related URLs:
URLURL TypeDescription
Additional Information:Copyright ©1982 by the National Academy of Sciences. Communicated by James Bonner, August 24, 1982. We thank Ilge Lielausis for her expert technical assistance with tissue culture and Chung Wang, John Ngai, Spencer Danto, Bruce Granger, and Jim Nelson for helpful discussions. This work was supported by grants from the National Institutes of Health, the National Science Foundation, and the Muscular Dystrophy Association of America. E.L. is a recipient of a Research Career Development Award from the National Institutes of Health. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Subject Keywords:intermediate filament; skeletal muscle; tryptic peptide analysis
Issue or Number:22
Record Number:CaltechAUTHORS:GARpnas82
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:11303
Deposited By: Archive Administrator
Deposited On:29 Jul 2008 23:30
Last Modified:03 Oct 2019 00:17

Repository Staff Only: item control page