Transformation by Rous sarcoma virus (RSV) has been reported to block the expression of differentiated cell products in chicken cells. The expression of these proteins may or may not be suppressed when temperature-sensitive mutants are shifted from the nonpermissive to the permissive temperature. A general characteristic of cellular transformation is the disruption of the microfilament system. In passaged chick embryo fibroblast cultures (CEF), this system is principally composed of isomeric forms of actin designated alpha, beta, and gamma by their isoelectric focusing and when subjected to SDS-PAGE behavior. We present evidence that an alpha-actin in CEF cultures, identified by its electrofocusing behavior, retention in the cytoskeleton, and DNase 1 binding properties, is selectively and dramatically reduced in amount upon transformation by RSV. Little or no reduction is observed in the beta- and gamma-isoactins. The reduction of alpha-actin is shown to be reversible and transformation related by use of a temperature-sensitive mutant, tsNY68. The decrease in this transformation-sensitive isoactin is apparently due to a decrease in synthesis, though other possibilities are discussed. A specific decrease in a particular isoactin after transformation may give insight into the mechanism by which the microfilaments are normally maintained.
Skip Nav Destination
Article navigation
1 June 1983
Article|
June 01 1983
Transformation-sensitive isoactin in passaged chick embryo fibroblasts transformed by Rous sarcoma virus.
D P Witt
D J Brown
J A Gordon
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1983) 96 (6): 1766–1771.
Citation
D P Witt, D J Brown, J A Gordon; Transformation-sensitive isoactin in passaged chick embryo fibroblasts transformed by Rous sarcoma virus.. J Cell Biol 1 June 1983; 96 (6): 1766–1771. doi: https://doi.org/10.1083/jcb.96.6.1766
Download citation file:
Sign in
Don't already have an account? Register
Client Account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Sign in via your Institution
Sign in via your InstitutionSuggested Content
Email alerts
Advertisement
Advertisement