scholarly journals Early appearance of desmin, the muscle-type intermediate filament protein, in the rat embryo.

1984 ◽  
Vol 32 (5) ◽  
pp. 473-476 ◽  
Author(s):  
A Bignami ◽  
D Dahl

Antisera raised to desmin, the protein subunit of muscle-type intermediate filaments (IFs), were used to study by indirect immunofluorescence and immunoperoxidase procedures the early development of skeletal muscle in the rat embryo. The specificity of the antisera (Dahl D, Bignami A: J Histochem Cytochem 30:207, 1982) was confirmed by immune blotting on chicken gizzard extracts and purified antigen. Desmin-positive cells were first observed on day 12 by immunofluorescence and on day 13 by the immunoperoxidase procedure. Desmin immunoreactivity was not found in caudal somites in which the dermatome was present, i.e., somites where the dorso-lateral part had maintained its definite boundaries and epithelioid characteristics. Desmin-positive cells were observed within the myotome of cranial somites where the dermatome had disappeared. Compared to day 13, desmin-positive cells had extended ventrally on day 14, while on day 15, they were found in the skeletal musculature of the trunk and the limbs.

1981 ◽  
Vol 90 (3) ◽  
pp. 803-808 ◽  
Author(s):  
E T Browning ◽  
M M Sanders

Past studies of norepinephrine-stimulated protein phosphorylation in intact C-6 glioma cells had identified a 58,000 molecular weight, 5.7 isoelectric point protein (58K-5.7) as a cyclic AMP-dependent phosphoprotein and had shown that 58K-5.7 was one of the most abundant proteins of the nuclear fraction. Initial experiments of present studies showed that the 58K-5.7 protein remained with the nuclear ghost, or matrix structure, after removal of chromatin. Based on the size, acidity, abundance, nonsolubilization by nonionic detergent and salt, and solubilization by urea, the hypothesis was advanced that the 58K-5.7 protein was the vimentin-type intermediate filament protein. The hypothesis was tested by two types of immunochemical experiments. Antisera against hamster vimentin reacted selectively with only the 58K-5.7 protein in polyacrylamide gels of urea-solubilized cellular residues (i.e., nonionic detergent and 0.6 M salt-insoluble material) as determined by immunoautoradiography. Antisera against the pure 58K-5.7 protein of C-6 cells bound selectively to a fibrous array of cellular material typical of vimentin filaments as determined by indirect immunofluorescence. It is concluded that the 58K-5.7 protein is vimentin.


1990 ◽  
Vol 57 (2) ◽  
pp. 235-248 ◽  
Author(s):  
James D. Gorham ◽  
Harriet Baker ◽  
Deena Kegler ◽  
Edward B. Ziff

Author(s):  
Yukiko Sugi

In cultured skeletal muscle cells of chick, one intermediate filament protein, vimentin, is primarily formed and then synthesis of desmin follows. Coexistence of vimentin and desmin has been immunocytochemically confirmed in chick embryonic skeletal musclecells. Immunofluorescent localization of vimentin and desmin has been described in developing myocardial cells of hamster. However, initial localization of desmin and vimentin in early embryonic heart has not been reported in detail. By quick-freeze deep-etch method a loose network of intermediate filaments was revealed to exist surrounding myofibrils. In this report, immunocytochemical localization of desmin and vimentin is visualized in early stages of chick embryonic my ocardium.Chick embryos, Hamburger-Hamilton (H-H) stage 8 to hatch, and 1 day old postnatal chicks were used in this study. For immunofluorescence study, each embryo was fixed with 4% paraformaldehyde and embedded in Epon 812. De-epoxinized with sodium methoxide, semithin sections were stained with primary antibodies (rabbit anti-desmin antibody and anti-vimentin antibody)and secondary antibody (RITC conjugated goat-anti rabbit IgG).


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