Expression of Nuclear Lamin A and Muscle-Specific Proteins in Differentiating Muscle Cells in Ovo and in vitro

Primary cultures and tissue samples of chicken embryonic muscle were immunologically probed for the expression of muscle-specific proteins, such as myosin heavy chain and the tropomyosins, as well as for the nuclear lamina protein, lamin A. As determined by quantitative immunoblotting, the expressio...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of cell biology 1989-08, Vol.109 (2), p.495-504
Main Authors: Lourim, David, Lin, Jim Jung-Ching
Format: Article
Language:English
Subjects:
Animals
Antibodies
Biological and medical sciences
Cell culture techniques
Cell Differentiation
Cell nucleus
Cells
Chick Embryo
Cultured cells
Embryonic cells
Fluorescent Antibody Technique
Fundamental and applied biological sciences. Psychology
Gels
Gene expression
Immunoblotting
Lamin Type A
Lamins
Molecular and cellular biology
Molecular genetics
Muscle Proteins - genetics
Muscles - cytology
Muscles - metabolism
Myoblasts
Myosins - genetics
Myosins - metabolism
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Precipitin Tests
Protein isoforms
skeletal muscle
Tropomyosin - genetics
Tropomyosin - metabolism
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Primary cultures and tissue samples of chicken embryonic muscle were immunologically probed for the expression of muscle-specific proteins, such as myosin heavy chain and the tropomyosins, as well as for the nuclear lamina protein, lamin A. As determined by quantitative immunoblotting, the expression of lamin A and the muscle-specific proteins were at low levels or absent in predifferentiation myoblasts both in vitro and in ovo. During differentiation, an increase of lamin A expression preceded the induction to high levels of expression of muscle-specific proteins. Immunofluorescence staining of chicken embryonic muscle cells in culture also indicates an accumulation of lamin A before the induction of muscle-specific proteins expression. Furthermore, the accumulation of lamin A reached a plateau before the muscle-specific proteins during muscle development. In two dimensional NEPHGE gel analysis of immunoprecipitated lamin A, no detectable change in the ratio of the acidic/basic isoelectric variants of lamin A was observed during myogenesis. A potential role for lamin A in the mechanisms which underlie the differential and coordinate expression of muscle-specific genes is proposed.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.109.2.495