ArticleCell and tissue research1986
Development of myofibrils in the gizzard of chicken embryos. Intracellular distribution of structural proteins and development of contractility.
Article in Cell and tissue research, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- In ovo monitoring of smooth muscle fiber development in the chick embryo: diffusion tensor imaging with histologic correlation.PloS one · 2012Article
- Neural and smooth muscle development in the chicken gizzard.Roux's archives of developmental biology : the official organ of the EDBO · 1995Article
- Embryonic chicken gizzard: expression of the smooth muscle regulatory proteins caldesmon and myosin light chain kinase.Cell and tissue research · 1995Article
- Embryonic chicken gizzard: smooth muscle and non-muscle myosin isoforms.Cell and tissue research · 1994Article
- Embryonic chicken gizzard: immunolocalization of collagen and smooth muscle myosin.Cell and tissue research · 1992Article
- Stress fibers in the mesenteric mesothelial cells of the large intestine of the bullfrog, Rana catesbeiana.Cell and tissue research · 1990Article
- Development of smooth muscle: ultrastructural study of the chick embryo gizzard.Anatomy and embryology · 1989Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intracellular distributions of major muscle proteins, myosin, actin, tropomyosin, alpha-actinin, and desmin, in smooth muscle cells of chicken gizzard at various stages of embryogenesis were investigated by immunofluorescence-labeling of enzyme-dispersed cells cultured up to three hours. These muscle proteins, except some part of myosin, were organized into fibrous structures as soon as synthesis and accumulation of proteins started. As for myosin, a considerable amount of it was dispersed in soluble cytoplasm as well. On the other hand, Ca++-dependent contractility was detected with detergent-extracted myoblasts and glycerinated tissue from embryos older than 7 days. Although the nascent myofibrils bear a resemblance to "stress fibers," the former could be distinguished from the latter by their high stability in dispersed, spherical cells. The above findings, therefore, show that the synthesis of contractile proteins is followed by immediate assembly of them into functional myofibrils without undergoing any intermediate structure. Based on these findings, the mechanism of myofibril formation in developing smooth muscle cells is discussed.
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