ArticleThe Journal of cell biology1990
Differential distribution of myosin isoforms among the myofibrils of individual developing muscle fibers.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 42 citations in OpenAlex.
- Transitional Hybrid Skeletal Muscle Fibers in Rat Soleus Development.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2019Article
- A continuum of myofibers in adult rabbit extraocular muscle: force, shortening velocity, and patterns of myosin heavy chain colocalization.Journal of applied physiology (Bethesda, Md. : 1985) · 2011Article
- The continuum of hybrid IIX/IIB fibers in normal mouse muscles: MHC isoform proportions and spatial distribution within single fibers.American journal of physiology. Regulatory, integrative and comparative physiology · 2010Article
- Nonmuscle myosin IIB, a sarcomeric component in the extraocular muscles.Experimental cell research · 2010Article
- Four novel myosin heavy chain transcripts define a molecular basis for muscle fibre types in Rana pipiens.The Journal of physiology · 1998Article
- Isomyosin patterns of single type IIB, IID and IIA fibres from rabbit skeletal muscle.Journal of muscle research and cell motility · 1995Article
- Analysis of Ca2+ and Sr2+ activation characteristics in skinned muscle fibre preparations with different proportions of myofibrillar isoforms.Journal of muscle research and cell motility · 1995Article
- Developmental transitions in the myosin patterns of two fast muscles.Journal of muscle research and cell motility · 1993Article
- Distribution of developmental myosin isoforms in isolated A-segments.Journal of muscle research and cell motility · 1992Article
- Visualization of myosin exchange between synthetic thick filaments.Journal of muscle research and cell motility · 1991Article
- Assembly of avian skeletal muscle myosins: evidence that homodimers of the heavy chain subunit are the thermodynamically stable form.The Journal of cell biology · 1991Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin was localized in situ in the posthatch chicken pectoralis using isoform-specific mAbs. The distribution among myofibrils was demonstrated by immunofluorescence and by immunogold EM. Fluorescein- or rhodamine-labeled antibody (12C5) specific for the head region (S1) of myosin was used as a marker to identify "embryonic" myosin. In longitudinal semithin frozen sections, a minority population of myofibrils stained intensely with 12C5. All other myofibrils in the same cell stained only weakly. Similarly, in Lowicryl-embedded ultrathin sections prepared for EM, a minority population reacted preferentially with gold-labeled 12C5. An antibody (5B4) specific for the rod portion of "neonatal" myosin reacted strongly with nearly all myofibrils, and this was evident by light and electron microscopy. A few of the fibrils that reacted strongly with 12C5 reacted weakly with 5B4. These observations demonstrate that an epitope reacting with 12C5 is more abundant in some myofibrils than in others within the same cell. Three categories of myofibrils can be identified by their relative proportions of embryonic and neonatal forms of myosin: in nearly all fibrils, a neonatal isoform predominates; in a minority population, embryonic and neonatal isoforms are both abundant; and in a few fibrils, an embryonic isoform predominates. It is concluded that there are distinct populations of myofibrils in which specific isoforms are segregated within an individual cell.
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