Co-expression of multiple myosin heavy chain genes, in addition to a tissue-specific one, in extraocular musculature.
Open Access
- 1 August 1985
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 101 (2) , 618-629
- https://doi.org/10.1083/jcb.101.2.618
Abstract
The developmental transitions of myosin H chain (MHC) gene expression were investigated in the rat extraocular musculature (EOM) at the mRNA level using S1-nuclease mapping techniques and at the protein level by polypeptide mapping and immunochemistry. A genomic clone was isolated, designated .lambda. 10B3, corresponding to an MHC gene which is expressed in the EOM fibers (recti and oblique muscles) of the adult rat but not in hind limb muscles. Using c[complementary]DNA and genomic probes for MHC genes expressed in skeletal (embryonic, neonatal, fast oxidative, fast glycolytic and slow/cardiac .beta.-MHC), cardiac (.alpha.-MHC) and EOM (.lambda. 10B3) muscles, demonstrates the concomitant expression at the mRNA level of at least 6 different MHC genes in adult EOM. Protein and immunochemical analyses confirm the presence of at least 4 different MHC types on EOM. Immunocytochemistry demonstrates that different myosin isozymes tend to segregate into individual myofibers, although some fibers seem to contain > 1 MHC type. The EOM fibers exhibit multiple patterns of MHC gene regulation. One set of fibers undergoes a sequence of isoform transitions similar to the one described for limb skeletal muscles, whereas other EOM myofiber populations arrest the MHC transition at the embryonic, neonatal/adult, or adult EOM-specific stage. The MHC gene family is not under the control of a strict development clock, but the individual genes can modify their expression by tissue-specific and/or environmental factors.This publication has 65 references indexed in Scilit:
- Immunochemical analysis of myosin heavy chains in the developing chicken heartDevelopmental Biology, 1984
- Regulation of myosin synthesis by thyroid hormone: relative change in the .alpha.- and .beta.-myosin heavy chain mRNA levels in rabbit heartBiochemistry, 1984
- Myosin isozyme transitions occurring during the postnatal development of the rat soleus muscleDevelopmental Biology, 1984
- The role of the neural crest in patterning of avian cranial skeletal, connective, and muscle tissuesDevelopmental Biology, 1983
- Developmental appearance of myosin heavy and light chain isoforms in vivo and in vitro in chicken skeletal muscleDevelopmental Biology, 1982
- “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein AAnalytical Biochemistry, 1981
- "Slow" myosins in vertebrae skeletal muscle. An immunofluorescence study.The Journal of cell biology, 1980
- Identification of a novel form of myosin light chain present in embryonic muscle tissue and cultured muscle cellsJournal of Molecular Biology, 1978
- Myogenic and neurogenic contributions to the development of fast and slow twitch muscles in ratDevelopmental Biology, 1978
- Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase IJournal of Molecular Biology, 1977