Primary structure and developmental acidic to basic transition of 13 alternatively spliced mouse fast skeletal muscle troponin T isoforms |
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| Institution: | 1. Gerontology Research Center, University of Jyväskylä, Finland;2. Department of Health Sciences, University of Jyväskylä, Finland;3. Department of Clinical and Molecular Sciences, Division of Experimental Pathology, Università Politecnica delle Marche, Ancona, Italy;4. Department of Clinical Pathology and Innovative Therapy, Advanced Technology Center for Aging Research, INRCA-IRCCS, Ancona, Italy;5. Department of Experimental, Diagnostic and Specialty Medicine, Via S. Giacomo, 12, University of Bologna, Bologna, Italy;6. Interdepartmental Center Galvani “CIG”, Via Selmi, 3, University of Bologna, Bologna, Italy;7. Department of Microbiology and Immunology, School of Medicine, University of Tampere, Finland;8. Gerontology Research Center, University of Tampere, Finland;9. Institute for Molecular Medicine, University of Helsinki, Finland;10. National Institute for Health and Welfare, Helsinki, Finland;1. Brigham and Women’s Hospital, Department of Neurology, Harvard Medical School, Boston, MA, USA;2. Department of Cell and Molecular Biology, St. Jude Children’s Research Hospital, Memphis, TN, USA;3. Children’s Hospital Informatics Program, Harvard-MIT Division of Health Sciences and Technology, Boston, MA, USA;1. Stanley Division of Developmental Neurovirology, Department of Pediatrics, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Blalock 1105, Baltimore, MD 21287-4933, USA;2. Department of Psychiatry, Johns Hopkins University School of Medicine, Baltimore, MD, USA;3. Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA;1. Division of Medical Physiology, MRC Centre for Tuberculosis Research, DST/NRF Centre of Excellence for Biomedical Tuberculosis Research, Faculty of Medicine and Health Sciences, Stellenbosch University, Tygerberg, South Africa;2. Task Applied Science, Bellville, Cape Town, South Africa;3. Department of Statistics, Faculty of Natural Sciences, University of the Western Cape, Cape Town, South Africa;4. Department of Paediatrics and Child Health, Faculty of Medicine and Health Sciences, Stellenbosch University, Tygerberg, South Africa |
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| Abstract: | Large samples of original cDNAs encoding neonatal and adult mouse fast skeletal muscle troponin T (fTnT) have been isolated and characterized. The results demonstrate expression relationships of 8 alternatively spliced exons of the fTnT gene and reveal the primary structure of as many as 13 fTnT isoforms that diverge into acidic and basic classes due to differential mRNA splicing in the N-terminal variable region. In the C-terminal variable region encoded by the mutually exclusive exons 16 and 17, the splicing pathway and structure of exon 16 appears to be adult fTnT-specific, suggesting an adaptation to the functional demands of mature fast skeletal muscle. The cloned cDNAs were expressed in E. coli as standards to identify a high Mr to low Mr, acidic to basic fTnT isoform transition in postnatal developing skeletal muscles. Different from the developmental cardiac TnT switch generated by alternative splicing of a single exon, the fTnT isoform transition is an additive effect of alternative splicing of multiple N-terminal-coding exons, especially exons 4, 8 and fetal that are expressed at higher frequencies in the neonatal than in the adult muscle. The developmental fTnT isoform primary structure transition in both N- and C-terminal variable regions suggest a physiological importance of the apparently complex TnT isoform expression. |
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