The objective is to determine what factors regulate the expression of myosin heavy chain isoforms during chicken skeletal muscle differentiation and maturation. Our immediate aim is to identify and characterize myosin heavy chain isoforms found in fast and slow skeletal muscles at various stages of normal development. Our studies will include a combination of biochemical and immunological techniques and employ the numerous monoclonal antibodies that we have prepared during the first three years of this project. Our initial studies have shown that there are more myosin heavy chain isoforms than previously believed and different developmental programs exist among fast muscle fibers. Thus we will continue to screen for monoclonal antibodies which can distinguish the closely related fast and the closely related slow developmental isoforms. We will compare the program of myosin heavy chain expression during the development of other fast and slow muscles and fast and slow muscle fibers to what we have already observed in the pectoralis major, the posterior latissimus dorsi, the anterior latissimus dorsi, and the lateral gastrocnemius. In order to understand the regulation of myosin isoform expression we will examine the myosin transitions that occur during muscle regeneration following cold injury or Marcaine injection in normally innervated and denervated muscles. We will also study the myosin changes that may accompany muscle degeneration and atrophy following denervation and/or limb immobilization. We will determine what myosins are expressed following hypertrophy in chicken wing muscles. We will also determine the effect of the administration of various hormones on myosin transitions during normal development and during the altered growth conditions described above. Finally, we will continue to study myosin expression of muscle cells in culture in order to determine appropriate conditions to induce myosin heavy chain transitions and muscle fiber maturation in vitro.

Agency
National Institute of Health (NIH)
Institute
National Institute on Aging (NIA)
Type
Research Project (R01)
Project #
5R01AG008573-08
Application #
3120294
Study Section
Molecular Cytology Study Section (CTY)
Project Start
1989-01-01
Project End
1993-12-31
Budget Start
1990-01-01
Budget End
1990-12-31
Support Year
8
Fiscal Year
1990
Total Cost
Indirect Cost
Name
University of California Davis
Department
Type
Schools of Earth Sciences/Natur
DUNS #
094878337
City
Davis
State
CA
Country
United States
Zip Code
95618
Singh, Sheetal; Bandman, Everett (2006) Dimerization specificity of adult and neonatal chicken skeletal muscle myosin heavy chain rods. Biochemistry 45:4927-35
Chen, Q; Moore, L A; Wick, M et al. (1997) Identification of a genomic locus containing three slow myosin heavy chain genes in the chicken. Biochim Biophys Acta 1353:148-56
Chao, T H; Bandman, E (1997) Cloning, nucleotide sequence and characterization of a full-length cDNA encoding the myosin heavy chain from adult chicken pectoralis major muscle. Gene 199:265-70
Tidyman, W E; Moore, L A; Bandman, E (1997) Expression of fast myosin heavy chain transcripts in developing and dystrophic chicken skeletal muscle. Dev Dyn 208:491-504
Moore, L A; Tidyman, W E; Arrizubieta, M J et al. (1993) The evolutionary relationship of avian and mammalian myosin heavy-chain genes. J Mol Evol 36:21-30
Moore, L A; Arrizubieta, M J; Tidyman, W E et al. (1992) Analysis of the chicken fast myosin heavy chain family. Localization of isoform-specific antibody epitopes and regions of divergence. J Mol Biol 225:1143-51
Moore, L A; Tidyman, W E; Arrizubieta, M J et al. (1992) Gene conversions within the skeletal myosin multigene family. J Mol Biol 223:383-7
Hartley, R S; Bandman, E; Yablonka-Reuveni, Z (1992) Skeletal muscle satellite cells appear during late chicken embryogenesis. Dev Biol 153:206-16
Kerwin, B; Bandman, E (1991) Assembly of avian skeletal muscle myosins: evidence that homodimers of the heavy chain subunit are the thermodynamically stable form. J Cell Biol 113:311-20
Hartley, R S; Bandman, E; Yablonka-Reuveni, Z (1991) Myoblasts from fetal and adult skeletal muscle regulate myosin expression differently. Dev Biol 148:249-60

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