Changes in tropomyosin subunits and myosin light chains during development of chicken and rabbit straited muscles

Roy, Rohan Basu; Sreter, F. A.; Sarkar, Satyapriya

doi:10.1016/0012-1606(79)90271-9

Cited by 111 publications

(38 citation statements)

References 43 publications

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“…Developmental changes also occur in the Tm composition of developing avian skeletal muscles. However, the attainment of the adult subunit composition is virtually complete by 14-days post-hatch for the PM, ALD, and PLD (Roy, Sreter & Sarker, 1979;Matsuda et al 1983; results of present study), indicating that the observed developmental transitions in the Ca2" sensitivity of tension production between 14-days post-hatch and adult ages are not due to changes in Tm composition for these muscles.…”

Section: Discussionsupporting

confidence: 56%

Developmental changes in troponin T isoform expression and tension production in chicken single skeletal muscle fibres.

Reiser

Greaser

Moss

1992

The Journal of Physiology

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SUMMARY1. The Ca2" sensitivity of tension development was characterized in single skinned fibres from the slow anterior latissimus dorsi (ALD), fast posterior latissimus dorsi (PLD), and fast pectoralis major (PM) muscles of the chicken at adult and neonatal (2 weeks post-hatch) stages of development. In the adult, the PM was most sensitive, the ALD intermediate, and the PLD least sensitive to Ca2 .2. PM and PLD fibres were less sensitive to Ca2`at the neonatal stage of development than in the adult. However, ALD fibres exhibited no age-dependent changes in Ca2+ sensitivity. 3. Characterization of regulatory protein composition indicated that the PM and PLD fibres had identical fast isoforms of troponin C and troponin I at each developmental stage examined, but there were muscle-specific and age-dependent expressions of troponin T isoforms in these fibres.4. In the ALD fibres, identical slow isoforms of troponin C, troponin I and tropomyosin were found at each stage. In addition, the troponin T isoform that was present did not change with age.5. The results suggest a relationship between the specifie troponin T isoform composition of individual muscle fibres and their calcium sensitivities of tension development.

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Section: Discussionsupporting

confidence: 56%

Developmental changes in troponin T isoform expression and tension production in chicken single skeletal muscle fibres.

Reiser

Greaser

Moss

1992

The Journal of Physiology

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“…The (20,21). DISCUSSION Fast muscle development, particularly of avian pectoral muscle, has generally been accepted to be characterized biochemically by the exclusive synthesis of fast myosin (3)(4)(5)(6)(7)(8)(22)(23)(24), though there are reports that myosin reactive with antibodies to slow or cardiac myosin is found in vivo in early avian and mammalian fast muscle (12,25,26). The data reported here clearly show that avian pectoral muscle synthesizes and accumulates both fast and slow myosin light chains early in development and ceases to synthesize and accumulate myofibrils that contain slow myosin light chains by mid-development.…”

Section: Resultsmentioning

confidence: 99%

Myosin light chains and the developmental origin of fast muscle.

Stockdale¹,

Raman²,

Baden³

1981

Proc. Natl. Acad. Sci. U.S.A.

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Physiological characteristics of embryonic and fetal fast muscle function are similar to those ofadult slow muscles, whereas most biochemical data suggest that embryonic and fetal fast muscles contain only fast muscle myosin. In the studies reported here, myofibrillar preparations from developing avian pectoral muscle (fast muscle) were isolated and analyzed for myosin light-chain type and synthesis. These Developing fast muscle has physiological characteristics similar to those of slow muscle of the adult (1, 2); however, most biochemical analyses of fetal fast muscle indicate the presence of only fast myosin (3-6). The basis for the discrepancy between physiological and biochemical measurements is complex, because of the varied developmental ages that have been studied and the age-related differences in stoichiometry of the proteins comprising the myofibrillar apparatus during embryonic development (7, 8). Furthermore, recent observations indicate that there are embryonic forms ofboth myosin heavy chain and light chain not found in the adult (9-11).Gauthier et aL (12) report that development of a mammalian fast muscle (the diaphragm) is characterized by the presence of immunologically reactive slow and fast myosin within every muscle fiber, whereas, after birth, nearly every fiber contains only fast myosin. However, in analyzing a different fast muscle (avian pectoral muscle), Hoh (7) and Rubinstein and coworkers (4, 5) report that only fast myosin and no slow myosin is found in embryonic or fetal stages of pectoral muscle development. The latter investigators propose that the more developmentally primitive muscle synthesizes fast myosin and that the initiation of slow myosin synthesis is a consequence of developmental events imposed upon the muscle, such as innervation. However, the recent work of Keller and Emerson (13) and of Stockdale et al. (14) demonstrates that innervation is not required for initiation of slow myosin synthesis; myoblasts from embryonic muscle differentiating in cell culture in the complete absence of nerves synthesize slow myosin light chains. This paper extends these observations to show that early in development avian fast muscle synthesizes and assembles myofibrils with both slow and fast myosin light chains. Later in development, fast muscle no longer assembles myofibrils containing slow myosin light chains due to the cessation of synthesis of slow myosin light chains in mid-development. MATERIALS AND METHODSMuscle Tissue. Muscle was prepared from White Leghorn chickens or White Leghorn chicken embryos. Fast muscle (pectoral muscle) or slow muscle (lateral adductor of the thigh or anterior latissimus dorsi) was dissected from embryonic or adult birds and cleaned, and myosin was extracted. Fast muscle development was studied from day 9 of incubation through day 1 after hatching and in the adult; slow muscle was studied in 13-day embryos through hatching and in the adult.Tissue Culture. For explant cultures, muscles were dissected from chicken embryos ofthe required age, ...

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“…Skeletal muscle cells have two tropomyosin isoforms, ␣ and ␤, that are developmentally regulated at the transcriptional level such that the ␤-tropomyosin gene is repressed at hatching (46). Thus, in adult breast muscle, ␣/␣ is the principal isoform found (47)(48)(49)(50). Furthermore, the ratio of ␣/␣, ␣/␤, and ␤/␤ dimers differs between mature muscle fiber types (51,52).…”

Section: Expression Of Different Tropomodulin Isoforms In Muscle Corrmentioning

confidence: 99%

Identification of a Novel Tropomodulin Isoform, Skeletal Tropomodulin, That Caps Actin Filament Pointed Ends in Fast Skeletal Muscle

Almenar-Queralt¹,

Lee²,

Conley³

et al. 1999

Journal of Biological Chemistry

104

149

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Tropomodulin (E-Tmod) is an actin filament pointed end capping protein that maintains the length of the sarcomeric actin filaments in striated muscle. Here, we describe the identification and characterization of a novel tropomodulin isoform, skeletal tropomodulin (SkTmod) from chickens. Sk-Tmod is 62% identical in amino acid sequence to the previously described chicken ETmod and is the product of a different gene. Sk-Tmod isoform sequences are highly conserved across vertebrates and constitute an independent group in the tropomodulin family. In vitro, chicken Sk-Tmod caps actin and tropomyosin-actin filament pointed ends to the same extent as does chicken E-Tmod. However, E-and Sk-Tmods differ in their tissue distribution; Sk-Tmod predominates in fast skeletal muscle fibers, lens, and erythrocytes, while E-Tmod is found in heart and slow skeletal muscle fibers. Additionally, their expression is developmentally regulated during chicken breast muscle differentiation with Sk-Tmod replacing E-Tmod after hatching. Finally, in skeletal muscle fibers that coexpress both Sk-and E-Tmod, they are recruited to different actin filament-containing cytoskeletal structures within the cell: myofibrils and costameres, respectively. All together, these observations support the hypothesis that vertebrates have acquired different tropomodulin isoforms that play distinct roles in vivo.

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Changes in tropomyosin subunits and myosin light chains during development of chicken and rabbit straited muscles

Cited by 111 publications

References 43 publications

Developmental changes in troponin T isoform expression and tension production in chicken single skeletal muscle fibres.

Developmental changes in troponin T isoform expression and tension production in chicken single skeletal muscle fibres.

Myosin light chains and the developmental origin of fast muscle.

Identification of a Novel Tropomodulin Isoform, Skeletal Tropomodulin, That Caps Actin Filament Pointed Ends in Fast Skeletal Muscle

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