Development of connectin/titin and nebulin in striated muscles of chicken

Shimada, Yohei

doi:10.1016/s0065-227x(96)90036-2

Cited by 7 publications

(10 citation statements)

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“…Previous studies demonstrated that desmin and titin appeared earlier in embryonic mouse somites than myosin (Furst et al, 1989;Shimada et al, 1996). The results presented here confirm and extend those findings by characterizing early contractile protein expression in the DML and nascent myotome and by linking the onset of expression of these proteins to specific stages in somite development.…”

Section: Onset Of Appearance Of Titin Desmin and Myosin According Tsupporting

confidence: 89%

“…Less information, however, is available for nascent myotome cells in embryonic somites. The developmental timing of the appearance of desmin in wing level somites have been reported (Kaehn et al, 1988;Borman and Yorde, 1994) as has the later appearance of myosin relative to desmin (Furst et al, 1989;Shimada et al, 1996). Recently, the localization of slow and fast myosin isoforms in the myotome was determined indicating the spatial relationship of older myotome fibers (Sacks et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

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The pattern of MyoD and contractile protein localization in primary epaxial myotome reflects the dynamic progression of nascent myoblast differentiation

Yang

Ordahl

2005

Developmental Dynamics

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The localization of contractile and regulatory proteins in early stages of epaxial primary myotome development was analyzed by immunofluorescence microscopy. Contractile proteins that appear in an ordered sequence in the rostro-caudal axis of somite development were found to reiterate that sequence in the dorso-medial-to-ventro-lateral axis of primary epaxial myotome development. Pair-wise localization of MyoD-titin, desmin-titin, and desmin-myosin defined three zones extending from the dermomyotome dorso-medial lip (DML) into the primary myotome layer. Zones M1 and M2, which were positive for MyoD ؉ titin and MyoD ؉ titin ؉ desmin, respectively, were restricted to the dorso-medial-most extremity of the myotome layer and did not expand during the course of myotome development. Zone M3 was positive for MyoD, desmin, titin, myosin, and cardiac troponin T and was the only zone that expanded during primary myotome development. Myotome fibers in zone M3 were unit-length, spanning the full rostro-caudal axis of the myotome while fibers in zones M1 and M2 were shorter than unit length. Anti-myoD immunofluorescence, when detected in cells lacking contractile-protein-positive cytoplasm, was restricted to the DML and nascent myotome cells immediately subjacent to the DML. These results demonstrate a dynamic spatiotemporal sequence in the differentiation program of nascent myotome cells as they emerge from the DML; zones M1 and M2 reflect standing waves of sequential contractile protein activation during the maturation of nascent myotomal myoblasts, while the expanding zone M3 reflects the accumulation of mature myotome fibers expressing a full cohort contractile proteins. Developmental Dynamics 235:382-394, 2006.

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Section: Onset Of Appearance Of Titin Desmin and Myosin According Tsupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

The pattern of MyoD and contractile protein localization in primary epaxial myotome reflects the dynamic progression of nascent myoblast differentiation

Yang

Ordahl

2005

Developmental Dynamics

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“…Tropomyosin is known to bind several thin-filament proteins including actin, troponinT, tropomodulin, and nebulin [Perry, 2001;Clark et al, 2002;Ogut et al, 2003], although it is not clear when these proteins begin to bind each other to form mature thin filaments during myofibrillogenesis [Littlefield et al, 2001;Sanger et al, 2005;Wang et al, 2005a,b]. There is evidence that one of these proteins, nebulin, is absent in premyofibrils in skeletal muscle cells [Moncman and Wang, 1996;Shimada et al, 1996], although there is one contrary report [Ojima et al, 1999]. Nebulin is a 600-900-kD actin-binding protein [Jin and Wang, 1991] in skeletal muscle that can bind actin, tropomyosin, troponinT, tropomodulin, and a-actinin allowing it to cross-link and stabilize thin filaments during myofibril assembly (Fig.…”

Section: Discussionmentioning

confidence: 99%

Ectopic expression and dynamics of TPM1α and TPM1κ in myofibrils of avian myotubes

Wang

Sanger

Kang

et al. 2007

Cell Motil. Cytoskeleton

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From the four known vertebrate tropomyosin genes (designated TPM1, TPM2, TPM3, and TPM4) over 20 isoforms can be generated. The predominant TPM1 isoform, TPM1alpha, is specifically expressed in both skeletal and cardiac muscles. A newly discovered alternatively spliced isoform, TPM1kappa, containing exon 2a instead of exon 2b contained in TPM1alpha, was found to be cardiac specific and developmentally regulated. In this work, we transfected quail skeletal muscle cells with green fluorescent proteins (GFP) coupled to chicken TPM1alpha and chicken TPM1kappa and compared their localizations in premyofibrils and mature myofibrils. We used the technique of fluorescence recovery after photobleaching (FRAP) to compare the dynamics of TPM1alpha and TPM1kappa in myotubes. TPM1alpha and TPM1kappa incorporated into premyofibrils, nascent myofibrils, and mature myofibrils of quail myotubes in identical patterns. The two tropomyosin isoforms have a higher exchange rate in premyofibrils than in mature myofibrils. F-actin and muscle tropomyosin are present in the same fibers at all three stages of myofibrillogenesis (premyofibrils, nascent myofibrils, mature myofibrils). In contrast, the tropomyosin-binding molecule nebulin is not present in the initial premyofibrils. Nebulin is gradually added during myofibrillogenesis, becoming fully localized in striated patterns by the mature myofibril stage. A model of thin filament formation is proposed to explain the increased stability of tropomyosin in mature myofibrils. These experiments are supportive of a maturing thin filament and stepwise model of myofibrillogenesis (premyofibrils to nascent myofibrils to mature myofibrils), and are inconsistent with models that postulate the immediate appearance of fully formed thin filaments or myofibrils.

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“…The direct interaction of titin with numerous sarcomeric proteins is particularly pertinent with respect to its proposed role as a molecular template during myofibril assembly. Titin is one of the first myofibrillar proteins that assembles into nascent sarcomeres in in vivo studies and in most, but not all, studies using primary striated muscle cell cultures (for in vivo studies see Tokuyasu and Maher, 1987 a , b ;Fürst et al, 1989 a ;Shimada et al, 1996; for discussion of discrepancies in in vitro studies see Epstein and Fischman, 1991;Handel et al, 1991;Dabiri et al, 1997;Fulton and Alftine, 1997;Holtzer et al, 1997). During myogenesis, the integration of titin into nascent sarcomeres begins with the assembly of the Z-line-associated NH 2 terminus and proceeds towards the COOH-terminal M band region in the middle of the sarcomere (Fürst et al, 1989 a ).…”

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confidence: 99%

The NH2 Terminus of Titin Spans the Z-Disc: Its Interaction with a Novel 19-kD Ligand (T-cap) Is Required for Sarcomeric Integrity

Gregorio

Trombitás

Centner

et al. 1998

The Journal of Cell Biology

278

254

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Titin is a giant elastic protein in vertebrate striated muscles with an unprecedented molecular mass of 3–4 megadaltons. Single molecules of titin extend from the Z-line to the M-line. Here, we define the molecular layout of titin within the Z-line; the most NH2-terminal 30 kD of titin is located at the periphery of the Z-line at the border of the adjacent sarcomere, whereas the subsequent 60 kD of titin spans the entire width of the Z-line. In vitro binding studies reveal that mammalian titins have at least four potential binding sites for α-actinin within their Z-line spanning region. Titin filaments may specify Z-line width and internal structure by varying the length of their NH2-terminal overlap and number of α-actinin binding sites that serve to cross-link the titin and thin filaments. Furthermore, we demonstrate that the NH2-terminal titin Ig repeats Z1 and Z2 in the periphery of the Z-line bind to a novel 19-kD protein, referred to as titin-cap. Using dominant-negative approaches in cardiac myocytes, both the titin Z1-Z2 domains and titin-cap are shown to be required for the structural integrity of sarcomeres, suggesting that their interaction is critical in titin filament–regulated sarcomeric assembly.

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Development of connectin/titin and nebulin in striated muscles of chicken

Cited by 7 publications

References 0 publications

The pattern of MyoD and contractile protein localization in primary epaxial myotome reflects the dynamic progression of nascent myoblast differentiation

The pattern of MyoD and contractile protein localization in primary epaxial myotome reflects the dynamic progression of nascent myoblast differentiation

Ectopic expression and dynamics of TPM1α and TPM1κ in myofibrils of avian myotubes

The NH2 Terminus of Titin Spans the Z-Disc: Its Interaction with a Novel 19-kD Ligand (T-cap) Is Required for Sarcomeric Integrity

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