The fusion of myoblasts

Wakelam, Michael J.O.

doi:10.1042/bj2280001

Cited by 305 publications

(207 citation statements)

References 111 publications

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“…However, in mammals, the cellular processes underlying myoblast fusion have been studied extensively on a cytological level Horwitz, 1977, 1978;Wakelam, 1985). Interestingly, comparison of these data with those from Drosophila revealed clear similarities for the myoblast fusion process.…”

Section: Functional Conservation Between Drosophila and Vertebrate Mymentioning

confidence: 99%

FuRMAS: triggering myoblast fusion in Drosophila

Önel

Renkawitz‐Pohl

2009

Developmental Dynamics

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In Drosophila, as in mammals, myoblast fusion is fundamental for development. This fusion process has two distinct phases that share common ultrastructural features and at least some molecular players between Drosophila and vertebrates. Here, we integrate the latest data on the key molecular players and ultrastructural features found during myoblast fusion into a new working model to explain this fundamental cellular process. At cell-cell contact sites, a protein complex (

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Section: Functional Conservation Between Drosophila and Vertebrate Mymentioning

confidence: 99%

FuRMAS: triggering myoblast fusion in Drosophila

Önel

Renkawitz‐Pohl

2009

Developmental Dynamics

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Section: Introductionmentioning

confidence: 99%

“…Myoblast differentiation and fusion can be studied in myoblast cultures, employing primary myoblast cultures or myoblast cell lines [1]. Cell-membrane fusion processes, including myoblast fusion, involve destabilization of cell membrane and cytoskeletal framework, allowing the creation of membranefusion-potent domains [1][2][3]. A limited membrane-protein degradation appears to be required for cell fusion, a degradation that would allow membrane disorganization in fusing cells [1][2][3][4][5][6].…”

Section: Introductionmentioning

confidence: 99%

“…Cell-membrane fusion processes, including myoblast fusion, involve destabilization of cell membrane and cytoskeletal framework, allowing the creation of membranefusion-potent domains [1][2][3]. A limited membrane-protein degradation appears to be required for cell fusion, a degradation that would allow membrane disorganization in fusing cells [1][2][3][4][5][6]. It has been proposed that calpain (Ca# + -dependent intracellular protease) is involved in the fusion-associated protein degradation [4][5][6][7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

“…1 These authors contributed equally to this work. 2 To whom correspondence should be addressed (e-mail nkosower!ccsg.tau.ac.il).…”

Section: Introductionmentioning

confidence: 99%

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Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability

Barnoy

Supino-Rosin

Kosower

2000

Biochemical Journal

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Tel Aviv 69978, IsraelCalpain (Ca# + -dependent intracellular protease)-induced proteolysis has been considered to play a role in myoblast fusion to myotubes. We found previously that calpastatin (the endogenous inhibitor of calpain) diminishes transiently during myoblast differentiation. To gain information about the regulation of calpain and calpastatin in differentiating myoblasts, we evaluated the stability and synthesis of calpain and calpastatin, and measured their mRNA levels in L8 myoblasts. We show here that µ-calpain and m-calpain are stable, long-lived proteins in both dividing and differentiating L8 myoblasts. Calpain is synthesized in differentiating myoblasts, and calpain mRNA levels do not change during differentiation. In contrast, calpastatin (though also a long-lived protein in myoblasts), is less stable in differentiating myoblasts than in the dividing cells, and its synthesis is inhibited upon initiation of differentiation. Inhibition of cal-

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Embryogenesis of the phrenic nerve and diaphragm in the fetal rat

Allan¹,

Greer²

1997

J. Comp. Neurol.

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The embryogenesis of the mammalian phrenic nerve and diaphragm continues to be poorly understood. The purpose of this study was to reexamine this general issue and resolve some long-standing controversies. Specifically, we examined 1) the migratory path and the initial target for phrenic axons; 2) the relationship between the phrenic nerve and the primordial diaphragm during descent from the cervical to the thoracic spinal cord levels; and 3) the nature of the interaction between the progression of phrenic nerve intramuscular branching, myoblast and/or myogenic cell migration, and diaphragmatic myotube formation. We demonstrate that a leading group of "pioneering" phrenic axons migrate along a well-defined track of neural cell adhesion molecule (NCAM)-expressing and low-affinity nerve growth factor (p75) receptor-expressing cells to reach the primordial diaphragm, the pleuroperitoneal fold, at embryonic day (E) 13. During the next day of development, the phrenic nerve and the primordial diaphragm descend together toward the level of the thoracic spinal cord. By E14.5, intramuscular branching has commenced. There is a tight spatiotemporal correlation between the outgrowth of intramuscular phrenic nerve branches, the distribution of myoblasts and/or myogenic cells, and the formation of myotubes within the developing diaphragm, implicating intimate mutual regulation.

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The fusion of myoblasts

Cited by 305 publications

References 111 publications

FuRMAS: triggering myoblast fusion in Drosophila

FuRMAS: triggering myoblast fusion in Drosophila

Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability

Embryogenesis of the phrenic nerve and diaphragm in the fetal rat

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