Calcium regulation of skeletal myogenesis. II. Extracellular and cell surface effects

Przybylski, Ronald J.; Szigeti, Vilma; Davidheiser, Sandra; Kirby, Albert C.

doi:10.1016/0143-4160(94)90052-3

Cited by 37 publications

(18 citation statements)

References 25 publications

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“…2C). Half-maximal phospholipid binding of myoferlin C2A occurs at 1 M calcium, which is similar to the 1.4 M calcium concentration reported in fusing myoblasts (Przybylski et al, 1994).…”

Section: Resultssupporting

confidence: 65%

Normal myoblast fusion requires myoferlin

et al. 2005

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Muscle growth occurs during embryonic development and continues in adult life as regeneration. During embryonic muscle growth and regeneration in mature muscle, singly nucleated myoblasts fuse to each other to form myotubes. In muscle growth, singly nucleated myoblasts can also fuse to existing large,syncytial myofibers as a mechanism of increasing muscle mass without increasing myofiber number. Myoblast fusion requires the alignment and fusion of two apposed lipid bilayers. The repair of muscle plasma membrane disruptions also relies on the fusion of two apposed lipid bilayers. The protein dysferlin, the product of the Limb Girdle Muscular Dystrophy type 2 locus, has been shown to be necessary for efficient, calcium-sensitive,membrane resealing. We now show that the related protein myoferlin is highly expressed in myoblasts undergoing fusion, and is expressed at the site of myoblasts fusing to myotubes. Like dysferlin, we found that myoferlin binds phospholipids in a calcium-sensitive manner that requires the first C2A domain. We generated mice with a null allele of myoferlin. Myoferlin null myoblasts undergo initial fusion events, but they form large myotubes less efficiently in vitro, consistent with a defect in a later stage of myogenesis. In vivo, myoferlin null mice have smaller muscles than controls do, and myoferlin null muscle lacks large diameter myofibers. Additionally, myoferlin null muscle does not regenerate as well as wild-type muscle does, and instead displays a dystrophic phenotype. These data support a role for myoferlin in the maturation of myotubes and the formation of large myotubes that arise from the fusion of myoblasts to multinucleate myotubes.

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“…2C). Half-maximal phospholipid binding of myoferlin C2A occurs at 1 M calcium, which is similar to the 1.4 M calcium concentration reported in fusing myoblasts (Przybylski et al, 1994).…”

Section: Resultssupporting

confidence: 65%

Normal myoblast fusion requires myoferlin

et al. 2005

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“…In skeletal muscles, terminal myogenic differentiation involves fusion of myoblasts into multi-nucleated myotubes, which is regulated by calcium-dependent processes such as cell adhesion (Przybylski et al 1994, Eng et al 1997. Based on the known role of fish STC in calcium homeostasis, it is tempting to speculate that STC1 may modulate myocyte differentiation by regulating calcium-dependent myoblast fusion.…”

Section: Discussionmentioning

confidence: 99%

The distribution of stanniocalcin 1 protein in fetal mouse tissues suggests a role in bone and muscle development

Jiang

Chang²,

Satoh³

et al. 2000

Journal of Endocrinology

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We previously isolated a mammalian gene STC1 that encodes a glycoprotein related to stanniocalcin (STC), a fish hormone that plays a major role in calcium homeostasis. However, the mammalian STC1 gene is expressed in a variety of adult tissues in contrast to fish where STC is expressed only in one unique gland, the corpuscles of Stannius. This suggested that STC1 may have wider autocrine/paracrine functions in mammals. In the present study, using immunocytochemistry, we showed that STC1 protein is localized in the developing bone and muscle of the mouse fetus. During endochondral bone formation, STC1 is found principally in prechondrocytes and prehypertrophic chondrocytes. During intramembranous bone formation STC1 is present in the mesenchyme that is about to undergo ossification. STC1 is also found in the myocardiocytes of the developing heart and at all stages of differentiation from myoblasts to myotube formation in developing skeletal muscle. The specific localization of STC1 to chondrocytes and muscle cells suggests a role for this protein in chondrogenic and myogenic differentiation.

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“…The fusion process is known to be Ca 2+ dependent. Indeed, formation of myotubes requires the presence of extracellular Ca 2+ (Schmid et al, 1984), and is preceded by an increase of cytosolic concentration of Ca 2+ ([Ca 2+ ] i ) (Przybylski et al, 1994) because of a net influx of Ca 2+ into the cell (David et al, 1981). The Ca 2+ influx occurs through T-type Ca 2+ channels (Bijlenga et al, 2000) and most probably through other not clearly identified Ca 2+ channels, possibly including store-operated and stretch-activated channels (Arnaudeau et al, 2006).…”

Section: Introductionmentioning

confidence: 99%