Cell fusion and differentiation in cultured chick muscle cells

Morris, Glenn E.; Cole, R. J.

doi:10.1016/0014-4827(72)90536-8

Cited by 82 publications

(23 citation statements)

References 18 publications

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“…fig.2 and each point is the average of two gels (maximum range of duplicates *-10%). 4. Discussion Figures 1 and 2 show that, by 120 h culture, a high proportion of the radioactivity extracted by the method described has the same charge and molecular weight as CPK, although, as iig.3 shows, this represents only 0.5% of the total radioactivity incorporated.…”

Section: Resultsmentioning

confidence: 99%

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Biosynthesis of muscle‐specific creatine kinase during differentiation in vitro

Morris

Cole

1977

FEBS Letters

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Section: Resultsmentioning

confidence: 99%

“…Gels were then cut into 1 mm slices and the enzyme activity in each slice was measured fluorimetrically [4] . Creatine klnase specific activity is expressed as IU/mg (1 unit converts 1 ~01 creatine phosphate to creature/mm, at 37'C) of soluble protein in the original cell extract.…”

Section: Separation Of Isoenzymesmentioning

confidence: 99%

Biosynthesis of muscle‐specific creatine kinase during differentiation in vitro

Morris

Cole

1977

FEBS Letters

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“…Cell cultures were maintained at 37°C in an atmosphere of 5% CO 2 –95% air in alpha MEM supplemented with either 10% horse serum (differentiation conditions) or fetal bovine serum (nondifferentiating conditions) as previously described [Jane and Dufresne, 1994]. The formation of myotubes was quantified as percent fusion (i.e., fusion index) according to the established procedure of Morris and Cole [1972].…”

Section: Methodsmentioning

confidence: 99%

Evidence for the involvement of cathepsin B in skeletal myoblast differentiation

Jane

DaSilva

Koblinski

et al. 2002

J of Cellular Biochemistry

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Our previous studies suggest that the cysteine protease cathepsin B (catB) is involved in skeletal myoblast differentiation (myogenesis). To test this hypothesis, we examined the effect of trapping one of the two catB alleles on the ability of C2C12 cells to differentiate. During differentiation, catB gene-trapped C2C12 mouse myoblasts (RT-27) demonstrated a similar pattern of intracellular catB activity and protein expression compared to that observed in control C2C12 myoblasts and myoblasts trapped in a gene other than catB. However, compared to control myoblast cell lines, levels of catB activity and protein at each stage of RT-27 differentiation were reduced. The reductions in levels of catB were associated with reductions in several myogenic phenotypes including reduced levels of creatine phosphokinase activity and myosin heavy chain protein, two late biochemical markers of myogenesis, and reduced myotube size and extent of myotube formation over time. Comparable reductions were not observed for myogenin protein, an early biochemical marker of myogenesis, or in myokinase activity and catB related cathepsin L-type activity, two non-specific proteins. Finally, both control and catB gene-trapped myoblasts secreted active catB at pH 7.0. However levels of active pericellular/secreted catB were 50% lower in catB gene-trapped myoblasts. Collectively, these results support a functional link between catB expression and skeletal myogenesis and suggest a role for active pericellular/secreted catB in myoblast fusion.

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“…This process involves the cessation of DNAsynthesis, activation of muscle-specific gene expression, and the fusion of single cells into multinucleated myotubes (2, 23,27,28,32,33,34,44).…”

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confidence: 99%

Characterization of Myogenin Expression in Myotubes Derived from Quail Myoblasts Transformed with a Temperature Sensitive Mutant of Rous Sarcoma Virus.

Isobe

Hirayama

Kim

1998

Cell Struct. Funct.

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ABSTRACT. During myogenic differentiation of quail myoblasts transformed with a temperature sensitive mutant of Rous sarcoma virus (QM-RSV cells), it was observed that myogenin was continuously expressed in myotubes. In contrast, in myotubes derived from quail primary cells (parent cells of QM-RSVcells), myogenin expression was seen only in the myotubes not having striated structures comprised of myofibrils, but not in myotubes having the structures. The fact that there are not striated structures of myofibrils formed in myotubes derived from QM-RSV cells suggests that these myotubes stop at an immature state prior to the final differentiation. These results also suggest that myogenin is not only required for early steps during differentiation but also maturation steps of myotubes. To clarify the roles of myogeninafter myotubeformation and maturation, myotubes derived from QM-RSVcells were treated with N,N'-hexamethylene bisacetamide (HMBA)or incubated at 35.5°C, a permissive temperature of RSVfor suppression of myogenin expression. Ontreatment with HMBA, myogenin expression disappeared and myotubes began to incorporate 5-bromo-2'-deoxyuridine (BrdU) into the nuclei, whereas the expression remained in manymyotubes on culture at 35.5°C. These results suggest that immature myotubes can return to an up step of differentiation, prior to the commitment step with HMBA treatment, but not with culture at 35.5°C.Skeletal myogenesis involves an initial period of myoblast replication, before undergoing terminal differentiation. This process involves the cessation of DNAsynthesis, activation of muscle-specific gene expression, and the fusion of single cells into multinucleated myotubes (2, 23,27,28,32,33,34,44).The MyoDfamily, which includes MyoD (9), myogenin (10, 43), myf5 (3), and MRF4/myf6/herculin (4, 30, 36), governs myogenic differentiation, and shares the remarkable properties of myogenic differentiation when expressed in non-muscle cells (ll, 31, 35, 41, 42). Studies of gene targeting of myogenin indicate that myogenin has unique functions in the muscle differentiation, especially for the commitment to terminal differentiation and the formation of myotubes (5, 6, 17,33, 37). Further its function is apparently not complemented by other members of the MyoDfamily, suggesting that it is a key regulator amongthe muscle specific transcription factors for the terminal differentiation. Wehave been studying myoblast differentiation using quail myoblasts (QM)transformed with a temperature

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Cell fusion and differentiation in cultured chick muscle cells

Cited by 82 publications

References 18 publications

Biosynthesis of muscle‐specific creatine kinase during differentiation in vitro

Biosynthesis of muscle‐specific creatine kinase during differentiation in vitro

Evidence for the involvement of cathepsin B in skeletal myoblast differentiation

Characterization of Myogenin Expression in Myotubes Derived from Quail Myoblasts Transformed with a Temperature Sensitive Mutant of Rous Sarcoma Virus.

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