The presence in embryo extract of a myotrophic protein that affects proliferation and fusion of chick embryonic myoblasts in culture.
1988
Lee C.H. | Kwak K.B. | Chung C.H. | Ha D.B. | Yoo B.Y.
A myotrophic protein that seemed to be essential for the fusion of chick embryonic myoblast in culture was isolated from chick embryo extract and was found to be identical or at least similar to the iron-transporting protein, transferrin. Embryo extract seemed to contain, in addition to this myotrophic protein, a heat stable protein that inhibits the fusion of myoblasts. Iron seemed to be necessary for myoblasts of fuse and it was supposed that the role of the myotrophic protein in myoblast fusion is to supply iron to the cell. The number of the myotrophic protein receptors on myoblast surface membrane decreased immediately after the start of myoblast fusion, supposedly due to the decreased need of iron after the fusion once commenced. It was estimated that endocytosis of myotrophic protein took about 10 minutes and one recycling about 2 hours. The accumulation of iron in myoblasts continued linearly with culture time and endocytosis of the myotrophic protein occurred at a constant rate.
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