Dodson M V, Allen R E, Shimizu N, Shimizu Y, Hossner K L
Department of Animal Sciences, University of Arizona, Tucson.
Acta Endocrinol (Copenh). 1987 Nov;116(3):425-32. doi: 10.1530/acta.0.1160425.
The interactions of 125I-multiplication stimulating activity (MSA) and 125I-ovine somatomedin with receptors on skeletal muscle satellite cells are described. Specific binding of 125I-MSA/rIGF-II was inhibited by MSA/rIGF-II and oSm but not by insulin. Binding of 125I-oSm was inhibited by MSA/rIGF-II, oSm and insulin. In addition, 24-h pre-incubation of satellite cells with insulin increased the amount of 125I-MSA/rIGF-II bound, but insulin concentrations below 550 micrograms/l had no effect on the subsequent binding of 125I-oSm. Preincubation of cultures with oSm or MSA/rIGF-II decreased the subsequent binding of 125I-oSm and 125I-MSA/rIGF-II. These preliminary experiments suggest that oSm is similar to IGF-I in its binding characteristics and that primary cultures of skeletal muscle satellite cells possess type I and type II IGF receptors.
本文描述了¹²⁵I-增殖刺激活性(MSA)和¹²⁵I-羊生长调节素与骨骼肌卫星细胞上受体的相互作用。¹²⁵I-MSA/rIGF-II的特异性结合受到MSA/rIGF-II和羊生长调节素(oSm)的抑制,但不受胰岛素的抑制。¹²⁵I-oSm的结合受到MSA/rIGF-II、oSm和胰岛素的抑制。此外,卫星细胞与胰岛素预孵育24小时会增加¹²⁵I-MSA/rIGF-II的结合量,但胰岛素浓度低于550微克/升时对随后¹²⁵I-oSm的结合没有影响。用oSm或MSA/rIGF-II对培养物进行预孵育会降低随后¹²⁵I-oSm和¹²⁵I-MSA/rIGF-II的结合。这些初步实验表明,oSm在结合特性上与IGF-I相似,并且骨骼肌卫星细胞的原代培养物具有I型和II型IGF受体。