THE TYPE-II INSULIN-LIKE GROWTH-FACTOR (IGF) RECEPTOR HAS LOW AFFINITY FOR IGF-I ANALOGS - PLEIOTYPIC ACTIONS OF IGFS ON MYOBLASTS ARE APPARENTLY MEDIATED BY THE TYPE-I RECEPTOR
THE TYPE-II INSULIN-LIKE GROWTH-FACTOR (IGF) RECEPTOR HAS LOW AFFINITY FOR IGF-I ANALOGS - PLEIOTYPIC ACTIONS OF IGFS ON MYOBLASTS ARE APPARENTLY MEDIATED BY THE TYPE-I RECEPTOR
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DOI:
10.1210/endo-120-1-115
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发表时间:
1987-01-01
期刊:
影响因子:
4.8
通讯作者:
FLORINI, JR
中科院分区:
文献类型:
--
作者:
EWTON, DZ;FALEN, SL;FLORINI, JR
We have characterized binding and several actions of the somatomedins [insulin-like growth factors I and II (IGF-I and IGF-II)] on L6 myoblasts. Both IGF-I and IGF-II are potent stimulators of amino acid uptake, cell proliferation, and differentiation; they also suppress protein degradation in these cells. In all measurements, the relative potencies are IGF-I > IGF-II > insulin. Two recombinant DNA-produced analogs of IGF-I, (Thr59)IGF-I and (N-Met)IGF-I, were as active as native IGF-I in all four assays. However, when 125I-labeled hormones were used for studies of binding to IGF receptors, there was a striking difference between the native and recombinant IGF-I molecules. Both were bound significantly by the type I receptor (a 350K molecule that is dissociated upon sulfhydryl reduction), but the recombinant analogs exhibited little cross-reactivity with the type II receptor (a 220K molecule that is not dissociated by reduction). Thus, the equal activity of native IGF-I and its recombinant DNA-produced analogs coupled with the higher potency of IGF-I (compared to IGF-II) suggest that the type II receptor plays little or no role in the four actions of the somatomedins studied in L6 myoblasts.