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J. Biol. Chem., Vol. 266, Issue 31, 20626-20635, Nov, 1991
K Sakano, T Enjoh, F Numata, H Fujiwara, Y Marumoto, N Higashihashi, Y Sato, JF Perdue and Y Fujita-Yamaguchi
Five mutants of recombinant insulin-like growth factor-II (rIGF-II) that
bound with high affinity to either the IGF-II/cation-independent mannose
6-phosphate (IGF-II/CIM6-P) or the IGF-I receptor were prepared by
site-directed mutagenic procedures, expressed as fusion proteins in the
larva of Bombyx mori or Escherichia coli, purified to homogeneity,
renatured, and characterized in terms of their receptor binding affinities
and specificities as well as their biological activities. Class I mutants
in which Phe26, Tyr27, and Val43 were substituted with Ser, Leu, and Leu,
respectively, bound to enriched preparations of rat placental IGF-II/CIM6-P
receptors with apparent equilibrium dissociation constants (Kd(app)) that
were only slightly greater, i.e. 0.10, 0.05, and 0.06 nM, than that of
rIGF-II (0.04 nM) or hIGF-II (0.03 nM). In contrast, replacing Phe26 with
Ser resulted in 5- and 20- fold decreases in the affinities of this mutant
for highly purified human placental IGF-I and insulin receptors,
respectively. The affinities of the two other Class I mutants, [Leu27]- and
[Leu43]rIGF- IIs, for these two receptors were reduced 80- to 220-fold. The
affinities of Class II mutants, i.e. [Thr48,Ser49,Ile50]- and [Arg54,Arg55]
rIGF-IIs, for IGF-I receptors were as potent as rIGF-II; however, they
bound very poorly or not at all to the IGF-II/CIM6-P receptor. In the
binding study of those mutant rIGF-IIs, IGF-II was observed to have an
unexpectedly high affinity for pure human placental insulin receptor
preparations. For example, the affinities of hIGF-II, rIGF-II, and two
Class II rIGF-II mutants for the insulin receptor were only 3-, 9-, and
5-fold less, respectively, than that of porcine insulin. In two biological
assay systems, i.e. the stimulation of DNA synthesis in Balb/c 3T3 cells
and glycogen synthesis in HepG2 cells, the Kd(app) of the rIGF-II mutants
for the IGF-I receptor but not the IGF-II/CIM6-P receptor correlated with
their abilities to produce biological responses.
The design, expression, and characterization of human insulin-like growth factor II (IGF-II) mutants specific for either the IGF-II/cation- independent mannose 6-phosphate receptor or IGF-I receptor
Molecular Biology Research Laboratory, Daiichi Pharmaceutical Co., Ltd, Tokyo, Japan.
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