Heterogeneity of insulin-like growth factor-I affinity for the insulin-like growth factor-II receptor: Comparison of natural, synthetic and recombinant DNA-derived insulin-like growth factor-I

Ronald (Ron) Rosenfeld, C. A. Conover, D. Hodges, P. D K Lee, P. Misra, R. L. Hintz, C. H. Li

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Abstract

Although insulin-like growth factors (IGF) I and II bind with high affinity to structurally discrete receptors, they bind with a lesser affinity to each other's receptor. We have evaluated the affinity of five different IGF-I preparations (three natural IGF-I preparations, one synthetic preparation, and one recombinant DNA-derived) for the IGF-II receptor in rat placental membranes, 18-54, SF cells and BRL-3A cells. In all tissues tested, the natural IGF-I preparations demonstrated an affinity for the IGF-II receptor which was 10-20% that of IGF-II. However, the recombinant and synthetic IGF-I preparations exhibited substantially lower affinities than natural IGF-I for this receptor, with only 10-25% reduction in (125-I)iodo IGF-II binding at peptide concentrations up to 400 ng/ml. Radioimmunoassay of the natural IGF-I preparations with an antibody directed against the unique C-peptide region of IGF-II demonstrated that contamination of IGF-I preparations with immunoreactive IGF-II could not exceed 5%. These results demonstrate that IGF-I purified from human plasma has a different affinity for the IGF-II receptor than does synthetic or recombinant IGF-I. Furthermore, there data are consistent with the hypothesis that IGF-I, itself, may be heterogeneous, and that subforms may vary in their affinities for the IGF receptors. Alternatively, IGF-I preparations which have been considered to be pure may be contaminated with small amounts of IGF-II, resulting in overestimation of the affinity of IGF-I for the type II IGF receptor.

Original languageEnglish (US)
Pages (from-to)199-205
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume143
Issue number1
DOIs
StatePublished - Feb 27 1987
Externally publishedYes

Fingerprint

IGF Type 2 Receptor
Recombinant DNA
Insulin-Like Growth Factor I
Insulin-Like Growth Factor II
Somatomedin Receptors
Plasma (human)
IGF Type 1 Receptor
C-Peptide
Radioimmunoassay
Rats

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Heterogeneity of insulin-like growth factor-I affinity for the insulin-like growth factor-II receptor : Comparison of natural, synthetic and recombinant DNA-derived insulin-like growth factor-I. / Rosenfeld, Ronald (Ron); Conover, C. A.; Hodges, D.; Lee, P. D K; Misra, P.; Hintz, R. L.; Li, C. H.

In: Biochemical and Biophysical Research Communications, Vol. 143, No. 1, 27.02.1987, p. 199-205.

Research output: Contribution to journalArticle

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abstract = "Although insulin-like growth factors (IGF) I and II bind with high affinity to structurally discrete receptors, they bind with a lesser affinity to each other's receptor. We have evaluated the affinity of five different IGF-I preparations (three natural IGF-I preparations, one synthetic preparation, and one recombinant DNA-derived) for the IGF-II receptor in rat placental membranes, 18-54, SF cells and BRL-3A cells. In all tissues tested, the natural IGF-I preparations demonstrated an affinity for the IGF-II receptor which was 10-20{\%} that of IGF-II. However, the recombinant and synthetic IGF-I preparations exhibited substantially lower affinities than natural IGF-I for this receptor, with only 10-25{\%} reduction in (125-I)iodo IGF-II binding at peptide concentrations up to 400 ng/ml. Radioimmunoassay of the natural IGF-I preparations with an antibody directed against the unique C-peptide region of IGF-II demonstrated that contamination of IGF-I preparations with immunoreactive IGF-II could not exceed 5{\%}. These results demonstrate that IGF-I purified from human plasma has a different affinity for the IGF-II receptor than does synthetic or recombinant IGF-I. Furthermore, there data are consistent with the hypothesis that IGF-I, itself, may be heterogeneous, and that subforms may vary in their affinities for the IGF receptors. Alternatively, IGF-I preparations which have been considered to be pure may be contaminated with small amounts of IGF-II, resulting in overestimation of the affinity of IGF-I for the type II IGF receptor.",
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