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J. Biol. Chem., Vol. 265, Issue 25, 14892-14898, 09, 1990
J Zapf, M Kiefer, J Merryweather, F Musiarz, D Bauer, W Born, JA Fischer and ER Froesch
We have isolated four insulin-like growth factor binding proteins (IGFBPs)
from adult human serum by insulin-like growth factor (IGF) I affinity
chromatography and high performance liquid chromatography. A 36-kDa binding
protein (BP), not digestible with N-glycanase, is increased in patients
with extrapancreatic tumor hypoglycemia and during IGF I administration in
healthy adults. Its 38 NH2-terminal amino acids are identical to those of
an IGFBP sequence derived from a human cDNA that cross-hybridizes with the
rat IGFBP-2 cDNA. With probes encoding a NH2-terminal, COOH-terminal, and a
middle region of this protein we have obtained three cDNA clones from a Hep
G2 cDNA library; one encodes human IGFBP-2, and the other two presumably
represent unspliced heteronuclear and alternatively spliced mRNA,
respectively. A 28-30-kDa IGFBP represents a novel BP species in human
serum. Its 30 NH2-terminal amino acids are not homologous to IGFBP-1, -2,
or -3. It is not digestible with N-glycanase and does not bind 125I-IGF I.
The NH2-terminal sequences of a 42/45- and a 31-kDa IGFBP are identical to
that of human IGFBP-3. The 42/45-kDa proteins are two glycosylation
variants of BP-3. The 31-kDa protein presumably is a degradation product of
BP-3 that lacks the COOH terminus. It is likely that the different IGFBPs
modulate auto-/paracrine and endocrine effects of IGFs on growth and
metabolism in a different and specific manner.
Isolation from adult human serum of four insulin-like growth factor (IGF) binding proteins and molecular cloning of one of them that is increased by IGF I administration and in extrapancreatic tumor hypoglycemia
Department of Medicine, University Hospital, Zurich CH-8091, Switzerland.
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