Phosphorylation of insulin-like growth factor binding protein-1 in patients with insulin-dependent diabetes mellitus and severe trauma
RA Frost, A Bereket, TA Wilson, MM Wojnar, CH Lang and MC Gelato
Department of Medicine, State University of New York at Stony Brook 11794.
We have determined the level of phosphorylated insulin-like growth factor
binding protein-1 (pIGFBP-1) in serum during two catabolic states: diabetes
mellitus and trauma. Human sera were incubated with [125I]IGF-I for 2 h
followed by non-denaturing PAGE. [125I]IGF-I/IGFBP- 1 complexes from serum
co-migrated with a pure p4IGFBP-1 standard. Complex formation was
specifically inhibited by unlabeled IGF-I. The migration of IGF-I/pIGFBP-1
complexes was retarded by IGFBP-1 antibodies, but not by antibodies against
IGFBP-2 or IGFBP-3. Sera from three severely traumatized patients had up to
12-fold more pIGFBP-1 than sera from age-matched controls. The level of
pIGFBP-1 was reduced in all three patients upon hospital discharge. Sera
from three patients with insulin dependent diabetes mellitus (IDDM) and
severe ketoacidosis (DKA) had more pIGFBP-1 than controls. Administration
of insulin to DKA patients lowered the level of pIGFBP-1. The present study
shows that IGFBP-1 exists as a free, high affinity, phosphorylated form in
vivo during two catabolic states.
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