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Antiserum Developed for the E Peptide Region of Insulin-Like Growth Factor IA Prohormone Recognizes a Serum Protein by Both Immunoblot and Radioimmunoassay^*

Department of Pediatrics, Stanford University Medical Center Stanford, California 94305
the Department of Pediatrics, Section of Nephrology, Baylor College of Medicine (D.R.P.) Houston, Texas 77054
the Division of Endocrinology, The Children's Hospital (P.D.K.L.) Denver, Colorado 80218
Peninsula Laboratories (D.C.) Belmont, California 94002

Address requests for reprints to: Dr. David R. Powell, Department of Pediatrics, Baylor College of Medicine, Diabetes Research Center, Suite 1246, 8080 North Stadium Drive, Houston, Texas 77054.

Nucleotide sequencing of the two known cDNAs encoding human insulin-like growth factor I (IGF-I) predicts two different prohormone forms of IGF-I. The predicted prohormone amino acid sequences (E peptide regions) extend the carboxy-terminus of IGF-I by either an additional 35 (IGF-IA) or 77 (IGF-IB) amino acids. We developed an antiserum directed against a synthetic peptide which is unique to the E peptide region of IGF-IA prohormone. In a RIA using this antiserum, synthetic E peptide immunoreactivity was found in the serum of patients with chronic renal failure. The protein recognized by this antiserum has a mol wt of about 13,000 by neutral gel filtration and about 19,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting. These data suggest that the E peptide region of the IGF-IA prohormone is expressed and circulates as part of the prohormone.

^* This work was supported by Research Grants DK-24085 and DK-33190 (to R.L.H.), DK-07781 and DK-38773 (to D.R.P.) from the NIH and a postdoctoral grant from the Juvenile Diabetes Foundation International (to P.D.K.L.).

Received January 5, 1987.

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