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(Received for publication, September 5, 1996, and in revised form, September 30, 1996)
From the Department of Pediatrics, School of Medicine, Oregon
Health Sciences University, Portland, Oregon 97201
The mac25 cDNA was originally cloned from
leptomeningial cells and subsequently reisolated through differential
display as a sequence preferentially expressed in senescent human
mammary epithelial cells. The deduced amino acid sequence of the human mac25 propeptide shares a 20-25% identity to human insulin-like growth factor-binding proteins (IGFBPs), suggesting that mac25 could be
another member of the IGFBP family.
In the present study, we have generated recombinant human mac25
(rh-mac25) in a baculovirus expression system and assessed its affinity
for IGFs and have evaluated the pattern of expression of the mac25 gene
in human tissues. Binding of 125I-IGF-I and
125I-IGF-II to rh-mac25 was demonstrated by Western ligand
blotting after nondenaturing polyacrylamide gel electrophoresis and by affinity cross-linking with as little as 2 nM rh-mac25.
Specificity of rh-mac25 binding to 125I-IGFs was
demonstrated by competition for rh-mac25 binding with unlabeled IGFs,
but not with [QAYLL]IGF-II analog, which has 100-fold less affinity
for IGFBPs. In comparison with IGFBP-3, rh-mac25 has at least a
5-6-fold lower affinity for IGF-I and 20-25-fold lower affinity for
IGF-II. mac25 mRNA was detectable in a wide range of normal human
tissues, with decreased expression in breast, prostate, colon, and lung
cancer cell lines.
In conclusion, mac25 specifically binds IGFs and constitutes a new
member of the IGFBP family, IGFBP-7. Its wider distribution in normal
tissue and lower expression in several cancer cells indicate that
IGFBP-7 may function as a growth-suppressing factor, as well as an
IGF-binding protein.
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30322-30325
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
RECOMBINANT HUMAN mac25 PROTEIN SPECIFICALLY BINDS IGF-I AND
-II
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