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(Received for publication, May 6, 1996, and in revised form, September 10, 1996)
From the Department of Cell Biology and Kaplan Cancer Center and
the Raymond and Beverly Sackler Foundation Laboratory, Most cultured cell types secrete small latent
transforming growth factor-
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29891-29896
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Binding Protein-1 that
Mediates Bonding to the Latent Transforming Growth Factor-1
(TGF-) as a disulfide-bonded complex
with a member of the latent TGF- binding protein (LTBP) family.
Using the baculovirus expression system, we have mapped the domain of
LTBP-1 mediating covalent association with small latent TGF-1.
Coexpression in Sf9 cells of small latent TGF-1 with deletion
mutants of LTBP-1 showed that the third eight-cysteine repeat of LTBP-1
is necessary and sufficient for covalent interaction with small latent
TGF-1. Analysis by mass spectrometry of this eight-cysteine repeat,
produced as a recombinant peptide in Sf9 cells, confirmed that it was
N-glycosylated, as expected from the primary sequence. No
other post-translational modifications of this domain were detected.
Alkylation of the recombinant peptide with vinyl pyridine failed to
reveal any free cysteines, indicating that, in the absence of small
latent TGF-, the eight cysteines of this domain are engaged in
intramolecular bonds. These data demonstrate that the third LTBP-1
eight-cysteine repeat recognizes and associates covalently with small
latent TGF-1 through a mechanism that does not require any specific post-translational modification of this domain. They also suggest that
this domain adopts different conformations depending on whether it is
free or bound to small latent TGF-.
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