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J. Biol. Chem., Vol. 276, Issue 25, 22544-22552, June 22, 2001
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Center for Molecular Medicine, Maine Medical Center Research
Institute, Scarborough, Maine 04074
S100A13, a member of the S100 gene family of
Ca2+-binding proteins has been previously
characterized as a component of a brain-derived heparin-binding
multiprotein aggregate/complex containing fibroblast growth factor 1 (FGF1). We report that while expression of S100A13 in NIH 3T3 cells
results in the constitutive release of S100A13 into the extracellular
compartment at 37 °C, co-expression of S100A13 with FGF1 represses
the constitutive release of S100A13 and enables NIH 3T3 cells to
release S100A13 in response to temperature stress. S100A13 release in
response to stress occurs with kinetics similar to that observed for
the stress-induced release of FGF1, but S100A13 expression is able to
reverse the sensitivity of FGF1 release to inhibitors of transcription
and translation. The release of FGF1 and S100A13 in response to heat
shock results in the solubility of FGF1 at 100% (w/v) ammonium sulfate
saturation, and the expression of a S100A13 deletion mutant lacking its
novel basic residue-rich domain acts as a dominant negative effector of
FGF1 release in vitro. Surprisingly, the expression of
S100A13 also results in the stress-induced release of a Cys-free FGF1
mutant, which is normally not released from NIH 3T3 cells in response
to heat shock. These data suggest that S100A13 may be a component of
the pathway for the release of the signal peptide-less polypeptide,
FGF1, and may involve a role for S100A13 in the formation of a
noncovalent FGF1 homodimer.
S100A13 Participates in the Release of Fibroblast Growth
Factor 1 in Response to Heat Shock in Vitro*
,
*
This work was supported in part by National Institutes of
Health Grants HL32348 and AG98503 (to T. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported in part by a fellowship from the Catholic University of Rome.
§
Present address: Dept. of Geriatric Medicine, University of
Florence, School of Medicine, Florence, Italy 50139.
¶
To whom correspondence should be addressed: Center for
Molecular Medicine, Maine Medical Center Research Institute, 81 Research Dr., Scarborough, ME 04074. Tel.: 207-885-8200; Fax:
207-885-8179; E-mail: maciat@mmc.org.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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