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Type: Protein
Species Reactivity: H; R
B=Bovine; Ca=Cat; Ch=Chicken; D=Dog; EQ=Equine; GP=Guinea Pig; H=Human; M=Mouse; P=Porcine; Pr=Primate; R=Rat; Rb=Rabbit; Y=Yeast; Xe=Xenopus; Ze=Zebrafish; ; ; ; NA-Not Applicable; STP=Step-Tactin Proteins; All

S100A13 is an 11 kDa member of the S100 (soluble in 100% saturated ammonium sulfate) family of vertebrate EFhand Ca++binding proteins (1 3). It is widely expressed as a homodimer with two 98 amino acid (aa) long subunits (2, 3). Human S100A13 shares 83%, 90%, 91%, 87%, 78% and 47% aa identity with mouse, rat, cow, dog, opossum and chicken S100A13, respectively. Like other S100 proteins, S100A13 is small and generally acidic, but contains a basic residuerich sequence at the C-terminus, and two EF hand motifs that bind with Ca++ differing affinities (2 4). Some S100 proteins, including S100A13, are able to bind the cell surface receptor for advanced glycation endproducts (RAGE) (5).

Image: S100A13-Induced Neurite Outgrowth.Recombinant human S100A13 immobilized on a nitrocellulose- coated microplate.

Despite lacking a signal sequence, S100A13 plays an important role in Cu++dependent export of FGF1 (FGF acidic) and IL1α from the cell in response to stresses such as heat shock, anoxia and starvation (6 8). Binding of copper is necessary for formation of a multiprotein complex between S100A13, FGF1 and p40 synaptotagmin1 (syt1) (9, 10). Cu++ ions supplied by S100A13 are thought to oxidize and downregulate the activity of FGF1 prior to export (10). Calcium influx may also play a similar role in FGF1 release from neuronal cells (11). S100A13 is composed of four amphiphilic helices that may interact with acidic phospholipid headgroups. With FGF1 and syt1, S100A13 likely perturbs the membrane, which allows the S100A13 protein complex to exit the cell (4, 12). S100A13 has been proposed as a marker for angiogenesis in tumors and endometrium, due to its role in stress induced export of FGF1 (13, 14). Based on in house studies, S100A13 has also been found to promote neurite outgrowth from rat cortical embryonic neurons.


1. SantamariaKisiel,
L. et al. (2006) Biochem. J. 396:201.
2. Wicki, R. et al. (1996) Biochem. Biophys. Res. Commun.227:594.
3. Ridinger, K. et al. (2000) J. Biol. Chem. 275:8686.
4. Li, M. et al. (2007) Biochem. Biophys. Res. Commun.356:616.
5. Hsieh, al. (2004) Biochem. Biophys. Res. Commun.316:949.
6. Landriscina, M. et al. (2001) J. Biol. Chem. 276:22544.
7. Sivaraja, V. et al. (2006) Biophys. J. 91:1832.
8. Mandinova, A. et al. (2003) J. Cell Sci. 116:2687.
9. Prudovsky, I. et al. (2002) J. Cell Biol. 158:201.
10. Landriscina, M. et al. (2001) J. Biol. Chem. 276:25549.
11. Matsunaga, H. and H. Ueda (2006) Cell. Mol. Neurobiol.
26:237.12. Graziani, I. et al. (2006) Biochem. Biophys. Res. Commun.349:192.
13. Landriscina, M. et al. (2006) J. Neurooncol. 80:251.
14. Hayrabedyan, S. et al. (2005) Reprod. Biol. 5:51.