Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

S100A12 - S100 calcium binding protein A12...

Bos taurus

Hitomi, J., Yamashita, K., Liu, S.H., Oyama, Y., Okada, M., et al.

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Disease relevance of S100A12

Purification of bovine S100A12 from recombinant Escherichia coli [1].

High impact information on S100A12

On the other hand, our ELISA studies showed that CAAF1 protein was present in amniotic fluid at a concentration of about 120 nM, which was over 30 times as high as that in the fetal serum [2].
An especially characteristic staining pattern was obtained in the squamous epithelium, including that of the esophagus, skin and amnion: CAAF1 was detected in the suprabasal squamous epithelial cells undergoing differentiation, but not in the cells in the proliferating basal layer [2].
Northern blot analysis also showed that CAAF1 mRNA was highly expressed in bovine fetal esophagus and skin [2].
A novel calcium-binding protein in amniotic fluid, CAAF1: its molecular cloning and tissue distribution [2].
These results suggested that CAAF1 is one of the stage-specific proteins in the differentiation of squamous epithelial cells, and that CAAF1 is preferentially produced by fetal squamous epithelial cells, including epidermal keratinocytes and amniotic epithelial cells, and it is stored in the amniotic fluid during embryogenesis [2].

Biological context of S100A12

The purified protein was identical to native S100A12 in the N-terminal amino acid sequence, lysylendopeptidase peptide mapping, mass spectrum, and Ca2+-dependent binding affinity to amlexanox, an antiallergy drug [1].
S100A12, a member of the S100 family of EF-hand calcium-binding proteins, was purified from Escherichia coli cells expressing the corresponding cDNA [1].
The proteins identified by deduced amino acid sequences demonstrate 100% sequence homology with human and bovine calgranulin C [3].

Anatomical context of S100A12

The sequence of CO-Ag shows a high homology with calgranulin C (CaG-C) previously purified from pig granulocytes [4].

Associations of S100A12 with chemical compounds

Recently, we reported that two antiallergic drugs, Amlexanox and Cromolyn, bind to S100A12 and S100A13 of the S100 protein family [5].
The number of Ca2+ -binding sites for the CO-Ag sub-unit is approximately half that of the CaG-C monomer, although these two proteins have a similar low binding constant of approximately 2 x 10(-4) M [4].

Other interactions of S100A12

These proteins were as follows: bovine calgranulin C homolog, an 8-kDa unknown protein, S-100L, calgranulin B, calcyphosine, and annexins I-V [6].

References

Purification of bovine S100A12 from recombinant Escherichia coli. Yamashita, K., Oyama, Y., Shishibori, T., Matsushita, O., Okabe, A., Kobayashi, R. Protein Expr. Purif. (1999)
A novel calcium-binding protein in amniotic fluid, CAAF1: its molecular cloning and tissue distribution. Hitomi, J., Yamaguchi, K., Kikuchi, Y., Kimura, T., Maruyama, K., Nagasaki, K. J. Cell. Sci. (1996)
Cloning and sequence analysis of human and bovine corneal antigen (CO-Ag) cDNA: identification of host-parasite protein calgranulin C. Gottsch, J.D., Stark, W.J., Liu, S.H. Transactions of the American Ophthalmological Society. (1997)
Amino acid sequence of an immunogenic corneal stromal protein. Liu, S.H., Gottsch, J.D. Invest. Ophthalmol. Vis. Sci. (1996)
Interaction of S100 proteins with the antiallergic drugs, olopatadine, amlexanox, and cromolyn: identification of putative drug binding sites on S100A1 protein. Okada, M., Tokumitsu, H., Kubota, Y., Kobayashi, R. Biochem. Biophys. Res. Commun. (2002)
Two distinct anti-allergic drugs, amlexanox and cromolyn, bind to the same kinds of calcium binding proteins, except calmodulin, in bovine lung extract. Oyama, Y., Shishibori, T., Yamashita, K., Naya, T., Nakagiri, S., Maeta, H., Kobayashi, R. Biochem. Biophys. Res. Commun. (1997)