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Gene Review:

S100A4 - S100 calcium binding protein A4

Bos taurus

Duarte, W.R. et al., Polans, A.S. et al., Duarte, W.R. et al., Duarte, W.R. et al.

Duarte, Iimura, Takenaga, Ohya, Ishikawa, Kasugai,

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High impact information on S100A4

The complete amino acid sequence of bovine Capl was established primarily by Edman degradation of peptides generated by cleavage of methionyl, lysyl, glutamyl, and aspartyl bonds [1].
Northern analysis using cloned Capl cDNA revealed that Capl mRNA is present not only in the retina but the choroid as well [1].
In addition, the expression of Capl correlates with the induction of the metastatic phenotype in tumor cell lines and the transformation of normal cells by activated oncogenes or chemical carcinogens [1].
Since there was a marked difference of S100A4 expression between PDL and gingiva, we propose that S100A4 could be a useful marker for distinguishing cells from these two tissues [2].
S100A4 expression was also high in the pulp tissue followed by the dental papilla of the tooth germ [2].

Biological context of S100A4

It is conceivable that the high expression of S100A4 in PDLE is a result of the maturation of the PDL and/or a response to mechanical stress generated by mastication [2].

Anatomical context of S100A4

PDL from teeth under eruption (PDLU) showed a lower expression of S100A4, and its expression in gingiva was faintly detectable [2].
Extracellular role of S100A4 calcium-binding protein in the periodontal ligament [3].

Other interactions of S100A4

Interestingly, only PDLE exhibited a high expression of both S100A4 and S100A2 [2].
Similarly, when bovine PDL cells were mechanically stimulated by means of the Flexercell Strain Unit, the expression of S100A4, beta-actin, and alpha-tubulin mRNAs increased over the control levels [4].

Analytical, diagnostic and therapeutic context of S100A4

In northern blotting analysis, the highest expression of S100A4 was detected in PDL from erupted teeth (PDLE) [2].
In the present study we showed by in situ hybridization that periodontal ligament (PDL) cells express the S100A4 mRNA [3].
Immunolocalization of the S100A4 protein in cryosections of PDL and analyses of PDL cell culture medium revealed that PDL cells secrete the S100A4 protein both in vivo and in vitro [3].

References

Purification and primary structure of Capl, an S-100-related calcium-binding protein isolated from bovine retina. Polans, A.S., Palczewski, K., Asson-Batres, M.A., Ohguro, H., Witkowska, D., Haley, T.L., Baizer, L., Crabb, J.W. J. Biol. Chem. (1994) [Pubmed]
cDNA cloning of S100 calcium-binding proteins from bovine periodontal ligament and their expression in oral tissues. Duarte, W.R., Kasugai, S., Iimura, T., Oida, S., Takenaga, K., Ohya, K., Ishikawa, I. J. Dent. Res. (1998) [Pubmed]
Extracellular role of S100A4 calcium-binding protein in the periodontal ligament. Duarte, W.R., Iimura, T., Takenaga, K., Ohya, K., Ishikawa, I., Kasugai, S. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
Effects of mechanical stress on the mRNA expression of S100A4 and cytoskeletal components by periodontal ligament cells. Duarte, W.R., Mikuni-Takagaki, Y., Kawase, T., Limura, T., Oida, S., Ohya, K., Takenaga, K., Ishikawa, L., Kasugai, S. J. Med. Dent. Sci. (1999) [Pubmed]

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S100A4	Canis lupus familiaris
icn2	Danio rerio
icn	Danio rerio
S100A4	Gallus gallus
S100A4	Homo sapiens
S100A4	Macaca mulatta
S100a4	Mus musculus
S100A4	Pan troglodytes
S100a4	Rattus norvegicus

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