The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

S100A3  -  S100 calcium binding protein A3

Homo sapiens

Synonyms: Protein S-100E, Protein S100-A3, S100 calcium-binding protein A3, S100E
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of S100A3

 

High impact information on S100A3

  • The crystal structure of S100A3 allows the prediction of one putative Zn(2+) binding site in the C terminus of each subunit of S100A3 involving Cys and His residues in the coordination of the metal ion [4].
  • S100A3 is a unique member of the EF-hand superfamily of Ca(2+)-binding proteins [4].
  • This high affinity for Zn(2+) is attributed to the unusual high Cys content of S100A3 [4].
  • Of the 10 Cys residues in S100A3, 5 only are free thiols, and accessible to 5,5'-dithiobis(2-nitro-benzoic acid); they display a high reactivity in the metal-free and Ca2+ form, but a 20-fold lowered reactivity in the Zn2+ form of S100A3 [5].
  • Purification and cation binding properties of the recombinant human S100 calcium-binding protein A3, an EF-hand motif protein with high affinity for zinc [5].
 

Biological context of S100A3

 

Anatomical context of S100A3

  • The S100A3 antibody only stained the inner root sheath cuticle of some hair follicles but no melanocytes or melanocytic lesions [9].
  • Aberrantly differentiated cells in benign pilomatrixoma reflect the normal hair follicle: immunohistochemical analysis of Ca-binding S100A2, S100A3 and S100A6 proteins [2].
  • In the endocuticle, S100A3 was present on the inner portion of the endocuticle adjacent to the cell membrane complex, whereas hair keratins were present on the outer portion [7].
  • In the hair shaft, S100A3 was primarily identified in the endocuticle and was also present in the intermacrofibrillar matrix surrounding macrofibril bundles of intermediate filament keratins in cortex cells [7].
 

Associations of S100A3 with chemical compounds

  • Iodide replaces a water molecule at the surface of the S100A3 protein, whereas xenon binds in a hydrophobic cavity at the dimer interface [6].
  • Metal-free S100A3, a cysteine-rich Ca(2+)- and Zn(2+)-binding protein, has been crystallized by vapour diffusion under the strict exclusion of oxygen and in the absence of divalent metal ions [6].
  • Tandem mass spectrometry of the peptides resulting from endoproteinase digest of cuticle S100A3 revealed that the N-terminal methionine is replaced with an acetyl group [10].
  • The transition metal ions Co2+, Zn2+ and Cd2+ were used as spectroscopic probes to investigate the role of the 10 cysteine residues per monomer S100A3 in metal binding [11].
  • At the minimum concentration of thioglycolate required to elute S100A3 protein from the endocuticle into the reductive permanent waving lotion, enlarged delaminated cuticle fragments were observed [12].
  • Gel filtration analyses showed that either enzymatic conversion of Arg-51 in S100A3 to citrulline or its mutational substitution with alanine (R51A) promotes a homotetramer assembly [13].
 

Other interactions of S100A3

  • S100A1 and S100A3 antibodies are not expressed in melanocytic lesions and S100A2 is only found in selected tumours [9].
  • In sharp contrast, the levels of expression of the S100A3 and S100A5 proteins differed markedly in the solid tumour tissue in relation to the astrocytic tumour types and grades [14].
 

Analytical, diagnostic and therapeutic context of S100A3

References

  1. Supratentorial pilocytic astrocytomas, astrocytomas, anaplastic astrocytomas and glioblastomas are characterized by a differential expression of S100 proteins. Camby, I., Nagy, N., Lopes, M.B., Schäfer, B.W., Maurage, C.A., Ruchoux, M.M., Murmann, P., Pochet, R., Heizmann, C.W., Brotchi, J., Salmon, I., Kiss, R., Decaestecker, C. Brain Pathol. (1999) [Pubmed]
  2. Aberrantly differentiated cells in benign pilomatrixoma reflect the normal hair follicle: immunohistochemical analysis of Ca-binding S100A2, S100A3 and S100A6 proteins. Kizawa, K., Toyoda, M., Ito, M., Morohashi, M. Br. J. Dermatol. (2005) [Pubmed]
  3. S100A3 mRNA expression displays an inverse correlation to breast cancer progression. Lloyd, B.H., Ruddell, C., Rudland, P.S., Barraclough, R. Biochem. Soc. Trans. (1996) [Pubmed]
  4. The crystal structure of metal-free human EF-hand protein S100A3 at 1.7-A resolution. Fritz, G., Mittl, P.R., Vasak, M., Grutter, M.G., Heizmann, C.W. J. Biol. Chem. (2002) [Pubmed]
  5. Purification and cation binding properties of the recombinant human S100 calcium-binding protein A3, an EF-hand motif protein with high affinity for zinc. Föhr, U.G., Heizmann, C.W., Engelkamp, D., Schäfer, B.W., Cox, J.A. J. Biol. Chem. (1995) [Pubmed]
  6. Metal-free MIRAS phasing: structure of apo-S100A3. Mittl, P.R., Fritz, G., Sargent, D.F., Richmond, T.J., Heizmann, C.W., Grütter, M.G. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
  7. Ultrastructural localization of S100A3, a cysteine-rich, calcium binding protein, in human scalp hair shafts revealed by rapid-freezing immunocytochemistry. Takizawa, T., Takizawa, T., Arai, S., Kizawa, K., Uchiwa, H., Sasaki, I., Inoue, T. J. Histochem. Cytochem. (1999) [Pubmed]
  8. In situ RNA-RNA hybridisation of phospholipase C beta 3 shows lack of expression in neuroendocrine tumours. Stålberg, P., Granberg, D., Carling, T., Wilander, E., Eriksson, B., Gobl, A., Akerström, G., Rastad, J., Modlin, I.M., Oberg, K., Skogseid, B. Anticancer Res. (2003) [Pubmed]
  9. Immunohistochemical localization of the Ca2+ binding S100 proteins in normal human skin and melanocytic lesions. Böni, R., Burg, G., Doguoglu, A., Ilg, E.C., Schäfer, B.W., Müller, B., Heizmann, C.W. Br. J. Dermatol. (1997) [Pubmed]
  10. Characterization of the cysteine-rich calcium-binding S100A3 protein from human hair cuticles. Kizawa, K., Troxler, H., Kleinert, P., Inoue, T., Toyoda, M., Morohashi, M., Heizmann, C.W. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  11. Probing the structure of the human Ca2+- and Zn2+-binding protein S100A3: spectroscopic investigations of its transition metal ion complexes, and three-dimensional structural model. Fritz, G., Heizmann, C.W., Kroneck, P.M. Biochim. Biophys. Acta (1998) [Pubmed]
  12. Dissimilar effect of perming and bleaching treatments on cuticles: advanced hair damage model based on elution and oxidation of S100A3 protein. Kizawa, K., Inoue, T., Yamaguchi, M., Kleinert, P., Troxler, H., Heizmann, C.W., Iwamoto, Y. Journal of cosmetic science. (2005) [Pubmed]
  13. Specific citrullination causes assembly of a globular S100A3 homotetramer: a putative Ca2+ modulator matures human hair cuticle. Kizawa, K., Takahara, H., Troxler, H., Kleinert, P., Mochida, U., Heizmann, C.W. J. Biol. Chem. (2008) [Pubmed]
  14. Differential expression of S100 calcium-binding proteins characterizes distinct clinical entities in both WHO grade II and III astrocytic tumours. Camby, I., Lefranc, F., Titeca, G., Neuci, S., Fastrez, M., Dedecken, L., Schäfer, B.W., Brotchi, J., Heizmann, C.W., Pochet, R., Salmon, I., Kiss, R., Decaestecker, C. Neuropathol. Appl. Neurobiol. (2000) [Pubmed]
  15. Gene expression of mouse S100A3, a cysteine-rich calcium-binding protein, in developing hair follicle. Kizawa, K., Tsuchimoto, S., Hashimoto, K., Uchiwa, H. J. Invest. Dermatol. (1998) [Pubmed]
 
WikiGenes - Universities