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Gene Review

S100P  -  S100 calcium binding protein P

Homo sapiens

Synonyms: MIG9, Migration-inducing gene 9 protein, Protein S100-E, Protein S100-P, S100 calcium-binding protein P, ...
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Disease relevance of S100P

  • These data suggest that an interaction between S100P and S100PBPR may be involved in early pancreatic cancer [1].
  • S100P is a member of the S100 family of calcium-binding proteins and there have been several recent reports of its overexpression in pancreatic ductal adenocarcinoma (PDAC) [1].
  • The cDNA was expressed in Escherichia coli and recombinant S100P was purified in high yield [2].
  • In a group of 303 breast cancer patients followed for up to 20 years, antibodies to S100P immunocytochemically stain 161 primary tumors [3].
  • Survival of patients with S100P-positive carcinomas is significantly worse by about 7-fold than for those with negatively stained carcinomas [3].

High impact information on S100P

  • Positive staining for S100P is significantly associated with that for two other metastasis-inducing proteins, S100A4 and osteopontin [3].
  • Induction of metastasis by S100P in a rat mammary model and its association with poor survival of breast cancer patients [3].
  • Transfection of an expression vector for S100P into a benign, nonmetastatic rat mammary cell line causes a 4- to 6-fold increase in its level in all four transformant cell clones [3].
  • Support for the success of the neoplastic cell gene expression identification strategy was obtained by immunocytochemical localization of four representative genes, 14-3-3sigma, S100P, S100A6, and beta4 integrin, to neoplastic cells in pancreatic tumors [4].
  • Expression of S100P and its novel binding partner S100PBPR in early pancreatic cancer [1].

Chemical compound and disease context of S100P


Biological context of S100P


Anatomical context of S100P

  • S100PBPR was found to localize to cell nuclei where S100P is also present, and the two proteins co-immunoprecipitate [1].
  • S100P-ezrin complex formation is Ca2+ dependent and most likely occurs within cells because both proteins colocalize at the plasma membrane after growth factor or Ca2+ ionophore stimulation [8].
  • The majority of Alzheimer type II glia (Alzg II) showed prominent immunoreactivity for S100P but not for GFAP, resembling normal astrocytes of protoplasmic type; Alzg II might be interpreted as being peculiar types of reactive astrocytes retaining characteristics of protoplasmic astrocytes [10].
  • S100P expression in human esophageal epithelial cells: Human esophageal epithelial cells sequentially produce different S100 proteins in the process of differentiation [11].
  • S100P was detected in vivo in the suprabasal layers of the epithelium [11].

Associations of S100P with chemical compounds

  • We have named this protein S100PBPR, and shown that its interaction with S100P is dependent on Ca(2+) or Mg(2+) [1].
  • Combined treatment with 5-aza-2'-deoxycytidie and trichostatin A resulted in synergistic induction of maspin and S100P mRNA in MiaPaCa2 cells where both genes were methylated [12].
  • Of these residues, F-15 is crucially important as a mutation to alanine abolishes dimerization even when the F15A S100P mutant polypeptide is allowed to interact with a wild-type chain [13].
  • Regulation of S100P expression by androgen [14].
  • Determination of mRNA and protein levels by real-time PCR and Western blotting revealed that IL6 is a more potent inducer of S100P than the synthetic androgen, R1881, in the LNCaP/C4-2B model of PCa progression [5].

Physical interactions of S100P

  • The S100P binding site is located in the N-terminal domain of ezrin and is accessible for interaction in dormant ezrin, in which binding sites for F-actin and transmembrane proteins are masked through an association between the N- and C-terminal domains [8].

Regulatory relationships of S100P


Other interactions of S100P

  • The encoded 99-amino acid protein, designated S100Z, is capable of interacting with another member of the family, S100P [17].
  • Since the placenta protein of 95 amino acid residues shares about 50% sequence identity with the brain S100 proteins alpha and beta, we proposed the name S100P [2].
  • The pattern of immunoreactivity for CK, S100P and CEA confirms previously reported data, while the B72.3-/Ber-EP4-/CD68+ staining profile represents a novel observation [18].
  • The protein exists as a homodimer formed by non-covalent interactions between large hydrophobic areas on monomeric S100P [9].
  • Like R1881, IL6 was unable to induce S100P in PC3 cells that lack a functional AR [5].

Analytical, diagnostic and therapeutic context of S100P

  • To isolate such target(s) of the S100P protein we devised an affinity chromatography approach that selects for S100 protein ligands requiring the biologically active S100 dimer for interaction [8].
  • Experiments with an optical biosensor to study binding parameters of the S100P monomer interaction showed that the association rate constant was faster in the presence of calcium than in their absence, whereas the dissociation rate constant was independent of calcium [9].
  • One of the most highly overexpressed genes in hormone-refractory CWR22R xenografts was the S100P gene [19].
  • In this study we used fluorescence and CD spectroscopies and isothermal titration calorimetry to characterize the target-recognition properties of S100P using a model peptide, melittin [20].
  • Quantitative RT-PCR on S100P gene expression was analyzed in 6 patients and 14 controls [21].


  1. Expression of S100P and its novel binding partner S100PBPR in early pancreatic cancer. Dowen, S.E., Crnogorac-Jurcevic, T., Gangeswaran, R., Hansen, M., Eloranta, J.J., Bhakta, V., Brentnall, T.A., Lüttges, J., Klöppel, G., Lemoine, N.R. Am. J. Pathol. (2005) [Pubmed]
  2. S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning, recombinant protein expression and Ca2+ binding properties. Becker, T., Gerke, V., Kube, E., Weber, K. Eur. J. Biochem. (1992) [Pubmed]
  3. Induction of metastasis by S100P in a rat mammary model and its association with poor survival of breast cancer patients. Wang, G., Platt-Higgins, A., Carroll, J., de Silva Rudland, S., Winstanley, J., Barraclough, R., Rudland, P.S. Cancer Res. (2006) [Pubmed]
  4. Molecular profiling of pancreatic adenocarcinoma and chronic pancreatitis identifies multiple genes differentially regulated in pancreatic cancer. Logsdon, C.D., Simeone, D.M., Binkley, C., Arumugam, T., Greenson, J.K., Giordano, T.J., Misek, D.E., Kuick, R., Hanash, S. Cancer Res. (2003) [Pubmed]
  5. Interleukin-6 is a potent inducer of S100P, which is up-regulated in androgen-refractory and metastatic prostate cancer. Hammacher, A., Thompson, E.W., Williams, E.D. Int. J. Biochem. Cell Biol. (2005) [Pubmed]
  6. Immediate up-regulation of the calcium-binding protein S100P and its involvement in the cytokinin-induced differentiation of human myeloid leukemia cells. Ishii, Y., Kasukabe, T., Honma, Y. Biochim. Biophys. Acta (2005) [Pubmed]
  7. Retinoic acid increases expression of the calcium-binding protein S100P in human gastric cancer cells. Shyu, R.Y., Huang, S.L., Jiang, S.Y. J. Biomed. Sci. (2003) [Pubmed]
  8. Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P. Koltzscher, M., Neumann, C., König, S., Gerke, V. Mol. Biol. Cell (2003) [Pubmed]
  9. The crystal structure at 2A resolution of the Ca2+ -binding protein S100P. Zhang, H., Wang, G., Ding, Y., Wang, Z., Barraclough, R., Rudland, P.S., Fernig, D.G., Rao, Z. J. Mol. Biol. (2003) [Pubmed]
  10. Glial fibrillary acidic protein and S-100 protein in human hepatic encephalopathy: immunocytochemical demonstration of dissociation of two glia-associated proteins. Kimura, T., Budka, H. Acta Neuropathol. (1986) [Pubmed]
  11. S100P expression in human esophageal epithelial cells: Human esophageal epithelial cells sequentially produce different S100 proteins in the process of differentiation. Sato, N., Hitomi, J. Anat. Rec. (2002) [Pubmed]
  12. Identification of maspin and S100P as novel hypomethylation targets in pancreatic cancer using global gene expression profiling. Sato, N., Fukushima, N., Matsubayashi, H., Goggins, M. Oncogene (2004) [Pubmed]
  13. Identification of hydrophobic amino acid residues involved in the formation of S100P homodimers in vivo. Koltzscher, M., Gerke, V. Biochemistry (2000) [Pubmed]
  14. Regulation of S100P expression by androgen. Averboukh, L., Liang, P., Kantoff, P.W., Pardee, A.B. Prostate (1996) [Pubmed]
  15. S-phase reduction in T47D human breast cancer epithelial cells induced by an S100P antisense-retroviral construct. Beissel, B., Silva, I.D., Pesquero, J.B., Russo, J., Schor, N., Bellini, M.H. Oncol. Rep. (2007) [Pubmed]
  16. Gene expression changes following androgen receptor elimination in LNCaP prostate cancer cells. Eder, I.E., Haag, P., Basik, M., Mousses, S., Bektic, J., Bartsch, G., Klocker, H. Mol. Carcinog. (2003) [Pubmed]
  17. Molecular characterization and tissue distribution of a novel member of the S100 family of EF-hand proteins. Gribenko, A.V., Hopper, J.E., Makhatadze, G.I. Biochemistry (2001) [Pubmed]
  18. Decisive role of immunocytochemistry in aspiration cytology of chordoma of the clivus: a case report with review of the literature. Gherardi, G., Marveggio, C., Cola, C., Redaelli, G. The Journal of laryngology and otology. (1994) [Pubmed]
  19. Clinical validation of candidate genes associated with prostate cancer progression in the CWR22 model system using tissue microarrays. Mousses, S., Bubendorf, L., Wagner, U., Hostetter, G., Kononen, J., Cornelison, R., Goldberger, N., Elkahloun, A.G., Willi, N., Koivisto, P., Ferhle, W., Raffeld, M., Sauter, G., Kallioniemi, O.P. Cancer Res. (2002) [Pubmed]
  20. Conformational and thermodynamic properties of peptide binding to the human S100P protein. Gribenko, A.V., Guzmán-Casado, M., Lopez, M.M., Makhatadze, G.I. Protein Sci. (2002) [Pubmed]
  21. Gene expression profiling in cluster headache: a pilot microarray study. Sj??strand, C., Duvefelt, K., Steinberg, A., Remahl, I.N., Waldenlind, E., Hillert, J. Headache (2006) [Pubmed]
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