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)



Gene Review

STATH  -  statherin

Homo sapiens

Synonyms: STR, Statherin
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 STATH


High impact information on STATH


Chemical compound and disease context of STATH


Biological context of STATH


Anatomical context of STATH


Associations of STATH with chemical compounds

  • Salivary statherin contains a 15-amino acid hydroxyapatite binding domain (N15) that is loosely helical in solution [14].
  • Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva [18].
  • The 2 serine residues (positions 2 and 3) in statherin were identified as phosphoserine [18].
  • The NH2-terminal half of this Mr=5380 (43 amino acids) polypeptide was determined by automated Edman degradations (liquid phase) on native statherin [18].
  • Several fragments of statherin, 1-15 (SN15), 5-15 (SN11), 15-29 (SM15), 29-43 (SC15), 19-43 (SC25), and analogs of the N-terminal 15-residue sequence, where phosphoserines at positions 2 and 3 have been replaced by Ser (SNS15) and Asp (SNA15), respectively, were synthesized [19].

Other interactions of STATH

  • The HIS1 sequence data were also compared with that of STATH [11].
  • The human CSN2 and STATH genes were not expressed in the transchromosomal mice [20].
  • In this study, various fragments and derivatives of statherin and P-B peptide were consistently detected by RP-HPLC ESI-IT MS in 23 samples of human saliva [13].
  • Besides high quantities of human serum albumin, alpha-defensins 1-4 and minor amounts of cystatin A, statherin, basic PB salivary peptide and other unidentified components were detected [16].
  • The adsorption, at hydroxyapatite surfaces of neutral cystatin SN, acidic cystatin S and the phosphoserine-containing acidic cystatin S1 was compared to that of statherin [21].

Analytical, diagnostic and therapeutic context of STATH


  1. Structure and sequence determination of the gene encoding human salivary statherin. Sabatini, L.M., He, Y.Z., Azen, E.A. Gene (1990) [Pubmed]
  2. The role of salivary peptides in dental caries. Vitorino, R., Lobo, M.J., Duarte, J.R., Ferrer-Correia, A.J., Domingues, P.M., Amado, F.M. Biomed. Chromatogr. (2005) [Pubmed]
  3. Statherin and histatin 1 reduce parotid saliva-promoted Streptococcus mutans strain MT8148 adhesion to hydroxyapatite surfaces. Shimotoyodome, A., Kobayashi, H., Tokimitsu, I., Matsukubo, T., Takaesu, Y. Caries Res. (2006) [Pubmed]
  4. Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals. Goobes, G., Goobes, R., Schueler-Furman, O., Baker, D., Stayton, P.S., Drobny, G.P. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  5. Salivary statherin peptide-binding epitopes of commensal and potentially infectious Actinomyces spp. delineated by a hybrid peptide construct. Niemi, L.D., Johansson, I. Infect. Immun. (2004) [Pubmed]
  6. A peptide that inhibits hydroxyapatite growth is in an extended conformation on the crystal surface. Long, J.R., Dindot, J.L., Zebroski, H., Kiihne, S., Clark, R.H., Campbell, A.A., Stayton, P.S., Drobny, G.P. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  7. cDNA cloning and chromosomal localization (4q11-13) of a gene for statherin, a regulator of calcium in saliva. Sabatini, L.M., Carlock, L.R., Johnson, G.W., Azen, E.A. Am. J. Hum. Genet. (1987) [Pubmed]
  8. Identification of protein components in human acquired enamel pellicle and whole saliva using novel proteomics approaches. Yao, Y., Berg, E.A., Costello, C.E., Troxler, R.F., Oppenheim, F.G. J. Biol. Chem. (2003) [Pubmed]
  9. Actinomyces naeslundii displays variant fimP and fimA fimbrial subunit genes corresponding to different types of acidic proline-rich protein and beta-linked galactosamine binding specificity. Hallberg, K., Holm, C., Ohman, U., Strömberg, N. Infect. Immun. (1998) [Pubmed]
  10. The effect of statherin and its shortened analogues on anaerobic bacteria isolated from the oral cavity. Kochańska, B., Kedzia, A., Kamysz, W., Maćkiewicz, Z., Kupryszewski, G. Acta Microbiol. Pol. (2000) [Pubmed]
  11. Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family. Sabatini, L.M., Ota, T., Azen, E.A. Mol. Biol. Evol. (1993) [Pubmed]
  12. Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. Iontcheva, I., Oppenheim, F.G., Offner, G.D., Troxler, R.F. J. Dent. Res. (2000) [Pubmed]
  13. Detection in human saliva of different statherin and P-B fragments and derivatives. Inzitari, R., Cabras, T., Rossetti, D.V., Fanali, C., Vitali, A., Pellegrini, M., Paludetti, G., Manni, A., Giardina, B., Messana, I., Castagnola, M. Proteomics (2006) [Pubmed]
  14. Chimeric peptides of statherin and osteopontin that bind hydroxyapatite and mediate cell adhesion. Gilbert, M., Shaw, W.J., Long, J.R., Nelson, K., Drobny, G.P., Giachelli, C.M., Stayton, P.S. J. Biol. Chem. (2000) [Pubmed]
  15. Tissue distribution of RNAs for cystatins, histatins, statherin, and proline-rich salivary proteins in humans and macaques. Sabatini, L.M., Warner, T.F., Saitoh, E., Azen, E.A. J. Dent. Res. (1989) [Pubmed]
  16. Peptides of human gingival crevicular fluid determined by HPLC-ESI-MS. Pisano, E., Cabras, T., Montaldo, C., Piras, V., Inzitari, R., Olmi, C., Castagnola, M., Messana, I. Eur. J. Oral Sci. (2005) [Pubmed]
  17. mRNAs for PRPs, statherin, and histatins in von Ebner's gland tissues. Azen, E.A., Hellekant, G., Sabatini, L.M., Warner, T.F. J. Dent. Res. (1990) [Pubmed]
  18. Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva. Schlesinger, D.H., Hay, D.I. J. Biol. Chem. (1977) [Pubmed]
  19. Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization. Raj, P.A., Johnsson, M., Levine, M.J., Nancollas, G.H. J. Biol. Chem. (1992) [Pubmed]
  20. Controlled transgene dosage and PAC-mediated transgenesis in mice using a chromosomal vector. Voet, T., Schoenmakers, E., Carpentier, S., Labaere, C., Marynen, P. Genomics (2003) [Pubmed]
  21. The effects of human salivary cystatins and statherin on hydroxyapatite crystallization. Johnsson, M., Richardson, C.F., Bergey, E.J., Levine, M.J., Nancollas, G.H. Arch. Oral Biol. (1991) [Pubmed]
  22. Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva. Ramasubbu, N., Reddy, M.S., Bergey, E.J., Haraszthy, G.G., Soni, S.D., Levine, M.J. Biochem. J. (1991) [Pubmed]
  23. Pellicle precursor protein crosslinking characterization of an adduct between acidic proline-rich protein (PRP-1) and statherin generated by transglutaminase. Yao, Y., Lamkin, M.S., Oppenheim, F.G. J. Dent. Res. (2000) [Pubmed]
  24. Human submandibular gland statherin and basic histidine-rich peptide are encoded by highly abundant mRNA's derived from a common ancestral sequence. Dickinson, D.P., Ridall, A.L., Levine, M.J. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
  25. Characterization of the immunologic responses to human in vivo acquired enamel pellicle as a novel means to investigate its composition. Li, J., Helmerhorst, E.J., Corley, R.B., Luus, L.E., Troxler, R.F., Oppenheim, F.G. Oral Microbiol. Immunol. (2003) [Pubmed]
WikiGenes - Universities