STATH

Statherin
Identifiers
Symbols	STATH ; STR
External IDs	OMIM: 184470 HomoloGene: 88673 GeneCards: STATH Gene
Gene ontology Molecular function • protein binding • extracellular matrix constituent, lubricant activity • structural constituent of tooth enamel • hydroxyapatite binding Cellular component • extracellular region Biological process • ossification • negative regulation of bone mineralization • biomineral tissue development • defense response to bacterium • saliva secretion Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6779	n/a
Ensembl	ENSG00000126549	n/a
UniProt	P02808	n/a
RefSeq (mRNA)	NM_001009181	n/a
RefSeq (protein)	NP_001009181	n/a
Location (UCSC)	Chr 4: 70 – 70 Mb	n/a
PubMed search		n/a

Statherin is a protein in humans that is encoded by the STATH gene.^[1][2] It prevents calcium phospate precipitation in saliva maintaining a high calcium level saliva available for remineralisation of enamel and high phosphate levels for buffering.^[3]

References

1. Sabatini LM, Carlock LR, Johnson GW, Azen EA (Jan 1988). "cDNA cloning and chromosomal localization (4q11-13) of a gene for statherin, a regulator of calcium in saliva". Am J Hum Genet 41 (6): 1048–60. PMC 1684366. PMID 3502720.
2. "Entrez Gene: STATH statherin".
3. Hay DI, Smith DJ, Schluckebier SK, Moreno EC (1984). "Relationship between concentration of human salivary statherin and inhibition of calcium phosphate precipitation in stimulated human parotid saliva". J. Dent. Res. 63 (6): 857–63. doi:10.1177/00220345840630060901. PMID 6429216.

Further reading

• Schlesinger DH, Hay DI (1977). "Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva". J. Biol. Chem. 252 (5): 1689–95. PMID 838735.
• Raj PA, Johnsson M, Levine MJ, Nancollas GH (1992). "Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization". J. Biol. Chem. 267 (9): 5968–76. PMID 1313424.
• Douglas WH, Reeh ES, Ramasubbu N, Raj PA, Bhandary KK, Levine MJ (1991). "Statherin: a major boundary lubricant of human saliva". Biochem. Biophys. Res. Commun. 180 (1): 91–7. doi:10.1016/S0006-291X(05)81259-8. PMID 1718282.
• Johnsson M, Richardson CF, Bergey EJ, Levine MJ, Nancollas GH (1992). "The effects of human salivary cystatins and statherin on hydroxyapatite crystallization". Arch. Oral Biol. 36 (9): 631–6. doi:10.1016/0003-9969(91)90014-L. PMID 1741693.
• Ramasubbu N, Reddy MS, Bergey EJ, Haraszthy GG, Soni SD, Levine MJ (1992). "Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva". Biochem. J. 280 ( Pt 2) (Pt 2): 341–52. PMC 1130552. PMID 1747107.
• Sabatini LM, He YZ, Azen EA (1990). "Structure and sequence determination of the gene encoding human salivary statherin". Gene 89 (2): 245–51. doi:10.1016/0378-1119(90)90012-G. PMID 2373369.
• Sabatini LM, Warner TF, Saitoh E, Azen EA (1990). "Tissue distribution of RNAs for cystatins, histatins, statherin, and proline-rich salivary proteins in humans and macaques". J. Dent. Res. 68 (7): 1138–45. doi:10.1177/00220345890680070101. PMID 2483725.
• Dickinson DP, Ridall AL, Levine MJ (1988). "Human submandibular gland statherin and basic histidine-rich peptide are encoded by highly abundant mRNA's derived from a common ancestral sequence". Biochem. Biophys. Res. Commun. 149 (2): 784–90. doi:10.1016/0006-291X(87)90436-0. PMID 3426601.
• Oppenheim FG, Hay DI, Smith DJ, Offner GD, Troxler RF (1987). "Molecular basis of salivary proline-rich protein and peptide synthesis: cell-free translations and processing of human and macaque statherin mRNAs and partial amino acid sequence of their signal peptides". J. Dent. Res. 66 (2): 462–6. doi:10.1177/00220345870660021301. PMID 3476566.
• Perinpanayagam HE, Van Wuyckhuyse BC, Ji ZS, Tabak LA (1995). "Characterization of low-molecular-weight peptides in human parotid saliva". J. Dent. Res. 74 (1): 345–50. doi:10.1177/00220345950740011001. PMID 7876428.
• Gururaja TL, Levine MJ (1997). "Solid-phase synthesis and characterization of human salivary statherin: a tyrosine-rich phosphoprotein inhibitor of calcium phosphate precipitation". Pept. Res. 9 (6): 283–9. PMID 9048421.
• Iontcheva I, Oppenheim FG, Troxler RF (1997). "Human salivary mucin MG1 selectively forms heterotypic complexes with amylase, proline-rich proteins, statherin, and histatins". J. Dent. Res. 76 (3): 734–43. doi:10.1177/00220345970760030501. PMID 9109822.
• Iontcheva I, Oppenheim FG, Offner GD, Troxler RF (2000). "Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system". J. Dent. Res. 79 (2): 732–9. doi:10.1177/00220345000790020601. PMID 10728974.
• Gilbert M, Shaw WJ, Long JR, Nelson K, Drobny GP, Giachelli CM, Stayton PS (2000). "Chimeric peptides of statherin and osteopontin that bind hydroxyapatite and mediate cell adhesion". J. Biol. Chem. 275 (21): 16213–8. doi:10.1074/jbc.M001773200. PMID 10748043.
• Yao Y, Lamkin MS, Oppenheim FG (2000). "Pellicle precursor protein crosslinking characterization of an adduct between acidic proline-rich protein (PRP-1) and statherin generated by transglutaminase". J. Dent. Res. 79 (4): 930–8. doi:10.1177/00220345000790040801. PMID 10831095.
• Tamaki N, Tada T, Morita M, Watanabe T (2003). "Comparison of inhibitory activity on calcium phosphate precipitation by acidic proline-rich proteins, statherin, and histatin-1". Calcif. Tissue Int. 71 (1): 59–62. doi:10.1007/s00223-001-1084-0. PMID 12060866.
• Yao Y, Berg EA, Costello CE, Troxler RF, Oppenheim FG (2003). "Identification of protein components in human acquired enamel pellicle and whole saliva using novel proteomics approaches". J. Biol. Chem. 278 (7): 5300–8. doi:10.1074/jbc.M206333200. PMID 12444093.