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Stathérine

La stathérine est une protéine spécifique jouant un rôle dans le maintien de calcium dans le suc pancréatique[1] - [2].

Notes et références

  1. (en) L. M. Sabatini, L. R. Carlock, G. W. Johnson et E. A. Azen, « cDNA cloning and chromosomal localization (4q11-13) of a gene for statherin, a regulator of calcium in saliva », Am J Hum Genet, vol. 41, no 6, , p. 1048–60 (PMID 3502720, PMCID 1684366)
  2. (en) « Entrez Gene: STATH statherin »

Bibliographie

  • (en) D. H. Schlesinger et D. I. Hay, « Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva », J. Biol. Chem., vol. 252, no 5, , p. 1689–95 (PMID 838735)
  • (en) P. A. Raj, M. Johnsson, M. J. Levine et G. H. Nancollas, « Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization », J. Biol. Chem., vol. 267, no 9, , p. 5968–76 (PMID 1313424)
  • (en) W. H. Douglas, E. S. Reeh, N. Ramasubbu, P. A. Raj, K. K. Bhandary et M. J. Levine, « Statherin: a major boundary lubricant of human saliva », Biochem. Biophys. Res. Commun., vol. 180, no 1, , p. 91–7 (PMID 1718282, DOI 10.1016/S0006-291X(05)81259-8)
  • (en) M. Johnsson, C. F. Richardson, E. J. Bergey, M. J. Levine et G. H. Nancollas, « The effects of human salivary cystatins and statherin on hydroxyapatite crystallization », Arch. Oral Biol., vol. 36, no 9, , p. 631–6 (PMID 1741693, DOI 10.1016/0003-9969(91)90014-L)
  • (en) N. Ramasubbu, M. S. Reddy, E. J. Bergey, G. G. Haraszthy, S. D. Soni et M. J. Levine, « Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva », Biochem. J., vol. 280 ( Pt 2), no Pt 2, , p. 341–52 (PMID 1747107, PMCID 1130552)
  • (en) L. M. Sabatini, Y. Z. He et E. A. Azen, « Structure and sequence determination of the gene encoding human salivary statherin », Gene, vol. 89, no 2, , p. 245–51 (PMID 2373369, DOI 10.1016/0378-1119(90)90012-G)
  • (en) L. M. Sabatini, T. F. Warner, E. Saitoh et E. A. Azen, « Tissue distribution of RNAs for cystatins, histatins, statherin, and proline-rich salivary proteins in humans and macaques », J. Dent. Res., vol. 68, no 7, , p. 1138–45 (PMID 2483725, DOI 10.1177/00220345890680070101)
  • (en) D. P. Dickinson, A. L. Ridall et M. J. Levine, « 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., vol. 149, no 2, , p. 784–90 (PMID 3426601, DOI 10.1016/0006-291X(87)90436-0)
  • (en) F. G. Oppenheim, D. I. Hay, D. J. Smith, G. D. Offner et R. F. Troxler, « 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., vol. 66, no 2, , p. 462–6 (PMID 3476566, DOI 10.1177/00220345870660021301)
  • (en) H. E. Perinpanayagam, B.C. Van Wuyckhuyse, Z. S. Ji et L. A. Tabak, « Characterization of low-molecular-weight peptides in human parotid saliva », J. Dent. Res., vol. 74, no 1, , p. 345–50 (PMID 7876428, DOI 10.1177/00220345950740011001)
  • (en) T. L. Gururaja et M. J. Levine, « Solid-phase synthesis and characterization of human salivary statherin: a tyrosine-rich phosphoprotein inhibitor of calcium phosphate precipitation », Pept. Res., vol. 9, no 6, , p. 283–9 (PMID 9048421)
  • (en) I. Iontcheva, F. G. Oppenheim et R. F. Troxler, « Human salivary mucin MG1 selectively forms heterotypic complexes with amylase, proline-rich proteins, statherin, and histatins », J. Dent. Res., vol. 76, no 3, , p. 734–43 (PMID 9109822, DOI 10.1177/00220345970760030501)
  • (en) I. Iontcheva, F. G. Oppenheim, G. D. Offner et R. F. Troxler, « Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system », J. Dent. Res., vol. 79, no 2, , p. 732–9 (PMID 10728974, DOI 10.1177/00220345000790020601)
  • (en) M. Gilbert, W. J. Shaw, J. R. Long, K. Nelson, G. P. Drobny, C. M. Giachelli et P. S. Stayton, « Chimeric peptides of statherin and osteopontin that bind hydroxyapatite and mediate cell adhesion », J. Biol. Chem., vol. 275, no 21, , p. 16213–8 (PMID 10748043, DOI 10.1074/jbc.M001773200)
  • (en) Y. Yao, M. S. Lamkin et F. G. Oppenheim, « Pellicle precursor protein crosslinking characterization of an adduct between acidic proline-rich protein (PRP-1) and statherin generated by transglutaminase », J. Dent. Res., vol. 79, no 4, , p. 930–8 (PMID 10831095, DOI 10.1177/00220345000790040801)
  • (en) N. Tamaki, T. Tada, M. Morita et T. Watanabe, « Comparison of inhibitory activity on calcium phosphate precipitation by acidic proline-rich proteins, statherin, and histatin-1 », Calcif. Tissue Int., vol. 71, no 1, , p. 59–62 (PMID 12060866, DOI 10.1007/s00223-001-1084-0)
  • (en) Y. Yao, E. A. Berg, C. E. Costello, R. F. Troxler et F. G. Oppenheim, « Identification of protein components in human acquired enamel pellicle and whole saliva using novel proteomics approaches », J. Biol. Chem., vol. 278, no 7, , p. 5300–8 (PMID 12444093, DOI 10.1074/jbc.M206333200)
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