메뉴 건너뛰기




Volumn 58, Issue 5, 2013, Pages 451-458

An evolutionary perspective of mammal salivary peptide families: Cystatins, histatins, statherin and PRPs

Author keywords

Evolution; Peptidomics; Phylogeny; Saliva

Indexed keywords

CYSTATIN; HISTATIN; PROLINE RICH PROTEIN; PROTEOME; SALIVA PROTEIN; STATH PROTEIN, HUMAN;

EID: 84876062523     PISSN: 00039969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.archoralbio.2012.12.011     Document Type: Review
Times cited : (40)

References (57)
  • 6
    • 35548992313 scopus 로고    scopus 로고
    • Saliva as research material: Biochemical, physicochemical and practical aspects
    • R.G. Schipper, E. Silletti, and M.H. Vingerhoeds Saliva as research material: biochemical, physicochemical and practical aspects Archives of Oral Biology 52 12 2007 1114 1135
    • (2007) Archives of Oral Biology , vol.52 , Issue.12 , pp. 1114-1135
    • Schipper, R.G.1    Silletti, E.2    Vingerhoeds, M.H.3
  • 8
    • 0027467129 scopus 로고
    • Fascinating families of proteins: Electrophoresis of human saliva
    • J.A. Beeley Fascinating families of proteins: electrophoresis of human saliva Biochemical Society Transactions 21 1 1993 133 138
    • (1993) Biochemical Society Transactions , vol.21 , Issue.1 , pp. 133-138
    • Beeley, J.A.1
  • 10
    • 56749177129 scopus 로고    scopus 로고
    • Potential biomarkers of human salivary function: A modified proteomic approach
    • J.D. Rudney, R.K. Staikov, and J.D. Johnson Potential biomarkers of human salivary function: a modified proteomic approach Archives of Oral Biology 54 1 2009 91 100
    • (2009) Archives of Oral Biology , vol.54 , Issue.1 , pp. 91-100
    • Rudney, J.D.1    Staikov, R.K.2    Johnson, J.D.3
  • 11
    • 68849122288 scopus 로고    scopus 로고
    • Kinetics of histatin proteolysis in whole saliva and the effect on bioactive domains with metal-binding, antifungal, and wound-healing properties
    • X. Sun, E. Salih, F.G. Oppenheim, and E.J. Helmerhorst Kinetics of histatin proteolysis in whole saliva and the effect on bioactive domains with metal-binding, antifungal, and wound-healing properties FASEB Journal 23 8 2009 2691 2701
    • (2009) FASEB Journal , vol.23 , Issue.8 , pp. 2691-2701
    • Sun, X.1    Salih, E.2    Oppenheim, F.G.3    Helmerhorst, E.J.4
  • 13
    • 18844400535 scopus 로고    scopus 로고
    • A review of protein structure and gene organisation for proteins associated with mineralised tissue and calcium phosphate stabilisation encoded on human chromosome 4
    • N.L. Huq, K.J. Cross, M. Ung, and E.C. Reynolds A review of protein structure and gene organisation for proteins associated with mineralised tissue and calcium phosphate stabilisation encoded on human chromosome 4 Archives of Oral Biology 50 7 2005 599 609
    • (2005) Archives of Oral Biology , vol.50 , Issue.7 , pp. 599-609
    • Huq, N.L.1    Cross, K.J.2    Ung, M.3    Reynolds, E.C.4
  • 14
    • 0036119654 scopus 로고    scopus 로고
    • Saliva-the defender of the oral cavity
    • A.V. Amerongen, and E.C. Veerman Saliva-the defender of the oral cavity Oral Diseases 8 1 2002 12 22
    • (2002) Oral Diseases , vol.8 , Issue.1 , pp. 12-22
    • Amerongen, A.V.1    Veerman, E.C.2
  • 15
    • 0024827038 scopus 로고
    • Complete primary structure of statherin, a potent inhibitor of calcium phosphate precipitation, from the saliva of the monkey, Macaca arctoides
    • D.H. Schlesinger, D.I. Hay, and M.J. Levine Complete primary structure of statherin, a potent inhibitor of calcium phosphate precipitation, from the saliva of the monkey, Macaca arctoides International Journal of Peptide and Protein Research 34 5 1989 374 380
    • (1989) International Journal of Peptide and Protein Research , vol.34 , Issue.5 , pp. 374-380
    • Schlesinger, D.H.1    Hay, D.I.2    Levine, M.J.3
  • 16
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans
    • F.G. Oppenheim, T. Xu, F.M. McMillian, S.M. Levitz, R.D. Diamond, and G.D. Offner Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans Journal of Biological Chemistry 263 16 1988 7472 7477
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.16 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3    Levitz, S.M.4    Diamond, R.D.5    Offner, G.D.6
  • 17
    • 0023748128 scopus 로고
    • The primary structures of six human salivary acidic proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s and PIF-f)
    • D.I. Hay, A. Bennick, D.H. Schlesinger, K. Minaguchi, G. Madapallimattam, and S.K. Schluckebier The primary structures of six human salivary acidic proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s and PIF-f) Biochemical Journal 255 1 1988 15 21
    • (1988) Biochemical Journal , vol.255 , Issue.1 , pp. 15-21
    • Hay, D.I.1    Bennick, A.2    Schlesinger, D.H.3    Minaguchi, K.4    Madapallimattam, G.5    Schluckebier, S.K.6
  • 18
    • 0020144053 scopus 로고
    • Characterization of cysteine-containing phosphoproteins from human submandibular-sublingual saliva
    • J.P. Shomers, L.A. Tabak, M.J. Levine, I.D. Mandel, and S.A. Ellison Characterization of cysteine-containing phosphoproteins from human submandibular-sublingual saliva Journal of Dental Research 61 6 1982 764 767
    • (1982) Journal of Dental Research , vol.61 , Issue.6 , pp. 764-767
    • Shomers, J.P.1    Tabak, L.A.2    Levine, M.J.3    Mandel, I.D.4    Ellison, S.A.5
  • 19
    • 0020413160 scopus 로고
    • Basic proline-rich proteins from human parotid saliva: Complete covalent structure of protein IB-9 and partial structure of protein IB-6, members of a polymorphic pair
    • D. Kauffman, R. Wong, A. Bennick, and P. Keller Basic proline-rich proteins from human parotid saliva: complete covalent structure of protein IB-9 and partial structure of protein IB-6, members of a polymorphic pair Biochemistry 21 25 1982 6558 6562
    • (1982) Biochemistry , vol.21 , Issue.25 , pp. 6558-6562
    • Kauffman, D.1    Wong, R.2    Bennick, A.3    Keller, P.4
  • 20
    • 0020262985 scopus 로고
    • Fractionation and characterization of basic proline-rich peptides of human parotid saliva and the amino acid sequence of proline-rich peptide P-E
    • S. Isemura, E. Saitoh, and K. Sanada Fractionation and characterization of basic proline-rich peptides of human parotid saliva and the amino acid sequence of proline-rich peptide P-E Journal of Biochemistry 91 6 1982 2067 2075
    • (1982) Journal of Biochemistry , vol.91 , Issue.6 , pp. 2067-2075
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3
  • 21
    • 0019312855 scopus 로고
    • The amino acid sequence of a salivary proline-rich peptide, P-C, and its relation to a salivary proline-rich phosphoprotein, protein C
    • S. Isemura, E. Saitoh, and K. Sanada The amino acid sequence of a salivary proline-rich peptide, P-C, and its relation to a salivary proline-rich phosphoprotein, protein C Journal of Biochemistry 87 4 1980 1071 1077
    • (1980) Journal of Biochemistry , vol.87 , Issue.4 , pp. 1071-1077
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3
  • 22
    • 0017372507 scopus 로고
    • Chemical and physical characterization of a phosphoprotein, Protein C, from human saliva and comparison with a related protein A
    • A. Bennick Chemical and physical characterization of a phosphoprotein, Protein C, from human saliva and comparison with a related protein A Biochemical Journal 163 2 1977 229 239
    • (1977) Biochemical Journal , vol.163 , Issue.2 , pp. 229-239
    • Bennick, A.1
  • 23
    • 0016661437 scopus 로고
    • Chemical and physical characteristics of a phosphoprotein from human parotid saliva
    • A. Bennick Chemical and physical characteristics of a phosphoprotein from human parotid saliva Biochemical Journal 145 3 1975 557 567
    • (1975) Biochemical Journal , vol.145 , Issue.3 , pp. 557-567
    • Bennick, A.1
  • 24
    • 0016268059 scopus 로고
    • The isolation from human parotid saliva of a further group of proline-rich proteins
    • D.I. Hay, and F.G. Oppenheim The isolation from human parotid saliva of a further group of proline-rich proteins Archives of Oral Biology 19 8 1974 627 632
    • (1974) Archives of Oral Biology , vol.19 , Issue.8 , pp. 627-632
    • Hay, D.I.1    Oppenheim, F.G.2
  • 25
    • 0015917546 scopus 로고
    • Genetic polymorphism of proline-rich human salivary proteins
    • E.A. Azen, and F.G. Oppenheim Genetic polymorphism of proline-rich human salivary proteins Science 180 90 1973 1067 1069
    • (1973) Science , vol.180 , Issue.90 , pp. 1067-1069
    • Azen, E.A.1    Oppenheim, F.G.2
  • 26
    • 0015150991 scopus 로고
    • Proline-rich proteins from human parotid saliva. I. Isolation and partial characterization
    • F.G. Oppenheim, D.I. Hay, and C. Franzblau Proline-rich proteins from human parotid saliva. I. Isolation and partial characterization Biochemistry 10 23 1971 4233 4238
    • (1971) Biochemistry , vol.10 , Issue.23 , pp. 4233-4238
    • Oppenheim, F.G.1    Hay, D.I.2    Franzblau, C.3
  • 27
    • 70149097991 scopus 로고    scopus 로고
    • Sheep and goat saliva proteome analysis: A useful tool for ingestive behavior research?
    • E. Lamy, G. da Costa, R. Santos, E.S.F. Capela, J. Potes, and A. Pereira Sheep and goat saliva proteome analysis: a useful tool for ingestive behavior research? Physiology & Behavior 98 4 2009 393 401
    • (2009) Physiology & Behavior , vol.98 , Issue.4 , pp. 393-401
    • Lamy, E.1    Da Costa, G.2    Santos, R.3    Capela, E.S.F.4    Potes, J.5    Pereira, A.6
  • 28
    • 0041015870 scopus 로고
    • Saliva secretion and its relation to feeding in cattle. 4. The relationship between the concentrations of sodium, potassium, chloride and inorganic phosphate in mixed saliva and rumen fluid
    • C.B. Bailey Saliva secretion and its relation to feeding in cattle. 4. The relationship between the concentrations of sodium, potassium, chloride and inorganic phosphate in mixed saliva and rumen fluid British Journal of Nutrition 15 1961 489 498
    • (1961) British Journal of Nutrition , vol.15 , pp. 489-498
    • Bailey, C.B.1
  • 29
    • 0036357785 scopus 로고    scopus 로고
    • Salivary (SD-type) cystatins: Over one billion years in the making-but to what purpose?
    • D.P. Dickinson Salivary (SD-type) cystatins: over one billion years in the making-but to what purpose? Critical Reviews in Oral Biology and Medicine 13 6 2002 485 508
    • (2002) Critical Reviews in Oral Biology and Medicine , vol.13 , Issue.6 , pp. 485-508
    • Dickinson, D.P.1
  • 31
    • 33646067439 scopus 로고    scopus 로고
    • Towards novel anti-cancer strategies based on cystatin function
    • D. Keppler Towards novel anti-cancer strategies based on cystatin function Cancer Letters 235 2 2006 159 176
    • (2006) Cancer Letters , vol.235 , Issue.2 , pp. 159-176
    • Keppler, D.1
  • 32
    • 72049098213 scopus 로고    scopus 로고
    • Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes
    • D. Kordis, and V. Turk Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes BMC Evolutionary Biology 9 2009 266
    • (2009) BMC Evolutionary Biology , vol.9 , pp. 266
    • Kordis, D.1    Turk, V.2
  • 34
    • 0036077458 scopus 로고    scopus 로고
    • Cysteine peptidases of mammals: Their biological roles and potential effects in the oral cavity and other tissues in health and disease
    • D.P. Dickinson Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease Critical Reviews in Oral Biology and Medicine 13 3 2002 238 275
    • (2002) Critical Reviews in Oral Biology and Medicine , vol.13 , Issue.3 , pp. 238-275
    • Dickinson, D.P.1
  • 36
    • 0022350512 scopus 로고
    • Genealogy of mammalian cysteine proteinase inhibitors. Common evolutionary origin of stefins, cystatins and kininogens
    • W. Muller-Esterl, H. Fritz, J. Kellermann, F. Lottspeich, W. Machleidt, and V. Turk Genealogy of mammalian cysteine proteinase inhibitors. Common evolutionary origin of stefins, cystatins and kininogens FEBS Letters 191 2 1985 221 226
    • (1985) FEBS Letters , vol.191 , Issue.2 , pp. 221-226
    • Muller-Esterl, W.1    Fritz, H.2    Kellermann, J.3    Lottspeich, F.4    Machleidt, W.5    Turk, V.6
  • 37
    • 0031013054 scopus 로고    scopus 로고
    • Friends and relations of the cystatin superfamily-new members and their evolution
    • W.M. Brown, and K.M. Dziegielewska Friends and relations of the cystatin superfamily-new members and their evolution Protein Science 6 1 1997 5 12
    • (1997) Protein Science , vol.6 , Issue.1 , pp. 5-12
    • Brown, W.M.1    Dziegielewska, K.M.2
  • 40
    • 77951621301 scopus 로고    scopus 로고
    • The genome sequence of taurine cattle: A window to ruminant biology and evolution
    • C.G. Elsik, R.L. Tellam, K.C. Worley, R.A. Gibbs, D.M. Muzny, and G.M. Weinstock The genome sequence of taurine cattle: a window to ruminant biology and evolution Science 324 5926 2009 522 528
    • (2009) Science , vol.324 , Issue.5926 , pp. 522-528
    • Elsik, C.G.1    Tellam, R.L.2    Worley, K.C.3    Gibbs, R.A.4    Muzny, D.M.5    Weinstock, G.M.6
  • 42
    • 0141678423 scopus 로고    scopus 로고
    • Multispecies comparative analysis of a mammalian-specific genomic domain encoding secretory proteins
    • M. Rijnkels, L. Elnitski, W. Miller, and J.M. Rosen Multispecies comparative analysis of a mammalian-specific genomic domain encoding secretory proteins Genomics 82 4 2003 417 432
    • (2003) Genomics , vol.82 , Issue.4 , pp. 417-432
    • Rijnkels, M.1    Elnitski, L.2    Miller, W.3    Rosen, J.M.4
  • 43
    • 0034585802 scopus 로고    scopus 로고
    • Salivary histatin 5 and its similarities to the other antimicrobial proteins in human saliva
    • M. Edgerton, and S.E. Koshlukova Salivary histatin 5 and its similarities to the other antimicrobial proteins in human saliva Advances in Dental Research 14 2000 16 21
    • (2000) Advances in Dental Research , vol.14 , pp. 16-21
    • Edgerton, M.1    Koshlukova, S.E.2
  • 44
    • 29144521244 scopus 로고    scopus 로고
    • Human antimicrobial peptides: Defensins, cathelicidins and histatins
    • K. De Smet, and R. Contreras Human antimicrobial peptides: defensins, cathelicidins and histatins Biotechnology Letters 27 18 2005 1337 1347
    • (2005) Biotechnology Letters , vol.27 , Issue.18 , pp. 1337-1347
    • De Smet, K.1    Contreras, R.2
  • 45
    • 0015831277 scopus 로고
    • A further study of the factors enhancing glycolysis in human saliva
    • I.B. Holbrook, and P.C. Molan A further study of the factors enhancing glycolysis in human saliva Archives of Oral Biology 18 10 1973 1275 1282
    • (1973) Archives of Oral Biology , vol.18 , Issue.10 , pp. 1275-1282
    • Holbrook, I.B.1    Molan, P.C.2
  • 46
    • 0021280786 scopus 로고
    • Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans
    • B.J. MacKay, L. Denepitiya, V.J. Iacono, S.B. Krost, and J.J. Pollock Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans Infection and Immunity 44 3 1984 695 701
    • (1984) Infection and Immunity , vol.44 , Issue.3 , pp. 695-701
    • Mackay, B.J.1    Denepitiya, L.2    Iacono, V.J.3    Krost, S.B.4    Pollock, J.J.5
  • 47
    • 0021263092 scopus 로고
    • Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida albicans
    • J.J. Pollock, L. Denepitiya, B.J. MacKay, and V.J. Iacono Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida albicans Infection and Immunity 44 3 1984 702 707
    • (1984) Infection and Immunity , vol.44 , Issue.3 , pp. 702-707
    • Pollock, J.J.1    Denepitiya, L.2    Mackay, B.J.3    Iacono, V.J.4
  • 48
    • 0026688607 scopus 로고
    • Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization
    • P.A. Raj, M. Johnsson, M.J. Levine, and G.H. Nancollas Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization Journal of Biological Chemistry 267 9 1992 5968 5976
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.9 , pp. 5968-5976
    • Raj, P.A.1    Johnsson, M.2    Levine, M.J.3    Nancollas, G.H.4
  • 49
    • 77957359728 scopus 로고    scopus 로고
    • Mass spectrometric identification of key proteolytic cleavage sites in statherin affecting mineral homeostasis and bacterial binding domains
    • E.J. Helmerhorst, G. Traboulsi, E. Salih, and F.G. Oppenheim Mass spectrometric identification of key proteolytic cleavage sites in statherin affecting mineral homeostasis and bacterial binding domains Journal of Proteome Research 9 10 2010 5413 5421
    • (2010) Journal of Proteome Research , vol.9 , Issue.10 , pp. 5413-5421
    • Helmerhorst, E.J.1    Traboulsi, G.2    Salih, E.3    Oppenheim, F.G.4
  • 51
    • 0027215164 scopus 로고
    • Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family
    • L.M. Sabatini, T. Ota, and E.A. Azen Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family Molecular Biology and Evolution 10 3 1993 497 511
    • (1993) Molecular Biology and Evolution , vol.10 , Issue.3 , pp. 497-511
    • Sabatini, L.M.1    Ota, T.2    Azen, E.A.3
  • 52
    • 0023263979 scopus 로고
    • The molecular clock runs more slowly in man than in apes and monkeys
    • W.H. Li, and M. Tanimura The molecular clock runs more slowly in man than in apes and monkeys Nature 326 6108 1987 93 96
    • (1987) Nature , vol.326 , Issue.6108 , pp. 93-96
    • Li, W.H.1    Tanimura, M.2
  • 53
    • 48949117187 scopus 로고    scopus 로고
    • Facts and artifacts in proteomics of body fluids. What proteomics of saliva is telling us?
    • I.R. Messana I, C. Fanali, T. Cabras, and M. Castagnola Facts and artifacts in proteomics of body fluids. What proteomics of saliva is telling us? Journal of Separation Science 31 11 2008 1948 1963
    • (2008) Journal of Separation Science , vol.31 , Issue.11 , pp. 1948-1963
    • Messana, I.I.R.1    Fanali, C.2    Cabras, T.3    Castagnola, M.4
  • 54
    • 0027357053 scopus 로고
    • The structure and evolution of the human salivary proline-rich protein gene family
    • H.S. Kim, K.M. Lyons, E. Saitoh, E.A. Azen, O. Smithies, and N. Maeda The structure and evolution of the human salivary proline-rich protein gene family Mammalian Genome 4 1 1993 3 14
    • (1993) Mammalian Genome , vol.4 , Issue.1 , pp. 3-14
    • Kim, H.S.1    Lyons, K.M.2    Saitoh, E.3    Azen, E.A.4    Smithies, O.5    Maeda, N.6
  • 56
    • 0024115251 scopus 로고
    • Proline-rich proteins and glycoproteins: Expression of salivary gland multigene families
    • D.M. Carlson Proline-rich proteins and glycoproteins: expression of salivary gland multigene families Biochimie 70 11 1988 1689 1695
    • (1988) Biochimie , vol.70 , Issue.11 , pp. 1689-1695
    • Carlson, D.M.1
  • 57
    • 0025366593 scopus 로고
    • A physical map of the human salivary proline-rich protein gene cluster covers over 700 kbp of DNA
    • H.S. Kim, O. Smithies, and N. Maeda A physical map of the human salivary proline-rich protein gene cluster covers over 700 kbp of DNA Genomics 6 2 1990 260 267
    • (1990) Genomics , vol.6 , Issue.2 , pp. 260-267
    • Kim, H.S.1    Smithies, O.2    Maeda, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.