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2012 | 59 | 4 |

Tytuł artykułu

Salivary proteins in health and disease

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
 Besides their structural catalytic and diverse regulatory functions, proteins are also precursors of many important biological compounds essential for normal functioning of humans. Many of these compounds may be used as markers for identification of specific pathological states. A comprehensive knowledge about the metabolism of salivary proteins and the mechanisms of action of their metabolites allowed the development of effective treatment for many disorders. However, it should not be forgotten that in some pathological conditions, these compounds not only could be involved in the pathogenesis but also could be used as tool in the prediction of many diseases. This paper is a review of the published literature on selected salivary proteins in the context of the physiological processes of the human body and chosen chronic disorders, such as diabetes, diabetic nephropathy, mucositis, oral mycoses and caries.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

59

Numer

4

Opis fizyczny

p.451-457,fig.,ref.

Twórcy

  • Department of Pediatric Dentistry, Institute of Dentistry, Jagiellonian University, Medical College, Cracow, Poland
autor
  • Department of Pediatric Dentistry, Institute of Dentistry, Jagiellonian University, Medical College, Cracow, Poland
autor
  • Department of Medical Diagnostics, Jagiellonian University, Medical College, Faculty of Pharmacy, Cracow, Poland
autor
  • Department of Medical Diagnostics, Jagiellonian University, Medical College, Faculty of Pharmacy, Cracow, Poland

Bibliografia

  • Ackermann A, Bélanger M, Brogden K, Burnell K, Cavanaugh J, Kohlgraf K, Lu X, Progulske-Fox A, Xie H (2010) Defensins attenuate cytokine responses yet enhance antibody responses to Porphyromonas gingivalis adhesins in mice. Future Microbiol 5: 115. 
  • Akamatsu T, Azlina A, Hasegawa T, Hiroshima Y, Hosoi K, Javkhlan P, Kido J, Nagata T, Yao C (2009) Induction of calprotectin mRNAs by lipopolysaccharide in the salivary gland of mice. J Med Invest 56: 287-289. 
  • Alagl A, Helmerhost E, Oppenheim F, Siqueira W (2006) Oral fluid proteolytic effects on histatin-5 structure and function. Arch Oral Biol 51: 1061-1070. 
  • Alam S, Henriksen P, Newby D (2012) Role of the endogenous elastase inhibitor, elafin, in cardiovascular injury. From epithelium to endothelium. Biochem Pharmacol 83: 695-704. 
  • Allgrove J, Davison G, Gleeson M (2009) Salivary antimicrobial peptides (LL-37 and alpha-defensins HNP1-3), antimicrobial and IgA responses to prolonged exercise. Eur J Appl Physiol 106: 277-284. 
  • Amado F, Lobo MJ, Domingues P, Duarte JA, Vitorino R (2010) Salivary peptidomics. Expert Rev Proteomics 7: 709-721. 
  • Antonyraj K, Karunakaran T, Raj P (2000) Large-scale synthesis and functional elements for the antimicrobial activity of defensins. Biochem J 347: 633-641. 
  • Baker O, Conti H, Edgerton M, Freeman A, Gaffen S, Holland S, Jang W, Li R (2011) New mechanism of oral immunity to mucosal candidiasis in hyper-IgE syndrome. Mucosal Immunol 4: 448-455. 
  • Bal W, Bonna A, Goch G, Kurowska E (2011) Salivary histatin-5, a physiologically relevant ligand for Ni(II) ions. J Inorg Biochem 105: 1220-1225. 
  • Belanger M, Brogden K, Burnell K, Cavanaugh J, Dawson D, Dietrich D, Eastman C, Hansen C, Guthmiller J, Johnson G, Joly S, Kohlgraf K, Kurago Z, Pingel L, Progulske-Fox A, Srikantha R, Xiao X (2008) Human beta-defensin 3 binds to hemagglutinin B (rHagB), a non-fimbrial adhesin from Porphyromonas gingivalis, and attenuates a pro- inflammatory cytokine response. Immunol Cell Biol 86: 643-649. 
  • Benakanakere M, Galicia J, Garcia C, Kinane D, Potempa J, Stathopoulou P (2009) Porphyromonas gingivalis induce apoptosis in human gingival epithelial cells through a gingipain-dependent mechanism. BMC Microbiology 9: 107. 
  • Bolscher JG, Adão R, Nazmi K, van den Keybus PA, van 't Hof W, Nieuw Amerongen AV, Bastos M, Veerman EC (2009) Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides. Biochimie 91: 123-132. 
  • Cabane B, Pascal C, Poncet-Legrand C, Vernhet A (2008) Aggregation of a proline-rich protein induced by epigallocatechin gallate and condensed tannins: effect of protein glycosylation. J Agric Food Chem 56: 6724-6732. 
  • Cabras T, Pisano E, Mastinu A, Denotti G, Pusceddu PP, Inzitari R, Fanali C, Nemolato S, Castagnola M, Messana I (2010) Alterations of the salivary secretory peptidome profile in children affected by type 1 diabetes. Mol Cell Proteomics 9: 2099-2108. 
  • Chotjumlong P, Khongkhunthian S, Krisanaprakornkit S, Ongchai S, Reutrakul V (2010) Human β-defensin-3 up-regulates cyclooxygenase-2 expression and prostaglandyn E2 synthesis In human gingival fibroblasts. J Periodont Res 45: 464-470. 
  • De Boer H, Geerts M, Mericskay M, Nuijens J, Van Berkel P, Van Veen H (1997) N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA. Biochem J 328: 145-151. 
  • Dietrich A, Duncan S, Eigel W, Hong J, Mallikarjunan K, O'Keefe S (2009) Interaction of copper and human salivary proteins. J Agric Food Chem 57: 6967-6975. 
  • Eick S, Guentsch A, Kantyka T, Laugisch O, Pfister W, Potempa J, Schacht M, Sculean A, Sroka A, Stennicke H (2012) Periodontal pathogens affect the level of protease inhibitors in gingival crevicular fluid. Mol Oral Microbiol 27: 45-56. 
  • Fidel P Jr, Hackett W, Jabra-Rizk M, Peters B, Scheper M, Shaye S, Zhu J (2010) Protection of the oral mucosa by salivary histatin-5 against candida albicans in an ex vivo murine model of oral infection. FEMS Yeast Res 10: 597-604. 
  • Freitas V, Mateus N, Soares S, Sousa A (2012) Effect of condensed tannins addition on the astringency of red wines. Chem Senses 37: 191-198. 
  • Fujimoto S, Katsura Y, Orita K., Shin-ya U, Usui T, Yoshikawa T, Yoshimura M (2011) Changes in salivary antimicrobial peptides, immunoglobulin A and cortisol after prolonged strenuous exercise. Eur J Appl Physiol 111: 2005-2014. 
  • Goldberg H.A, McDonald E, Mendes F.M, Tabbara N, Siqueira W (2011) Histatin 1 resists proteolytic degradation when adsorbed to hydroxyapatite. J Dent Res 90: 268-272. 
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  • Gunduz M, Kaneda Y, Katase N, Matsubara M, Mizukawa N, Nagatsuka H, Sawaki K, Takagi S, Yamaai T, Yamachika E, Yamanishi Y (2009) Localization of antimicrobial peptides human β-defensins in minor salivary glans with Sjögren's syndrome. Eur J Oral Sci 117: 506-510. 
  • Guo Y, Nguyen K, Potempa J (2010) Dichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins. Periodontology 2000 54: 15-44. 
  • Harriott P, Greer B, Lockhart D, Lundy F, Nelson J, Marley J (2008) Antimicrobial activity of truncated α-defensin (human neutrophil peptide (HNP)-1) analogues without disulphide bridges. Mol Immunol 45: 190-193. 
  • Hirose S. Schalkwijk J, Wiedow O (1999) The trappin gene family: proteins defined by an N-terminal transglutaminase substrate domain and a C-terminal four-disulphide core. Biochem J 340: 569-577. 
  • Huang X, Huo L, Gu L, Ling J, Liu H, Peng Z, Zhang K (2011) Antimicrobial and DNA-binding activities of the peptide fragments of human lactoferrin and histatin 5 against Streptococcus mutans. Arch Oral Biol 56: 869-876. 
  • 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: 734-743. 
  • Krishnakumari V, Nagaraj R, Rangaraj N (2009) Antifungal activities of human beta-defensins HBD-1 to HBD-3 and their C-terminal analogs Phd1 to Phd3. Antimicrob Agents Chem 53: 256-260. 
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Bibliografia

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