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Salivary proteomic profile of dogs with and without dental calculus (2020)

  • Authors:
  • USP affiliated authors: MACHADO, MARIA APARECIDA DE ANDRADE MOREIRA - FOB ; JORGE, PAULA KARINE - FOB ; ISHIKIRIAMA, BELLA LUNA COLOMBINI - FOB
  • Unidade: FOB
  • DOI: 10.1186/s12917-020-02514-0
  • Subjects: PROTEÔMICA; SALIVA; CÁLCULO DENTÁRIO; CÃES
  • Agências de fomento:
  • Language: Inglês
  • Imprenta:
  • Source:
  • Acesso à fonteDOI
    Informações sobre o DOI: 10.1186/s12917-020-02514-0 (Fonte: oaDOI API)
    • Este periódico é de acesso aberto
    • Este artigo é de acesso aberto
    • URL de acesso aberto
    • Cor do Acesso Aberto: gold
    • Licença: cc-by

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    • ABNT

      BRINGEL, Mayara; JORGE, Paula Karine; FRANCISCO, Priscila Amanda; et al. Salivary proteomic profile of dogs with and without dental calculus. BMC Veterinary Research, London, BioMed Central Ltd, v. 16, 2020. Disponível em: < https://doi.org/10.1186/s12917-020-02514-0 > DOI: 10.1186/s12917-020-02514-0.
    • APA

      Bringel, M., Jorge, P. K., Francisco, P. A., Lowe, C., Sabino-Silva, R., Colombini-Ishikiriama, B. L., et al. (2020). Salivary proteomic profile of dogs with and without dental calculus. BMC Veterinary Research, 16. doi:10.1186/s12917-020-02514-0
    • NLM

      Bringel M, Jorge PK, Francisco PA, Lowe C, Sabino-Silva R, Colombini-Ishikiriama BL, Machado MA de AM, Siqueira WL. Salivary proteomic profile of dogs with and without dental calculus [Internet]. BMC Veterinary Research. 2020 ; 16Available from: https://doi.org/10.1186/s12917-020-02514-0
    • Vancouver

      Bringel M, Jorge PK, Francisco PA, Lowe C, Sabino-Silva R, Colombini-Ishikiriama BL, Machado MA de AM, Siqueira WL. Salivary proteomic profile of dogs with and without dental calculus [Internet]. BMC Veterinary Research. 2020 ; 16Available from: https://doi.org/10.1186/s12917-020-02514-0

    Referências citadas na obra
    Helmerhorst EJ, Oppenheim FG. Saliva: a dynamic proteome. J Dent Res. 2007;86:680–93.
    Schipper RG, Silletti E, Vingerhoeds MH. Saliva as research material: biochemical, physicochemical and practical aspects. Arch Oral Biol. 2007;52:1114–35.
    Humphrey SP, Williamson RT. A review of saliva: normal composition, flow, and function. J Prosthet Dent. 2001;2:162–9.
    Pasha S, Inui T, Chapple I, Harris S, Holcombe L, Grant MM. The saliva proteome of dogs: variations within and between breeds and between species. Proteomics. 2018;18:1–7.
    Lamy E, da Costa G, Santos R, Capela E, Silva F, Potes J, Pereira A, et al. Sheep and goat saliva proteome analysis: a useful tool for ingestive behavior research? Physiol Behav. 2009;98:393–401.
    Larmas M, Scheinin A. Studies on dog saliva. I. some physico-chemical characteristics. Acta Odontol Scand. 1971;2:205–14.
    Borah BM, Halter TJ, Xie B, Henneman ZJ, Siudzinski TR, Harris S, et al. Kinetics of canine dental calculus crystallization: an in vitro study on the influence of inorganic components of canine saliva. J Colloid Interface Sci. 2014;425:20–6.
    Harvey CE. Periodontal disease in dogs. Etiopathogenesis, prevalence, and significance. Vet Clin North Am Small Anim Pr. 1998;28:1111–28 vi.
    Cleland WP. Opportunities and obstacles in veterinary dental drug delivery. Adv Drug Deliv Rev. 2001;50:261–75.
    Pinto ABF, Saad FMOB, Leite CAL, Aquino AA, Alves MP, Pereira DAR. Sodium tripolyphosphate and sodium hexametaphosphate in preventing dental calculus accumulation in dogs. Arq Bras Med Vet e Zootec. 2008;60:1426–31.
    Lendenmann U, Grogan J, Oppenheim FG. Saliva and dental pellicle-a review. Adv Dent Res. 2000;14:22–8.
    Siqueira WL, Bakkal M, Xiao Y, Sutton JN, Mendes FM. Quantitative proteomic analysis of the effect of fluoride on the acquired enamel pellicle. PLoS One. 2012;7:e42204.
    Coignoul E, Cheville N. Calcified microbial plaque. Dental calculus of dogs. Am J Pathol. 1984;117:499–501.
    Jepsen S, Deschner J, Braun A, Schwarz F, Eberhard J. Calculus removal and the prevention of its formation. Periodontol 2000. 2011;55:167–88.
    Lorenzo MA, Bello LFCO, Rothstein JMJ, Santos AC. Incidence of dental calculus and periodontal disease by dental group, dental arch and age in beagle dogs. J Agro Sci. 2014;13:275–83.
    Camargo A, Novais AA, Júnior DF. Periodontal disease in dogs and cats referred to the veterinary hospital of UFMT, campus Sinop. MT Seasinop. 2015;3:16–24.
    Emily P, Penman S. Handbook of small animal dentistry. 1st ed. Oxford: Pergamon Press plc; 1990.
    Kortegaard HE, Eriksen T, Baelum V. Screening for periodontal disease in research dogs - a methodology study. Acta Vet Scand. 2014;56:77.
    Fernandes NA, Borges APB, Reis EC, Sepulveda RV, Pontes KCD. Prevalence of periodontal disease in dogs and owners’ level of awareness - a prospective clinical trial. Rev Ceres. 2012;59:446–51.
    Aebersold R, Goodlett DR. Mass spectrometry in proteomics. Chem Rev. 2001;2:269–96.
    Oppenheim FG, Salih E, Siqueira WL, Zhang W, Helmerhorst EJ. Salivary proteome and its genetic polymorphisms. Ann N Y Acad Sci. 2007;1098:22–50.
    Xiao Y, Karttunen M, Jalkanen J, Mussi MC, Liao Y, Grohe B, et al. Hydroxyapatite growth inhibition effect of pellicle statherin peptides. J Dent Res. 2015;94:1106–12.
    de Sousa-Pereira P, Amado F, Abrantes J, Ferreira R, Esteves PJ, Vitorino R. An evolutionary perspective of mammal salivary peptide families: cystatins, histatins, statherin and PRPs. Arch Oral Biol. 2013;58:451–8.
    de Sousa-Pereira P, Abrantes J, Pinheiro A, Colaço B, Vitorino R, Esteves PJ. Evolution of C, D and S-type cystatins in mammals: an extensive gene duplication in primates. PLoS One. 2014;9:e109050.
    de Sousa-Pereira P, Cova M, Abrantes J, Ferreira R, Trindade F, Barros A, et al. Cross-species comparison of mammalian saliva using an LC-MALDI based proteomic approach. Proteomics. 2015;15:1598–607.
    Milac TI, Randolph TW, Wang P. Analyzing LC-MS/MS data by spectral count and ion abundance: two case studies. Stat Interface. 2012;5:75–87.
    Khurshid Z, Zohaib S, Najeeb S, Zafar MS, Slowey PD, Almas K. Human saliva collection devices for proteomics: an update. Int J Mol Sci. 2016;17(6):846.
    Sanguansermsri P, Jenkinson HF, Thanasak J, Chairatvit K, Roytrakul S, Kittisenachai S, et al. Comparative proteomic study of dog and human saliva. PLoS One. 2018;13:e0208317.
    Lucena S, Coelho AV, Capela-Silva F, Tvarijonaviciute A, Lamy E. The effect of breed, gender, and acid stimulation in dog saliva proteome. Biomed Res Int. 2018; https://doi.org/10.1155/2018/7456894 .
    Wenger-Riggenbach B, Boretti FS, Quante S, Schellenberg S, Reusch CE, Sieber-Ruckstuhl NS. Salivary cortisol concentrations in healthy dogs and dogs with hypercortisolism. J Vet Intern Med. 2010;24:551–6.
    Gioso MA, Carvalho VG. Oral anatomy of the dog and cat in veterinary dentistry practice. Vet Clin North Am Small Anim Pract. 2005;35:763–80.
    Harvey CE, Nieves MA. Perspectives on veterinary dental care: issues and answers. Small Anim Scope. 1991;11:12–5.
    VenturiniI, MAFA. Retrospective study of 3055 pets referred to ODONTOVET® (Veterinary Dental Center) during 44 months. USP Teses Database. 2006; doi: https://doi.org/10.11606/D.10.2007.tde-14052007-081635 .
    Parker HG, Kim LV, Sutter NB, Carlson S, Lorentzen TD, Malek TB, et al. Genetic structure of the purebred domestic dog. Science. 2004;21(304):1160–4.
    Torres SMF, Furrow E, Souza CP, Granick JL, de Jong EP, Griffin TJ, et al. Salivary proteomics of healthy dogs: An in depth catalog. PLoS One. 2018;13:e0191307.
    Arendt M, Fall T, Lindblad-Toh K, Axelsson E. Amylase activity is associated with AMY2B copy numbers in dog: implications for dog domestication, diet and diabetes. Anim Genet. 2014;45:716–22.
    Boehlke C, Zierau O, Hannig C. Salivary amylase - the enzyme of unspecialized euryphagous animals. Arch Oral Biol. 2015;60:1162–76.
    Oppenheim FG. Wiley-Blackwell (Org.), Salivary Diagnostics. Iowa: EUA; 2008. p. 81.
    Carpenter GH. The secretion, components, and properties of saliva. Annu Rev Food Sci Technol. 2013;4:267–76.
    Ide M, Saruta J, To M, Yamamoto Y, Sugimoto M, Fuchida S, et al. Relationship between salivary immunoglobulin a, lactoferrin and lysozyme flow rates and lifestyle factors in Japanese children: a cross-sectional study. Acta Odontol Scand. 2016;74:576–83.
    Yu LP, Sun BG, Li J, Sun L. Characterization of a c-type lysozyme of Scophthalmus maximus: expression, activity, and antibacterial effect. Fish Shellfish Immunol. 2013;34:46–54.
    Prager EM, Jollès P. Animal lysozymes c and g: an overview. EXS. 1996;75:9–31.
    Magnadottir B. Fish Shellfish Immunol. 2006;20:137–51.
    Callewaert L, Michiels CW. Lysozymes in the animal kingdom. J Biosci. 2010;35(1):127–60.
    Elias-Boneta AR, Ramirez K, Rivas-Tumanyan S, Murillo M, Toro MJ. Prevalence of gingivitis and calculus in 12-year-old Puerto Ricans: a cross-sectional study. BMC Oral Health. 2018;18(1):13.
    Goetzl EJ, An S. Diversity of cellular receptors and functions for the lysophospholipid growth factors lysophosphatidic acid and sphingosine 1-phosphate. FASEB J. 1998;12(15):1589–98.
    Zhang G, Contos JJ, Weiner JA, Fukushima N, Chun J. Comparative analysis of three murine G-protein coupled receptors activated by sphingosine-1-phosphate. Gene. 1999;227(1):89–99.
    Lemos JP, Smaniotto S, Messias CV, Moreira OC, Cotta-de-Almeida V, Dardenne M, et al. Sphingosine-1-phosphate receptor 1 is involved in non-obese diabetic mouse Thymocyte migration disorders. Int J Mol Sci. 2018;19:1446.
    Murata N, Sato K, Kon J, Tomura H, Yanagita M, Kuwabara A, et al. Interaction of sphingosine 1-phosphate with plasma components, including lipoproteins, regulates the lipid receptor-mediated actions. Biochem J. 2000;352:809–15.
    Okajima F. Plasma lipoproteins behave as carriers of extracellular sphingosine 1-phosphate: is this an atherogenic mediator or an anti-atherogenic mediator? Biochim Biophys Acta. 2002;1582:132–7.
    Naiff PF, Ferraz R, Cunha CF, Orlandi PP, Boechat AL, Bertho AL, Dos-Santos MC. Immunophenotyping in saliva as an alternative approach for evaluation of immunopathogenesis in chronic periodontitis. J Periodontol. 2014;85(5):e111–20.
    Lee JH, Daud AN, Cribbs LL, Lacerda AE, Pereverzev A, Klöckner U, et al. Cloning and expression of a novel member of the low voltage-activated T-type calcium channel family. J Neurosci. 1999;19:1912–21.
    Murbartian J, Arias JM, Lee JH, Gomora JC, Perez-Reyes E. Alternative splicing ofthe rat Cav3.3 T-type calcium channel gene produces variants with distinctfunctional properties. FEBS Lett. 2002;528:272–8.
    Zhang L, Henson BS, Camargo PM, Wong DT. The clinical value of salivary biomarkers for periodontal disease. Periodontol 2000. 2009;51:25–37.
    Mize TW, Sundararaj KP, Leite RS, Huang Y. Increased and correlated expression of connective tissue growth factor and transforming growth factor beta 1 in surgically removed periodontal tissues with chronic periodontitis. J Periodontal Res. 2015;50(3):315–9.
    Jun JI, Lau LF. Taking aim at the extracellular matrix: CCN proteins as emerging therapeutic targets. Nat Rev Drug Discov. 2011;10(12):945–63.
    Yan C, Boyd DD. Regulation of matrix metalloproteinase gene expression. J Cell Physiol. 2007;211(1):19–26.
    Jagels MA, Hugli TE. Mixed effects of TGF-beta on human airway epithelial-cell chemokine responses. Immunopharmacology. 2000;48(1):17–26.
    Vezzoli G, Soldati L, Gambaro G. Roles of calcium-sensing receptor (CaSR) in renal mineral ion transport. Curr Pharm Biotechnol. 2009;10:302–10.
    Bandyopadhyay BC, Swaim WD, Sarkar A, Liu X, Ambudkar IS. Extracellular Ca(2+) sensing in salivary ductal cells. J Biol Chem. 2012;287:30305–16.
    Lee J, Ko M, Joo CK. Rho plays a key role in TGF-beta1-induced cytoskeletal rearrangement in human retinal pigment epithelium. J Cell Physiol. 2008;216(2):520–6.
    Hall A. Rho GTPases and the actin cytoskeleton. Science. 1998;279(5350):509–14.
    Bhowmick NA, Ghiassi M, Bakin A, et al. Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol Biol Cell. 2001;12(1):27–36.
    Wang L, Wang T, Song M, Pan J. Rho plays a key role in TGF-β1-induced proliferation and cytoskeleton rearrangement of human periodontal ligament cells. Arch Oral Biol. 2014;59(2):149–57. https://doi.org/10.1016/j.archoralbio.2013.11.004 .
    Siqueira WL, de Oliveira E, Mustacchi Z, Nicolau J. Electrolyte concentrations in saliva of children aged 6-10 years with Down syndrome. Oral Surg Oral Med Oral Pathol Oral Radiol Endod. 2004;98:76–9.
    Siqueira WL, Siqueira MF, Mustacchi Z, de Oliveira E, Nicolau J. Salivary parameters in infants aged 12 to 60 months with Down syndrome. Spec Care Dentist. 2007;27:202–5.
    Toda M, Morimoto K. Comparison of saliva sampling methods for measurement of salivary adiponectin levels. Scand J Clin Lab Invest. 2008;68:823–5.
    Strazdins L, Meyerkort S, Brent V, D'Souza RM, Broom DH, Kyd JM. Impact of saliva collection methods on sIgA and cortisol assays and acceptability to participants. J Immunol Methods. 2005;307:167–71.
    Siqueira WL, Oppenheim FG. Small molecular weight proteins/peptides present in the in vivo formed human acquired enamel pellicle. Arch Oral Biol. 2009;5:437–44.
    Siqueira WL, Margolis HC, Helmerhorst EJ, Mendes FM, Oppenheim FG. Evidence of intact histatins in the in vivo acquired enamel pellicle. J Dent Res. 2010;6:626–30.
    Siqueira WL, Lee YH, Xiao Y, Held K, Wong W. Identification and characterization of histatin 1 salivary complexes by using mass spectrometry. Proteomics. 2012;12:3426–35.

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