Skip to main content
SpringerLink
Log in

15 Nieuwe ontwikkelingen in oraal biochemisch onderzoek

  • Chapter
Speeksel, speekselklieren en mondgezondheid

  • 1024 Accesses

Samenvatting

Moleculairbiologische technieken zoals de recombinant-DNA-techniek en genklonering worden steeds vaker routinematig gebruikt, voor onder andere productie van humane eiwitten zoals insuline en groeihormoon, en voor de ontwikkeling van veilige vaccins. Synthese van glycoproteïnen met deze methode is echter nog altijd een groot probleem. Voor de synthese van kleine (niet-geglycosyleerde) eiwitten en peptiden is organisch-chemische synthese een goed alternatief. In principe kan met deze techniek elk gewenst eiwitdomein in relatief grote hoeveelheden worden gesynthetiseerd. Organisch-chemisch synthese van peptiden is een belangrijk hulpmiddel bij onderzoek naar de structuur-functierelatie van eiwitten. Daarnaast biedt deze techniek de mogelijkheid tot grootschalige synthese van peptiden voor biomedische toepassingen.

De nieuwe ontwikkelingen op het gebied van de celbiologie (onder andere weefselregeneratie, stamcelonderzoek, gentransfer en micro-arraytechniek) zijn veelbelovend. Hierdoor kunnen toepassingen op onder andere het terrein van weefselherstel en de vroege diagnostiek van maligniteiten op korte termijn worden verwacht.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 99.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Literatuur

  • Amado F.M.L., R.M.P. Vitorino, P.M.D.N. Domingues, M.J.C. Lobo en J.A.R. Duarte. Analysis of the human saliva proteome. Expert Rev. Proteomics 2, (2005)521–539.

    Article  CAS  PubMed  Google Scholar 

  • Auerswald E.A., G. Genenger, I. Assfalg-Machleidt, J. Kos en W. Bode. Synthesis of a (desSer 1 - Ile29 - Leu 89) chicken cystatin gene, expression in E. coli as fusion protein and its isolation. FEBS Letters, 243, (1989)186–192.

    Article  CAS  PubMed  Google Scholar 

  • Barrett A.J. Cystatin, the egg white inhibitor of cysteine proteinases. Methods Enzymology 80, (1981)771–778.

    Google Scholar 

  • Baum B.J. en B.C. O’Connell. In vivo gene transfer to salivary glands. Crit. Rev. Oral Biol. Med. 10, (1999)276–283.

    Article  CAS  PubMed  Google Scholar 

  • Baum B.J., R.B. Wellner en C. Zheng. Gene transfer to salivary glands. Int. Rev. Cytology 213, (2002)93–146.

    Article  CAS  Google Scholar 

  • Bikker F.J., A.J.M. Ligtenberg, K. Nazmi, E.C.I. Veerman, W. van ’t Hof, J.G.M. Bolscher, e.a. Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily. J. Biol. Chem. 277, (2002) 32109–32115.

    Article  CAS  PubMed  Google Scholar 

  • Blankenvoorde M.F.J., Y.M.C, Henskens, G.A. van der Weijden, P.A.M. van den Keijbus, E.C.I. Veerman en A. van Nieuw Amerongen. Cystatin A in gingival crevicular fluid of periodontal patients. J. Periodont. Res. 32, (1997)583–588.

    Article  CAS  PubMed  Google Scholar 

  • Blankenvoorde M.F.J., W. van ’t Hof, E. Walgreen-Weterings, T.J.M. van Steenbergen, E.C.I. Veerman, H.S. Brand, e.a. Cystatins and cystatin-derived peptides have antibacterial activity against the pathogen Porphyromonas gingivalis. Biol. Chem. 379, (1998)1371–1375.

    CAS  PubMed  Google Scholar 

  • Bobek L.A., A. Aguirre en M.J. Levine. Human salivary cystatin S. Cloning, sequence analysis, hybridization in situ and immunocytochemistry. Biochem. J. 278, (1991)627–635.

    CAS  PubMed Central  PubMed  Google Scholar 

  • Bobek L.A., X. Wang en M.J. Levine. Efficient production of biologically active human salivary cystatins in Escherichia coli. Gene 123, (1993a)203–210.

    Article  CAS  PubMed  Google Scholar 

  • Bobek L.A., H. Tsai, A.R. Biesbroek en M.J. Levine. Molecular cloning, sequence, and specificity of expression of the gene encoding the low molecular weight human salivary mucin (MUC7). J. Biol. Chem. 268, (1993b)20563–20569.

    CAS  PubMed  Google Scholar 

  • Bolstad A.I. en R. Jonsson. Gene therapeutics in SjÖgren’s syndrome. Expert Opin. Biol. Ther. 5, (2005)763–772.

    Article  CAS  PubMed  Google Scholar 

  • Cohen R.E., A. Aguirre, M.E. Neiders, M.J. Levine, P.C. Jones, M.S. Reddy, e.a. Immunochemistry of high molecular-weight human salivary mucin. Archs Oral Biol. 35, (1990)127–136.

    Article  CAS  Google Scholar 

  • Cohen R.E., A. Aguirre, M.E. Neiders, M.J. Levine, P.C. Jones, M.S. Reddy, e.a. Immunochemistry and immunogenicity of low molecular weight human salivary mucin. Archs Oral Biol. 36, (1991)347–356.

    Article  CAS  Google Scholar 

  • Colella R., Y. Sakaguchi, H. Nagase en J.W.C. Bird. Chicken egg white cystatin - Molecular cloning, nucleotide sequence, and tissue distribution. J. Biol. Chem. 264, (1989)17164–17169.

    CAS  PubMed  Google Scholar 

  • Coppes R.P., R. Licht, P.K. Wierenga, H.H. Kampinga en G. de Haan. Recovery of radiation-induced deterioration of salivary gland morphology after transplantation with bone marrow derived stem cells, Int. J. Radiat. Oncol. Biol. Phys. 55, (2003) 491.

    Google Scholar 

  • Fackelman K.A. Bloodsuckers reconsidered. Science News 139, (1991)172–173.

    Article  Google Scholar 

  • Fong D., T. Kartasova, F. Sloane en M.M. Chan. Bacterial expression of human cysteine proteinase inhibitor Stefin A. FEBS Letters, 257, (1989)55–58.

    Article  CAS  PubMed  Google Scholar 

  • Gardell S.J., D.R. Ramjit, I.I. Stabilito, T. Fujita, J.J. Lynch, G.C. Cuca, e.a. Effective thrombolysis without marked plasminemia after bolus intravenous administration of vampire bat salivary plasminogen activator in rabbits. Circulation 84, (1991)244–253.

    Article  CAS  PubMed  Google Scholar 

  • Ghafouri B., C. Tagesson en M. Lindahl. Mapping of proteins in human saliva using two-dimensional gel electrophoresis and peptide mass fingerprinting. Proteomics 3, (2003)1003–1015.

    Article  CAS  PubMed  Google Scholar 

  • Groenink J., E. Walgreen-Weterings, W. van ’t Hof, E.C.I. Veerman en A. van Nieuw Amerongen. Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens. FEMS Microbiol. Lett. 179, (1999)217–222.

    Article  CAS  PubMed  Google Scholar 

  • Grubb A., M. Abrahamson, I. Olafsson, J. Trojnar, R. Kasprzykowska, F. Kasprzykowski, e.a. Synthesis of cysteine proteinase inhibitors structurally based on the proteinase interacting N-terminal region of human cystatin-C. Biol. Chem. Hoppe-Seyler 371, (1990)137–144.

    Article  CAS  PubMed  Google Scholar 

  • Guo T., P.A. Rudnick, W. Wang, C.S. Lee, D.L. Devoe en B.M. Balgley. Characterization of the human salivary proteome by capillary isoelectric focusing/ nanoreversed-phase liquid chromatography coupled with ESI-tandem MS. J. Proteome Res. 5, (2006)1469–1478.

    Article  CAS  PubMed  Google Scholar 

  • Hall A., M. Abrahamson, A. Grubb, J. Trojnar, P. Kania, R. Kasprzykowska, e.a. Cystatin C based peptidyl diazomethanes as cysteine proteinase inhibitors: influence of the peptidyl chain length. J. Enzyme Inhib. 6, (1992)113–123.

    Article  CAS  PubMed  Google Scholar 

  • Helmerhorst E.J. Design and characterization of antimicrobial peptides base don salivary histatins. Dissertatie, 1999. Vrije Universiteit, Amsterdam.

    Google Scholar 

  • Helmerhorst E.J., W. van ’t Hof, E.C.I. Veerman, I. Simoons-Smit en A. van Nieuw Amerongen. Synthetic histatin analogues with broad-spectrum antimicrobial activity. Biochem. J. 326, (1997)39–45.

    CAS  PubMed Central  PubMed  Google Scholar 

  • Helmerhorst E.J., I.M. Reijnders, W. van ’t Hof, I. Simoons-Smit, E.C.I. Veerman en A. van Nieuw Amerongen. Amphotericin B- and fluconazoleresistant Candida spp., Aspergillus fumigatus, and other newly emerging pathogenic fungi are susceptible to basic antifungal peptides. Antimicrob. Agents Chemother. 43, (1999a)702–704.

    CAS  PubMed Central  PubMed  Google Scholar 

  • Helmerhorst E.J., P. Breeuwer, W. van ’t Hof, E. Walgreen-Weterings, L.C. Oomen, E.C.I. Veerman, e.a. The cellular target of histatin 5 on Candida albicans is the energized mitochondrion. J. Biol. Chem. 274, (1999b)7286–7291.

    Article  CAS  PubMed  Google Scholar 

  • Helmerhorst E.J., M.P. Murphy, R.F. Troxler en F.G. Oppenheim. Characterization of the mitochondrial respiratory pathways in Candida albicans. Biochim. Biophys. Acta 1556, (2002)73–80.

    Article  CAS  PubMed  Google Scholar 

  • Henskens Y.M.C., U. van der Velden, E.C.I. Veerman en A. van Nieuw Amerongen. Protein, albumin and cystatin concentrations in saliva of healthy subjects and of patients with gingivitis or periodontitis. J. Periodont. Res. 28, (1993)43–48.

    Article  CAS  PubMed  Google Scholar 

  • Hertog A.L. den, J. van Marle, E.C.I. Veerman, M. Valentijn-Benz, K. Nazmi, H. Kalay, C.H. Grün, e.a. The human cathelicidin peptide LL-37 and truncated variants induce segregation of lipids and proteins in the plasma membrane of Candida albicans. Biol. Chem. 387, (2006)1495–1502.

    Google Scholar 

  • Hirtz C., F. Chevalier, D. Centeno, V. Rofidal, J.-C. Egea, M. Rossignol, e.a. MS characterization of multiple forms of alpha-amylase in human saliva. Proteomics 5, (2005)4597–4607.

    Article  CAS  PubMed  Google Scholar 

  • HofW. van ’t, E.C.I. Veerman, E.J. Helmerhorst en A. van Nieuw Amerongen. Antimicrobial peptides: properties and applicability. Biol. Chem. 382, (2001)597–619.

    Article  Google Scholar 

  • Hof W. van ’t, M.F.J. Blankenvoorde, E.C.I. Veerman en A. van Nieuw Amerongen. The salivary lipocalin Von Ebner’s gland protein is a cysteine proteinase inhibitor. J. Biol. Chem. 272, (1997)1837–1841.

    Article  Google Scholar 

  • Hu S., J.A. Loo en D.T. Wong. Human saliva proteome analysis. Ann. N. Y. Acad. Sci. 1098, (2007)323–329.

    Article  CAS  PubMed  Google Scholar 

  • Jürgens M. en M. Schrader. Peptidomic approaches in proteomic research. Curr. Opin. Mol. Therap. 4, (2002)236–241.

    Google Scholar 

  • Kraan M.I.A. van der, K. Nazmi,W. van ’t Hof, A. van Nieuw Amerongen, E.C.I. Veerman en J.G.M. Bolscher. Distinct bactericidal activities of bovine lactoferrin peptides LF-ampin 268-284 and LF-ampin 265-284: Asp-Leu-Ile sequence makes the difference. Biochem. Cell Biol. 84, (2006)358–362.

    Article  PubMed  Google Scholar 

  • Levine M.J., M.S. Reddy, L.A. Tabak, R.E. Loomis, E.J. Bergey, P.C. Jones, e.a. Structural aspects of salivary glycoproteins. J. Dent. Res. 66, (1987)436–441.

    Article  CAS  PubMed  Google Scholar 

  • Levine M.J., A. Aguirre, M.N. Hatton en L.A. Tabak. Artificial salivas: present and future. J. Dent. Res. 66, (1987)693–698.

    Article  PubMed  Google Scholar 

  • Li Y., X. Zhou, M.A.R. St. John en W.T. Wong. RNA profiling of cell-free saliva using microarray technology. J. Dent. Res. 83, (2004)199–203.

    Google Scholar 

  • Ligtenberg A.J.M., E. Walgreen-Weterings, E.C.I. Veerman, J.J. de Soet, J. de Graaff en A. van Nieuw Amerongen. Influence of saliva on the aggregation and adherence of Streptococcus gordonii HG 222. Infect. Immun. 60, (1992)3878–3884.

    CAS  PubMed Central  PubMed  Google Scholar 

  • Loomis R.E., A. Prakobphol, M.J. Levine, M.S. Reddy en P.C. Jones. Biochemical and biophysical comparison of two mucins from human submandibular- sublingual saliva. Archs Biochem. Biophys. 258, (1987)452–464.

    Article  CAS  Google Scholar 

  • Mackay B.J., J.J. Pollock, V.J. Iacono en B.J. Baum. Isolation of milligram quantities of a group of histidine-rich polypeptides from human parotid saliva. Infect. Immun. 44, (1984)688–694.

    CAS  PubMed Central  PubMed  Google Scholar 

  • Mandel I.D. A contemporary view of salivary research. Crit. Rev. Oral Biol. Med. 4, (1993)599–604.

    CAS  PubMed  Google Scholar 

  • Messana I., R. Inzitari, C. Fanali, T. Cabras en M. Castagnola. Facts and artifacts in proteomics of body fluids. What proteomics of salvia is telling us? J. Seperation Sci. 31, (2008)1948–1963.

    Article  CAS  Google Scholar 

  • Nikawa T., T. Towatari, Y. Ike en N. Katunuma. Studies on the reactive site of the cystatin superfamily using recombinant cystatin A mutants - Evidence that the QVVAG region is not essential for cysteine proteinase inhibitory activities. FEBS Letters 255, (1989)309–314.

    Article  CAS  PubMed  Google Scholar 

  • Nishikata M., T. Kanehira, H. Oh, H. Tani, M. Tazaki en Y. Kuboki. Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis. Biochem. Biophys. Res. Comm. 174, (1991)625–630.

    Article  CAS  PubMed  Google Scholar 

  • O’Connell B.C., C. Zheng, D. Jacobson-Kram en B.J. Baum. Distribution and toxicity resulting from adenoviral vector administration to a single salivary gland in adult rats. J. Oral Pathol. Med. 32, (2003)414–421.

    Article  PubMed  Google Scholar 

  • Oppenheim F.G., T. Xu, F.M. McMillian, S.M. Levitz, R.D. Diamond, G.D. Offner, e.a. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J. Biol. Chem. 263, (1988)7472–7477.

    CAS  PubMed  Google Scholar 

  • Papagianni M. Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function and applications. Biotechn. Adv. 21, (2003)465–499.

    Article  CAS  Google Scholar 

  • Prakobphol A., M.J. Levine, L.A. Tabak en M.S. Reddy. Purification of a low-molecular-weight, mucin-type glycoprotein from human submandibular- sublingual saliva. Carbohydr. Res. 108, (1982)111–122.

    Article  CAS  PubMed  Google Scholar 

  • Reijden W.A. van der, M.J. Buijs, J.J.M. Damen, E.C.I. Veerman, J.M. ten Cate en A. van Nieuw Amerongen. Influence of polymers for use in artificial saliva substitutes on de- and remineralization of enamel in vitro. Caries Res. 31, (1997)216–223.

    Article  PubMed  Google Scholar 

  • Ruissen A.L.A., J. Groenink, E.J. Helmerhorst, E. Walgreen-Weterings, W. van ’t Hof, E.C.I. Veerman en A. van Nieuw Amerongen. Effects of histatin 5 and derived peptides on Candida albicans. Biochem. J. 356, (2001) 361–368.

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Ruissen A.L.A., J. Groenink, C.H. Lommerse, W. van ’t Hof, E.C.I. Veerman en A. van Nieuw Amerongen. Effects of carbohydrate polymers applicable in saliva substitutes on the anti-Candida activity of a histatin-derived peptide. Archs Oral Biol. 47, (2002)749–756.

    Article  CAS  Google Scholar 

  • Santarpia R.P., M.I. Cho en J.J. Pollock. Parameters affecting the inhibition of Candida albicans GDH 2023 and GRI 2773 blastospore viability by purified synthetic salivary histidine-rich polypeptides. Oral Microb. Immunol. 5, (1990)226–232.

    Article  CAS  Google Scholar 

  • Schipper R.G., E. Silletti en M.H. Vingerhoeds. Saliva as research material: Biochemical, physicochemical and practical aspects. Archs Oral Biol. 52, (2007)1114–1135.

    Article  CAS  Google Scholar 

  • Spek J.C. van der, G.D. Offner, R.F. Troxler en F.G. Oppenheim. Molecular cloning of human submandibular histatins. Archs Oral Biol. 35, (1990)137–143.

    Article  Google Scholar 

  • Strietzel F.P., R. Martin-Granizo, S. Fedele, L. Lo Russo, M. Mignogna, P.A. Reichart, e.a. Electrostimulating device in the management of xerostomia. Oral Dis. 13, (2007)206–213.

    Article  CAS  PubMed  Google Scholar 

  • Tabak L.A. en W.H. Bowen. Roles of saliva (pellicle), diet, and nutrition on plaque formation. J. Dent. Res., 68, (1989)1560–1566.

    Google Scholar 

  • Veerman E.C.I., M. Valentijn-Benz en A. van Nieuw Amerongen. Isolation of high molecular weight mucins from human whole saliva by ultracentrifugation. J. Biol. Buccale 17, (1989)307–312.

    CAS  PubMed  Google Scholar 

  • Veerman E.C.I., M. Valentijn-Benz, P.A.M. van den Keijbus, W.M. Rathman, J.K. Sheehan en A. van Nieuw Amerongen. Immunochemical analysis of human salivary mucins using monoclonal antibodies. Archs Oral Biol. 36, (1991)923–932.

    Article  CAS  Google Scholar 

  • Veerman E.C.I., P.A.M. van den Keijbus, M. Valentijn-Benz en A. van Nieuw Amerongen. Isolation of different high molecular weight mucin species from human whole saliva. Biochem. J. 283, (1992)807–811.

    CAS  PubMed Central  PubMed  Google Scholar 

  • Voutetakis, I. Bossis, M.R. Kok, W. Zhang, J. Wang, A.P. Cotrim, e.a. Salivary A. glands as a potential gene transfer target for gene therapeutics of some monogenetic endocrine disorders. J. Endocrinol. 185, (2005)363–372.

    Article  PubMed  Google Scholar 

  • Waxman L., D.E. Smith, K.E. Arcuri en G.P. Vlasuk. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 248, (1990)593–596.

    Article  CAS  PubMed  Google Scholar 

  • Yamano S., L.-Y. Huang, C. Ding, J.A. Chiorini, C.M. Goldsmith, R.B. Wellner, e.a. Recombinant adenoassociated virus serotype 2 vectors mediate stable interleukin 10 secretion from salivary glands into the bloodstream. Human Gen. Ther. 13, (2002)287–298.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Sectie Orale Biochemie, Academisch Centrum Tandheelkunde Amsterdam (ACTA), Vrije Universiteit en Universiteit van Amsterdam, Amsterdam

    Prof. dr. A. van Nieuw Amerongen

Authors
  1. Prof. dr. A. van Nieuw Amerongen
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 2008 Bohn Stafleu van Loghum, onderdeel van Springer Uitgeverij

About this chapter

Cite this chapter

van Nieuw Amerongen, A. (2008). 15 Nieuwe ontwikkelingen in oraal biochemisch onderzoek. In: Speeksel, speekselklieren en mondgezondheid. Bohn Stafleu van Loghum, Houten. https://doi.org/10.1007/978-90-313-6317-9_15

Download citation

  • DOI: https://doi.org/10.1007/978-90-313-6317-9_15

  • Publisher Name: Bohn Stafleu van Loghum, Houten

  • Print ISBN: 978-90-313-5173-2

  • Online ISBN: 978-90-313-6317-9

  • eBook Packages: Dutch language eBook collection

Publish with us

Policies and ethics

Search

Navigation