A2 Vertaisarvioitu katsausartikkeli tieteellisessä lehdessä
Origin, structure, and biological activities of peroxidases in human saliva
Tekijät: Ihalin R, Loimaranta V, Tenovuo J
Kustantaja: ELSEVIER SCIENCE INC
Julkaisuvuosi: 2006
Journal: Archives of Biochemistry and Biophysics
Tietokannassa oleva lehden nimi: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Lehden akronyymi: ARCH BIOCHEM BIOPHYS
Vuosikerta: 445
Numero: 2
Aloitussivu: 261
Lopetussivu: 268
Sivujen määrä: 8
ISSN: 0003-9861
DOI: https://doi.org/10.1016/j.abb.2005.07.004
Verkko-osoite: https://www.sciencedirect.com/science/article/pii/S0003986105002870?via=ihub
Tiivistelmä
Human whole saliva contains peroxidases, salivary peroxidase (hSPO) and myeloperoxidase (hMPO), which are part of the innate host defence in oral cavity. Both hSPO as well as milk lactoperoxidase (hLPO) are coded by the same gene, but to What extent the different producing glands, salivary and mammary glands, affect the final conformation of the enzymes is not known. In human saliva the major function of hSPO and hMPO is to catalyze the oxidation of thiocyanate (SCN-) in the presence of hydrogen peroxide (H2O2) resulting in end products of wide antimicrobial potential. In addition cytotoxic H2O2 is degraded. Similar peroxidation reactions inactivate some mutagenic and carcinogenic compounds, Which Suggests another protective mechanism of peroxidases in human saliva. Although being target of an active antimicrobial research, the structure-function relationships of hSPO are poorly known. However, recently published method for recombinant hSPO production offers new tools for those investigations. (C) 2005 Elsevier Inc. All rights reserved.
Human whole saliva contains peroxidases, salivary peroxidase (hSPO) and myeloperoxidase (hMPO), which are part of the innate host defence in oral cavity. Both hSPO as well as milk lactoperoxidase (hLPO) are coded by the same gene, but to What extent the different producing glands, salivary and mammary glands, affect the final conformation of the enzymes is not known. In human saliva the major function of hSPO and hMPO is to catalyze the oxidation of thiocyanate (SCN-) in the presence of hydrogen peroxide (H2O2) resulting in end products of wide antimicrobial potential. In addition cytotoxic H2O2 is degraded. Similar peroxidation reactions inactivate some mutagenic and carcinogenic compounds, Which Suggests another protective mechanism of peroxidases in human saliva. Although being target of an active antimicrobial research, the structure-function relationships of hSPO are poorly known. However, recently published method for recombinant hSPO production offers new tools for those investigations. (C) 2005 Elsevier Inc. All rights reserved.
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