Enzymes of Human Saliva

Chauncey, Howard H.; Lionetti, Fabian J.; Winer, Richard A.; Lisanti, Vincent F.

doi:10.1177/00220345540330030501

Cited by 95 publications

(17 citation statements)

References 26 publications

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“…Two additional key enzymes i.e. arylsulfatase and β-glucuronidase are known to be present in human saliva (17). …”

Section: Resultsmentioning

confidence: 99%

“…Finally, two additional key enzymes essential for recycling of Phase II anthocyanin conjugates i.e. β-glucuronidase and arylsulfatase, are known to be present in human saliva (17). …”

Section: Discussionmentioning

confidence: 99%

“…Due to lack of SULT detection in oral tissues, arylsulfatase-based IHC studies were not conducted. Notably, arylsulfatase has been detected in human saliva (17). …”

Section: Figurementioning

confidence: 99%

See 2 more Smart Citations

Effects of Human Oral Mucosal Tissue, Saliva, and Oral Microflora on Intraoral Metabolism and Bioactivation of Black Raspberry Anthocyanins

Mallery

Budendorf

Larsen

et al. 2011

Cancer Prevention Research

102

111

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Our oral cancer chemoprevention trial data implied that patient-specific differences in local retention and metabolism of freeze-dried black raspberries' (BRB) components affected therapeutic responsiveness. Subsequent studies have confirmed that anthocyanins are key contributors to BRB's chemopreventive effects. Consequently, functional assays, immunoblotting and immunohistochemical analyses to evaluate levels and distribution of BRB anthocyanin-relevant metabolic enzymes in human oral tissues were performed. LC-MS/MS analyses of time course saliva samples collected following BRB rinses were conducted to assess local pharmacokinetics and compare the capacities of three different BRB rinse formulations to provide sustained intraoral levels of anthocyanins. Protein profiles demonstrated the presence of key metabolic enzymes in all 15 oral mucosal tissues evaluated while immunohistochemistry confirmed these enzymes were distributed within surface oral epithelia and terminal salivary ducts. β-glucosidase assays confirmed that whole and microflora-reduced saliva can deglycosylate BRB anthocyanins, enabling generation of the bioactive aglycone, cyanidin. LC-MS/MS analyses demonstrated retention of parent anthocyanins and their functional, stable metabolite, protocatechuic acid, in saliva for up to 4 hours after rinsing. Furthermore, post-rinse saliva samples contained glucuronidated anthocyanin conjugates, consistent with intracellular uptake and Phase II conversion of BRB anthocyanins into forms amenable to local recycling. Our data demonstrate that comparable to the small intestine, the requisite hydrolytic, Phase II and efflux transporting enzymes necessary for local enteric recycling are present and functional in human oral mucosa. Notably, inter-patient differences in anthocyanin bioactivation and capacities for enteric recycling would impact treatment as retention of bioactivated chemopreventives at the target site would sustain therapeutic effectiveness.

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“…Two additional key enzymes i.e. arylsulfatase and β-glucuronidase are known to be present in human saliva (17). …”

Section: Resultsmentioning

confidence: 99%

“…Finally, two additional key enzymes essential for recycling of Phase II anthocyanin conjugates i.e. β-glucuronidase and arylsulfatase, are known to be present in human saliva (17). …”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Effects of Human Oral Mucosal Tissue, Saliva, and Oral Microflora on Intraoral Metabolism and Bioactivation of Black Raspberry Anthocyanins

Mallery

Budendorf

Larsen

et al. 2011

Cancer Prevention Research

102

111

View full text Add to dashboard Cite

show abstract

“…The enzymes of human^saliva have Jb'fi^ salivary glands, serum-like gingival crevistudied for decades with respect to j^igin, cular fluid, polymorphonuclear leukocytes, purification and characterizatio% distri-epithelial cells, and dietary constituents bution among individuals, and relationship (Chauncey 1961). However, the extent to to pathological conditions of the oral cavity which each source contributes to the total (Chauncey et al 1954, Amunsen & Nustad amount of salivary enzymes is not clear. 1964, Brandtzaeg & Mann 1964 The relationship between most salivary 1966a, 1966b, 1966c, Soder 1972, Lindqvist enzymes and periodontal disease is also et al 1974, Lindqvist, Nord & Soder 1977 Enzymes may alter bacterial re- Nakamura 1979, Watanabe et al 1981.…”

mentioning

confidence: 99%

Salivary enzymes

Nakamura¹,

Slots²

1983

J of Periodontal Research

129

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Seventy‐six enzyme activities of mixed whole saliva, parotid saliva, serum, and polymorphonuclear leukocytes were examined in 10 individuals with healthy periodontium, 10 adult periodontitis patients, and 4 localized juvenile periodontitis patients by using the API ZYM (Analytab Products Inc., Plainview, N. Y.) and API ZYM AP (API System, La Balme les Grottes, France) semi‐quantitative micromethod systems. Enzymes assayed included phosphatases, esterase, lipase, glycosidases, and proteases including numerous aminopeptidases. Among the three study groups, mixed whole saliva of adult periodontitis patients revealed the highest and mixed whole saliva of healthy individuals the lowest enzyme activities. Statistically significant differences were found for alkaline phosphatase, esterase, β‐glucuronidase, α‐glucosidase, and some aminopeptidases. Bacterial sediment of whole saliva exhibited higher enzyme activities than whole saliva supernatant. Serum contained numerous aminopeptidases which were virtually undetectable in whole saliva. Some enzyme activities found in mixed whole saliva could not be detected in parotid saliva. Polymorphonuclear leukocytes demonstrated a distinct enzyme profile. The present study shows that varying enzyme profiles exist among the various components which make up whole saliva. It also indicates that numerous salivary enzymes originate from oral microorganisms and that the enzyme activity of whole saliva is higher in individuals with periodontal disease than in periodontally healthy subjects.

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“…Its constituents are responsible for essential functions such as food tasting and initiation of digestion, as well as protecting the oral mucosa from pathogenic microbiota, in order to maintain a healthy oral condition [1]. From the proteinaceous composition of WS, several enzymes were already identified, including amylase, carbonic anhydrase, catalase and proteases [2,3]. Indeed, proteases present in oral fluid effectively modulate the structure and function of some salivary proteins and have been implicated in tissue destruction in oral disease, e.g.…”

Section: Introductionmentioning

confidence: 99%