α-Galactosidase activity in human saliva

Oh, Jeong-Kyu; Lee, Jeong-Yun; Park, Heekyung; Kho, Hong‐Seop

doi:10.1016/j.archoralbio.2008.03.005

Cited by 3 publications

(2 citation statements)

References 41 publications

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“…Abbreviations are as in Table 1. more specifically at individual proteins, levels of α-galactosidase [31] or α-amylase activity [24] were reported to be independent of gender. Conflicting results are found for secretory IgA, from over-expression in women [32], no effect of gender [33] or over-expression in men [34].…”

Section: Discussionmentioning

confidence: 99%

Inter-individual variability of protein patterns in saliva of healthy adults

Quintana

Palicki

Lucchi³

et al. 2009

Journal of Proteomics

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In order to document inter-individual variability in salivary protein patterns, unstimulated whole saliva was obtained from 12 subjects at 10 am and 3 pm of the same day. Saliva proteins were separated using two-dimensional gel electrophoresis, and semi-quantified using image analysis. One-way ANOVA was used to test the effects "time of sampling" and "subject". Data were further explored by multivariate analyses (PCA, hierarchical clustering). Spots of interest were identified by mass spectrometry (MALDI-TOF MS/MS and nanoLC ESI-IT MS/MS). A dataset of 509 spots matched in all gels was obtained. There was no diurnal statistical effect on salivary patterns while inter-individual variability was high with 47 spots differentially expressed between subjects (p<1%). Clustering of these spots revealed that subjects could be discriminated first based on several proteins participating to the non-specific immune response (cystatins, lipocalin 1, parotid-secretory protein and prolactin-induced protein). Independently, subjects were also differentiated by their level of proteins originating from serum and involved in the immune system (complement C3, transferrin, IgG2), as well as the relative abundance of enzymes involved in carbohydrates metabolism (amylase and glycolytic enzymes). Inter-individual variability should be accounted for when searching for salivary biomarkers or when studying in-mouth biochemical mechanisms.

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Section: Discussionmentioning

confidence: 99%

Inter-individual variability of protein patterns in saliva of healthy adults

Quintana

Palicki

Lucchi³

et al. 2009

Journal of Proteomics

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“…This salivary α-galactosidase converts blood group B antigen to H antigen by removing Gal [34]. Saliva from healthy adults has activity levels of 100–300 µunits/mL [35]. Whether this α-galactosidase activity is human produced or produced by oral bacteria (both Streptococcus mutans and Actinomyces spp.…”

Section: Glycosidases Produced By Infant and Adult Gitmentioning

confidence: 99%

Protein-Linked Glycan Degradation in Infants Fed Human Milk

Dallas

Sela

Underwood

et al. 2012

Journal of Glycomics & Lipidomics

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Many human milk proteins are glycosylated. Glycosylation is important in protecting bioactive proteins and peptide fragments from digestion. Protein-linked glycans have a variety of functions; however, there is a paucity of information on protein-linked glycan degradation in either the infant or the adult digestive system. Human digestive enzymes can break down dietary disaccharides and starches, but most of the digestive enzymes required for complex protein-linked glycan degradation are absent from both human digestive secretions and the external brush border membrane of the intestinal lining. Indeed, complex carbohydrates remain intact throughout their transit through the stomach and small intestine, and are undegraded by in vitro incubation with either adult pancreatic secretions or intact intestinal brush border membranes. Human gastrointestinal bacteria, however, produce a wide variety of glycosidases with regio- and anomeric specificities matching those of protein-linked glycan structures. These bacteria degrade a wide array of complex carbohydrates including various protein-linked glycans. That bacteria possess glycan degradation capabilities, whereas the human digestive system, perse, does not, suggests that most dietary protein-linked glycan breakdown will be of bacterial origin. In addition to providing a food source for specific bacteria in the colon, protein-linked glycans from human milk may act as decoys for pathogenic bacteria to prevent invasion and infection of the host. The composition of the intestinal microbiome may be particularly important in the most vulnerable humans-the elderly, the immunocompromised, and infants (particularly premature infants).

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