Invited Review: Genetics of Human Salivary Proteins

Minaguchi, Kiyoshi; Bennick, Anders

doi:10.1177/00220345890680010201

Cited by 62 publications

(31 citation statements)

References 168 publications

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“…The pattern of proteins translated in vitro with mRNA from rabbit sublingual gland is very similar, but in the presence of submandibular RNA one or fwo proteins with Mr 34,000 and 36,000 were synthesized. This variation between animals is most likely due to polymorphism, which is well documented in other species such as humans (Minaguchi and Bennick, 1989). Differences were also noted in the ultrastructural location of the proteins.…”

Section: Discussionmentioning

confidence: 70%

“…Saliva and salivary glands from a number of species including humans, monkeys, rabbits, hamsters, rats, and mice contain an unusual family of proline-rich proteins (PRPs) (Minaguchi and Bennick, 1989;Spielman and Bennick, 1989;Mehansho et al, 1987;Mehansho et al, 1985;Oppenheim et al, 1985;Zemer et al, 1984). On the basis of their charge, they can be divided into acidic and basic proteins and some of them are phosphorylated or glycosylated (Bennick, 1987).…”

Section: Introductionmentioning

confidence: 99%

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Differential expression of proline-rich proteins in rabbit salivary glands.

Ferreira

Robinson

Hand³

et al. 1992

J Histochem Cytochem.

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Salivary glands synthesize and secrete an unusual family of proline-rich proteins (PRPs) that can be broadly divided into acidic and basic PRPs. We studied the tissue-specific expression of these proteins in rabbits, using antibodies to rabbit acidic and basic PRPs as well as antibodies and cDNA probes to human PRPs. By immunoblotting, in vitro translation, and Northern blotting, basic PRPs could be readily detected in the parotid gland but were absent in other salivary glands. In contrast, synthesis in vitro of acidic PRPs was detected in parotid, sublingual, and submandibular glands. Ultrastructural localization with immunogold showed heavy labeling with antibodies to acidic PRPs of secretory granules of parotid acinar cells and sublingual serous demilune cells. Less intense labeling occurred in the seromucous acinar cells of the submandibular gland. With antibodies to basic PRPs, the labeling of the parotid gland was similar to that observed with antibodies to acidic PRPs, but there was only weak labeling of granules of a few sublingual demilune cells, and no labeling of the submandibular gland. These results demonstrate a variable pattern of distribution of acidic and basic PRPs in rabbit salivary glands. These animals are therefore well suited for study of differential tissue expression of PRPs.

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Section: Discussionmentioning

confidence: 70%

Section: Introductionmentioning

confidence: 99%

Differential expression of proline-rich proteins in rabbit salivary glands.

Ferreira

Robinson

Hand³

et al. 1992

J Histochem Cytochem.

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“…Frequent intragenic homologous and unequal crossovers occur within the tandemly repetitious sequences of the third exons of PRP genes and result in frequent length polymorphisms (Azen et al, 1984;Lyons et al, 1988b). Several PRPs (to be discussed later) have been assigned to the different PRP genes (Lyons et al, 1988a;Minaguchi. and Bennick, 1989).…”

Section: Background Information a Prp Gene Familymentioning

confidence: 99%

“…Detailed description of these polymorphisms, their gene frequencies in different populations, molecular-genetic studies, and techniques for electrophoretic analysis of proline-rich protein (PRP) polymorphisms have been recently reviewed (Azen and Maeda, 1988;Azen, 1989;Minaguchi and Bennick, 1989).…”

Section: Introductionmentioning

confidence: 99%

Genetics of Salivary Protein Polymorphisms

Azen

1993

Critical Reviews in Oral Biology & Medicine

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Human salivary PRPs are detennined by six closely linked genes on chromosome 12pl3.2. The many PRPs show complex electrophoretic patterns that differ between individuals and reflect numerous genetic polymorphisms. Frequent length and null polymorphisms are common among PRPs. Common themes emerge as a background for these PRP polymorphisms. First, posttranslational proteolysis occurs with double-banded patterns among acidic PRPs and the generation of numerous basic PRPs derived from precursor proteins. Specific mutations may interfere with proteolysis, preventing generation of double-banded acidic PRPs (as with the Pa protein) or of small basic PRPs from precursor proteins (as with Pm proteins). Second, single cysteine substitutions in PRPs (Pa from PRHI and Gl 8 from PRB3) may lead to disulfide bonded homodimers as well as heterodimers with salivary peroxidase. Third, frequent homologous and unequal crossing-over within the PRP gene cluster leads to frequent protein size-variants (intragenic events as with the Gl protein variants) and the generation of the PRB2/1 fusion gene (intergenic event) with deletion of the PRB1 coding region and absence of multiple PRBI coded proteins (Ps, Pm, Pe) in PRB2/1 homozygotes. Fourth, null mutations may also be produced (as with PsO and Gl 0) by single nucleotide changes.

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“…Acidic PRPs bind calcium and inhibit hydroxyapatite crystal growth thus contributing to calcium homeostasis in the mouth and the acquired enamel pellicle of erupted teeth (39). PRPs are encoded by six genes with each gene having several alleles giving rise to ~20 secreted proteins showing complex patterns of polymorphism (40). PRPs are synthesized as precursor proteins and undergo proteolysis as well as posttranslational modifications giving rise to basic PRPs and glycosylated PRPs.…”

Section: Discussionmentioning

confidence: 99%

Discovery of putative salivary biomarkers for Sjögren’s syndrome using high resolution mass spectrometry and bioinformatics

et al. 2012

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Abstract:The purpose of the current study was to determine if saliva contains biomarkers that can be used as diagnostic tools for Sjögren's syndrome (SjS). Twenty seven SjS patients and 27 age-matched healthy controls were recruited for these studies. Unstimulated glandular saliva was collected from the Wharton's duct using a suction device. Two μl of salvia were processed for mass spectrometry analyses on a prOTOF 2000 matrix-assisted laser desorption/ ionization orthogonal time of flight (MALDI O-TOF) mass spectrometer. Raw data were analyzed using bioinformatic tools to identify biomarkers. MALDI O-TOF MS analyses of saliva samples were highly reproducible and the mass spectra generated were very rich in peptides and peptide fragments in the 750-7,500 Da range. Data analysis using bioinformatic tools resulted in several classification models being built and several biomarkers identified. One model based on 7 putative biomarkers yielded a sensitivity of 97.5%, specificity of 97.8% and an accuracy of 97.6%. One biomarker was present only in SjS samples and was identified as a proteolytic peptide originating from human basic salivary proline-rich protein 3 precursor. We conclude that salivary biomarkers detected by high-resolution mass spectrometry coupled with powerful bioinformatic tools offer the potential to serve as diagnostic/prognostic tools for SjS. (J Oral Sci 54, 61-70, 2012)

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Invited Review: Genetics of Human Salivary Proteins

Cited by 62 publications

References 168 publications

Differential expression of proline-rich proteins in rabbit salivary glands.

Differential expression of proline-rich proteins in rabbit salivary glands.

Genetics of Salivary Protein Polymorphisms

Discovery of putative salivary biomarkers for Sjögren’s syndrome using high resolution mass spectrometry and bioinformatics

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