High-resolution electrophoretic analysis of rat parotid salivary proteins

Williams, Katherine M.; Ekström, Jørgen; Marshall, T. C.

doi:10.1002/(sici)1522-2683(19990601)20:7<1373::aid-elps1373>3.0.co;2-z

Cited by 12 publications

(5 citation statements)

References 40 publications

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“…Williams et al [18] obtained 2-DE maps from rat parotid saliva using a pI range similar to that used in the present study (pH 3-10). Comparisons with our gels indicate a similar distribution for some spots, notably those we identified as α-amylase, deoxyribonuclease, parotid secretory protein, and demilune cell and parotid protein.…”

Section: Discussionmentioning

confidence: 94%

“…whole saliva). The presence of basic and acidic PRPs was suggested in a rat parotid saliva 2-DE pattern [18]. These proteins are not constitutively expressed in mouse salivary glands [9], but rather induced by isoproterenol administration or tannin ingestion [5,9], which can also explain the failure to detect them in our control samples.…”

Section: Discussionmentioning

confidence: 95%

“…Mouse saliva and salivary glands have been studied for diet-induced changes, and 2-DE maps of rodent saliva have been reported for rat parotid [18] and submandibular [19] saliva. However, no extensive protein characterization was performed in any of these studies.…”

Section: Introductionmentioning

confidence: 99%

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Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet

et al. 2010

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BackgroundPrevious studies suggested that dietary tannin ingestion may induce changes in mouse salivary proteins in addition to the primarily studied proline-rich proteins (PRPs). The aim of the present study was to determine the protein expression changes induced by condensed tannin intake on the fraction of mouse whole salivary proteins that are unable to form insoluble tannin-protein complexes. Two-dimensional polyacrylamide gel electrophoresis protein separation was used, followed by protein identification by mass spectrometry.ResultsFifty-seven protein spots were excised from control group gels, and 21 different proteins were identified. With tannin consumption, the expression levels of one α-amylase isoform and one unidentified protein increased, whereas acidic mammalian chitinase and Muc10 decreased. Additionally, two basic spots that stained pink with Coomassie Brilliant Blue R-250 were newly observed, suggesting that some induced PRPs may remain uncomplexed or form soluble complexes with tannins.ConclusionThis proteomic analysis provides evidence that other salivary proteins, in addition to tannin-precipitating proteins, are affected by tannin ingestion. Changes in the expression levels of the acidic mammalian chitinase precursor and in one of the 14 salivary α-amylase isoforms underscores the need to further investigate their role in tannin ingestion.

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 95%

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Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet

et al. 2010

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“…Salivary proteomic studies on animals have not been well illustrated through MS analysis. However, 2D gel electrophoresis-based proteomic studies have been carried out on parotid salivary proteins in cats (38), rats (39), and ferrets (40); detailed MS study was carried out on goat and bovine salivary proteins (22). Lamy et al (21) reported detailed differentiation in protein expression using sheep and goat saliva in their study of ingestive behavior.…”

Section: Discussionmentioning

confidence: 99%

Exploration of salivary proteins in buffalo: an approach to find marker proteins for estrus

et al. 2014

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Saliva is considered as the best source of biological material for biomarker discovery studies since it is noninvasive in comparison to other body sources. Usually buffalo cannot precisely express estrus signals. Hence, there is a need for concise methods to detect the time of estrus to ensure the success of artificial insemination. Therefore, we have established a reference proteome map on the whole saliva of buffalo during their estrous cycle with special reference to estrus. Nearly 12 bands have been observed using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of whole saliva. Collectively, 179 proteins are identified with respect to different phases of the estrous cycle using mass spectrometry. On the whole, 37 proteins are exclusively expressed in the estrus phase, which include ␤-enolase, Toll-like receptor (TLR) 4, clusterin, lactoperoxidase, serotransferrin, TGM3, UBA6, and transducin. Among the proteins, ␤-enolase and TLR 4 were validated, and their specific expression was found during estrus as compared to other phases using immunoblot. The functional annotation reveals many as binding proteins in the estrus saliva when compared to the other phases. The present findings conclude that the proteomic approach adopted to identify the proteins from buffalo saliva around the estrous cycle may provide a new tool for screening the estrus phase. The results further conclude that the specific expression of ␤-enolase and TLR 4 can be taken as the indicator of estrus in buffalo.-Muthukumar, S., Rajkumar, R., Rajesh, D

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“…These maps may provide valuable tools for identifying markers of different diseases. Although many proteins have been described in human saliva using different techniques [12], and the protein composition of rodent saliva has been investigated by 2-DE [13,14], a large human saliva 2-DE protein map has not yet been constructed.…”

Section: Introductionmentioning

confidence: 99%

Mapping of proteins in human saliva using two‐dimensional gel electrophoresis and peptide mass fingerprinting

2003

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Human saliva contains a large number of proteins that can be used for diagnosis and are of great potential in clinical and epidemiological research. The aim of this work was to map the proteins in saliva by two-dimensional gel electrophoresis (2-DE), and to identify abundant proteins by peptide mass fingerprinting using trypsin cleavage and matrix-assisted laser desorption/ionization-time of flight-mass spectrometry analysis. One hundred proteins were identified representing 20 different identities according to accession numbers. Abundant proteins expressed in different forms were: alpha-amylase, immunoglobulin A, prolactin-inducible protein, zinc-alpha(2)-glycoprotein and cystatins (S, SA, D and SN). Other proteins found were interleukin-1 receptor antagonist, von Ebner's gland protein (lipocalin-1) and calgranulin A and B (S100A8 and A9). Furthermore, apolipoprotein A-I, beta(2)-microglobulin, glutathione S-transferase P and fatty acid-binding protein were also identified. Our results show that human saliva contains a large number of proteins that are involved in inflammatory and immune responses. The 2-DE protein map constructed opens the possibility to investigate protein changes associated with disease processes.

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High-resolution electrophoretic analysis of rat parotid salivary proteins

Cited by 12 publications

References 40 publications

Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet

Changes in mouse whole saliva soluble proteome induced by tannin-enriched diet

Exploration of salivary proteins in buffalo: an approach to find marker proteins for estrus

Mapping of proteins in human saliva using two‐dimensional gel electrophoresis and peptide mass fingerprinting

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