Role of associated and covalently bound lipids in salivary mucin hydrophobicity: Effect of proteolysis and disulfide bridge reduction
The hydrophobic properties of salivary mucus glycoprotein were investigated by fluorescence spectroscopy using bis(8-anilino-1-naphthalene-sulfonate). The mucin, purified from rat submandibular salivary gland, was subjected to removal of associated and covalently bound lipids, degradation with prona...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1988-03, Vol.151 (3), p.1046-1053 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Slomiany, B.L. Murty, V.L.N. Sarosiek, J. Piotrowski, J. Slomiany, A. |
| description | The hydrophobic properties of salivary mucus glycoprotein were investigated by fluorescence spectroscopy using bis(8-anilino-1-naphthalene-sulfonate). The mucin, purified from rat submandibular salivary gland, was subjected to removal of associated and covalently bound lipids, degradation with pronase, and reduction with β-mercaptoethanol, and titrated with the probe. Analyses of fluorescence data revealed the presence of 49 ± 5 hydrophobic binding sites in the intact mucin molecule, a 69% increase in the number of binding sites occurred following extraction of associated lipids, while the removal of covalently bound fatty acids caused a 25% decrease in the binding sites. Proteolytic destruction of the nonglycosylated regions of the glycoprotein essentially abolished the probe binding, whereas reduction produced glycoprotein subunits whose combined number of hydrophobic binding sites was 2.4 times greater than that of mucus glycoprotein polymer. The results suggest that associated and covalently bound lipids contribute to hydrophobic characteristics of salivary mucin and that the hydrophobic binding sites reside on the nonglycosylated regions of this glycoprotein buried within its core. |
| doi_str_mv | 10.1016/S0006-291X(88)80471-6 |
| format | Article |
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The mucin, purified from rat submandibular salivary gland, was subjected to removal of associated and covalently bound lipids, degradation with pronase, and reduction with β-mercaptoethanol, and titrated with the probe. Analyses of fluorescence data revealed the presence of 49 ± 5 hydrophobic binding sites in the intact mucin molecule, a 69% increase in the number of binding sites occurred following extraction of associated lipids, while the removal of covalently bound fatty acids caused a 25% decrease in the binding sites. Proteolytic destruction of the nonglycosylated regions of the glycoprotein essentially abolished the probe binding, whereas reduction produced glycoprotein subunits whose combined number of hydrophobic binding sites was 2.4 times greater than that of mucus glycoprotein polymer. The results suggest that associated and covalently bound lipids contribute to hydrophobic characteristics of salivary mucin and that the hydrophobic binding sites reside on the nonglycosylated regions of this glycoprotein buried within its core.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(88)80471-6</identifier><identifier>PMID: 3281667</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Disulfides - analysis ; Fundamental and applied biological sciences. Psychology ; Glycosylation ; Hydrogen Bonding ; Lipids - analysis ; Mucins - analysis ; Peptide Hydrolases - metabolism ; Rats ; Saliva - analysis ; salivary mucus glycoprotein ; Spectrometry, Fluorescence ; submandibular gland ; Submandibular Gland - analysis</subject><ispartof>Biochemical and biophysical research communications, 1988-03, Vol.151 (3), p.1046-1053</ispartof><rights>1988 Academic Press, Inc.</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c421t-c30a77e9d737e098c26c177688fecbee69237762e1dc180320abb8948cfa13973</citedby><cites>FETCH-LOGICAL-c421t-c30a77e9d737e098c26c177688fecbee69237762e1dc180320abb8948cfa13973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(88)80471-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19558353$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3281667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Slomiany, B.L.</creatorcontrib><creatorcontrib>Murty, V.L.N.</creatorcontrib><creatorcontrib>Sarosiek, J.</creatorcontrib><creatorcontrib>Piotrowski, J.</creatorcontrib><creatorcontrib>Slomiany, A.</creatorcontrib><title>Role of associated and covalently bound lipids in salivary mucin hydrophobicity: Effect of proteolysis and disulfide bridge reduction</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The hydrophobic properties of salivary mucus glycoprotein were investigated by fluorescence spectroscopy using bis(8-anilino-1-naphthalene-sulfonate). The mucin, purified from rat submandibular salivary gland, was subjected to removal of associated and covalently bound lipids, degradation with pronase, and reduction with β-mercaptoethanol, and titrated with the probe. Analyses of fluorescence data revealed the presence of 49 ± 5 hydrophobic binding sites in the intact mucin molecule, a 69% increase in the number of binding sites occurred following extraction of associated lipids, while the removal of covalently bound fatty acids caused a 25% decrease in the binding sites. Proteolytic destruction of the nonglycosylated regions of the glycoprotein essentially abolished the probe binding, whereas reduction produced glycoprotein subunits whose combined number of hydrophobic binding sites was 2.4 times greater than that of mucus glycoprotein polymer. The results suggest that associated and covalently bound lipids contribute to hydrophobic characteristics of salivary mucin and that the hydrophobic binding sites reside on the nonglycosylated regions of this glycoprotein buried within its core.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Disulfides - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycosylation</subject><subject>Hydrogen Bonding</subject><subject>Lipids - analysis</subject><subject>Mucins - analysis</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Rats</subject><subject>Saliva - analysis</subject><subject>salivary mucus glycoprotein</subject><subject>Spectrometry, Fluorescence</subject><subject>submandibular gland</subject><subject>Submandibular Gland - analysis</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1q3TAQhUVpSG_TPkJAm5Z04VaybEnuppSQpIVAoT_QnZClcTNF17qV7At-gLx3dH9Il1mJ0Zw5M5yPkHPO3nPG5YcfjDFZ1R3_faH1O80axSv5jKw461hVc9Y8J6tHyQvyMue_jHHeyO6UnIpacynVitx_jwFoHKjNOTq0E3hqR09d3NoA4xQW2se5fATcoM8UR5ptwK1NC13PrpR3i09xcxd7dDgtH-nVMICbdpabFCeIYcmY954e8xwG9ED7hP4P0AR-dhPG8RU5GWzI8Pr4npFf11c_L79Ut99uvl5-vq1cU_OpcoJZpaDzSihgnXa1dFwpqXVZ2QPIrhalrIF7xzUTNbN9r7tGu8Fy0SlxRt4efMtp_2bIk1ljdhCCHSHO2aiSSsuFeFLI28KgZFiE7UHoUsw5wWA2CdclHcOZ2XEye05mB8FobfacjCxz58cFc78G_zh1BFP6b459m50NQ7Kjw_zfvGtbLdrdoZ8OOiixbRGSyQ5hdOAxFQzGR3zikgdK_LHP</recordid><startdate>19880330</startdate><enddate>19880330</enddate><creator>Slomiany, B.L.</creator><creator>Murty, V.L.N.</creator><creator>Sarosiek, J.</creator><creator>Piotrowski, J.</creator><creator>Slomiany, A.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19880330</creationdate><title>Role of associated and covalently bound lipids in salivary mucin hydrophobicity: Effect of proteolysis and disulfide bridge reduction</title><author>Slomiany, B.L. ; Murty, V.L.N. ; Sarosiek, J. ; Piotrowski, J. ; Slomiany, A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c421t-c30a77e9d737e098c26c177688fecbee69237762e1dc180320abb8948cfa13973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Disulfides - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycosylation</topic><topic>Hydrogen Bonding</topic><topic>Lipids - analysis</topic><topic>Mucins - analysis</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Rats</topic><topic>Saliva - analysis</topic><topic>salivary mucus glycoprotein</topic><topic>Spectrometry, Fluorescence</topic><topic>submandibular gland</topic><topic>Submandibular Gland - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Slomiany, B.L.</creatorcontrib><creatorcontrib>Murty, V.L.N.</creatorcontrib><creatorcontrib>Sarosiek, J.</creatorcontrib><creatorcontrib>Piotrowski, J.</creatorcontrib><creatorcontrib>Slomiany, A.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Slomiany, B.L.</au><au>Murty, V.L.N.</au><au>Sarosiek, J.</au><au>Piotrowski, J.</au><au>Slomiany, A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of associated and covalently bound lipids in salivary mucin hydrophobicity: Effect of proteolysis and disulfide bridge reduction</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1988-03-30</date><risdate>1988</risdate><volume>151</volume><issue>3</issue><spage>1046</spage><epage>1053</epage><pages>1046-1053</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The hydrophobic properties of salivary mucus glycoprotein were investigated by fluorescence spectroscopy using bis(8-anilino-1-naphthalene-sulfonate). The mucin, purified from rat submandibular salivary gland, was subjected to removal of associated and covalently bound lipids, degradation with pronase, and reduction with β-mercaptoethanol, and titrated with the probe. Analyses of fluorescence data revealed the presence of 49 ± 5 hydrophobic binding sites in the intact mucin molecule, a 69% increase in the number of binding sites occurred following extraction of associated lipids, while the removal of covalently bound fatty acids caused a 25% decrease in the binding sites. Proteolytic destruction of the nonglycosylated regions of the glycoprotein essentially abolished the probe binding, whereas reduction produced glycoprotein subunits whose combined number of hydrophobic binding sites was 2.4 times greater than that of mucus glycoprotein polymer. The results suggest that associated and covalently bound lipids contribute to hydrophobic characteristics of salivary mucin and that the hydrophobic binding sites reside on the nonglycosylated regions of this glycoprotein buried within its core.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3281667</pmid><doi>10.1016/S0006-291X(88)80471-6</doi><tpages>8</tpages></addata></record> |
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| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Disulfides - analysis Fundamental and applied biological sciences. Psychology Glycosylation Hydrogen Bonding Lipids - analysis Mucins - analysis Peptide Hydrolases - metabolism Rats Saliva - analysis salivary mucus glycoprotein Spectrometry, Fluorescence submandibular gland Submandibular Gland - analysis |
| title | Role of associated and covalently bound lipids in salivary mucin hydrophobicity: Effect of proteolysis and disulfide bridge reduction |
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