The major soluble 19.6 kDa protein of the organic shell matrix of the freshwater snail Biomphalaria glabrata is an N-glycosylated dermatopontin
The major Biomphalaria glabrata shell matrix protein of 19.6 kDa was isolated by preparative electrophoresis and sequenced. The sequence of 148 amino acids showed 32% sequence identity to mammalian dermatopontin sequences and 34–37% identity to two invertebrate dermatopontins described previously. A...
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| Veröffentlicht in: | Biochimica et biophysica acta 2003-08, Vol.1650 (1), p.92-98 |
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| creator | Marxen, Julia C. Nimtz, Manfred Becker, Wilhelm Mann, Karlheinz |
| description | The major
Biomphalaria glabrata shell matrix protein of 19.6 kDa was isolated by preparative electrophoresis and sequenced. The sequence of 148 amino acids showed 32% sequence identity to mammalian dermatopontin sequences and 34–37% identity to two invertebrate dermatopontins described previously. A unique feature of the shell matrix dermatopontin was the presence of a single N-glycosylation consensus sequence, the asparagine of which was completely modified with a pentasaccharide. Sequence analysis of this short
N-glycan by mass spectrometry and carbohydrate composition analysis indicated that it was the ubiquitous
N-glycan core oligosaccharide with the exception that the terminal mannoses were 3-
O-methylated. Dermatopontin is widespread in mammalian extracellular matrices, including the matrix of biominerals such as bone and teeth. Its occurrence in an invertebrate biomineral indicates that such phylogenetically distant biomineral-forming systems as vertebrate bone and mollusk shell share components which have undergone surprisingly few changes during a long evolution. |
| doi_str_mv | 10.1016/S1570-9639(03)00203-6 |
| format | Article |
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Biomphalaria glabrata shell matrix protein of 19.6 kDa was isolated by preparative electrophoresis and sequenced. The sequence of 148 amino acids showed 32% sequence identity to mammalian dermatopontin sequences and 34–37% identity to two invertebrate dermatopontins described previously. A unique feature of the shell matrix dermatopontin was the presence of a single N-glycosylation consensus sequence, the asparagine of which was completely modified with a pentasaccharide. Sequence analysis of this short
N-glycan by mass spectrometry and carbohydrate composition analysis indicated that it was the ubiquitous
N-glycan core oligosaccharide with the exception that the terminal mannoses were 3-
O-methylated. Dermatopontin is widespread in mammalian extracellular matrices, including the matrix of biominerals such as bone and teeth. Its occurrence in an invertebrate biomineral indicates that such phylogenetically distant biomineral-forming systems as vertebrate bone and mollusk shell share components which have undergone surprisingly few changes during a long evolution.</description><identifier>ISSN: 1570-9639</identifier><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1878-1454</identifier><identifier>DOI: 10.1016/S1570-9639(03)00203-6</identifier><identifier>PMID: 12922172</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Biomineralization ; Biomphalaria - metabolism ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; Cell Adhesion Molecules - isolation & purification ; Cell Adhesion Molecules - metabolism ; Chondroitin Sulfate Proteoglycans ; Dermatopontin ; Electrophoresis, Polyacrylamide Gel ; Extracellular Matrix Proteins ; Freshwater ; Glycosylation ; Humans ; Molecular Sequence Data ; Mollusk shell ; N-glycan</subject><ispartof>Biochimica et biophysica acta, 2003-08, Vol.1650 (1), p.92-98</ispartof><rights>2003 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-a7194a06d8776a1fc88cf717178ec39b45bca14f96aae5c72417f7082dd453ee3</citedby><cites>FETCH-LOGICAL-c458t-a7194a06d8776a1fc88cf717178ec39b45bca14f96aae5c72417f7082dd453ee3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1570963903002036$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12922172$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marxen, Julia C.</creatorcontrib><creatorcontrib>Nimtz, Manfred</creatorcontrib><creatorcontrib>Becker, Wilhelm</creatorcontrib><creatorcontrib>Mann, Karlheinz</creatorcontrib><title>The major soluble 19.6 kDa protein of the organic shell matrix of the freshwater snail Biomphalaria glabrata is an N-glycosylated dermatopontin</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>The major
Biomphalaria glabrata shell matrix protein of 19.6 kDa was isolated by preparative electrophoresis and sequenced. The sequence of 148 amino acids showed 32% sequence identity to mammalian dermatopontin sequences and 34–37% identity to two invertebrate dermatopontins described previously. A unique feature of the shell matrix dermatopontin was the presence of a single N-glycosylation consensus sequence, the asparagine of which was completely modified with a pentasaccharide. Sequence analysis of this short
N-glycan by mass spectrometry and carbohydrate composition analysis indicated that it was the ubiquitous
N-glycan core oligosaccharide with the exception that the terminal mannoses were 3-
O-methylated. Dermatopontin is widespread in mammalian extracellular matrices, including the matrix of biominerals such as bone and teeth. Its occurrence in an invertebrate biomineral indicates that such phylogenetically distant biomineral-forming systems as vertebrate bone and mollusk shell share components which have undergone surprisingly few changes during a long evolution.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biomineralization</subject><subject>Biomphalaria - metabolism</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Adhesion Molecules - isolation & purification</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Chondroitin Sulfate Proteoglycans</subject><subject>Dermatopontin</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Extracellular Matrix Proteins</subject><subject>Freshwater</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Mollusk shell</subject><subject>N-glycan</subject><issn>1570-9639</issn><issn>0006-3002</issn><issn>1878-1454</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctuFDEQRVsIRELgE0BeIVh0sNvPXiEITymCBWFtVburZxzc7cH2APMV_DKezEQsIy_KUp17S1W3aZ4yes4oU6--Malp2yvev6D8JaUd5a2615wyo03LhBT36_8WOWke5Xy9h7SWD5sT1vVdx3R32vy9WiOZ4TomkmPYDgEJ688V-fEOyCbFgn4hcSKlUjGtYPGO5DWGUDUl-T-3vSlhXv-GgtVmAR_IWx_nzRoCJA9kFWBIUID4TGAhX9pV2LmYd6EKRjJiqmZxE5fil8fNgwlCxifHetZ8__D-6uJTe_n14-eLN5etE9KUFjTrBVA1Gq0VsMkZ4ybN6jPoeD8IOThgYuoVAEqnO8H0pKnpxlFIjsjPmucH37rkzy3mYmefXV0MFozbbDWXRnRc3AkyLXuuFK-gPIAuxZwTTnaT_AxpZxm1-8jsTWR2n4el3N5EZlXVPTsO2A4zjv9Vx4wq8PoAYL3HL4_JZudxcTj6hK7YMfo7RvwD-nmnbg</recordid><startdate>20030821</startdate><enddate>20030821</enddate><creator>Marxen, Julia C.</creator><creator>Nimtz, Manfred</creator><creator>Becker, Wilhelm</creator><creator>Mann, Karlheinz</creator><general>Elsevier B.V</general><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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20030821</creationdate><title>The major soluble 19.6 kDa protein of the organic shell matrix of the freshwater snail Biomphalaria glabrata is an N-glycosylated dermatopontin</title><author>Marxen, Julia C. ; Nimtz, Manfred ; Becker, Wilhelm ; Mann, Karlheinz</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-a7194a06d8776a1fc88cf717178ec39b45bca14f96aae5c72417f7082dd453ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biomineralization</topic><topic>Biomphalaria - metabolism</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Adhesion Molecules - isolation & purification</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Chondroitin Sulfate Proteoglycans</topic><topic>Dermatopontin</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Extracellular Matrix Proteins</topic><topic>Freshwater</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Mollusk shell</topic><topic>N-glycan</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marxen, Julia C.</creatorcontrib><creatorcontrib>Nimtz, Manfred</creatorcontrib><creatorcontrib>Becker, Wilhelm</creatorcontrib><creatorcontrib>Mann, Karlheinz</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marxen, Julia C.</au><au>Nimtz, Manfred</au><au>Becker, Wilhelm</au><au>Mann, Karlheinz</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The major soluble 19.6 kDa protein of the organic shell matrix of the freshwater snail Biomphalaria glabrata is an N-glycosylated dermatopontin</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>2003-08-21</date><risdate>2003</risdate><volume>1650</volume><issue>1</issue><spage>92</spage><epage>98</epage><pages>92-98</pages><issn>1570-9639</issn><issn>0006-3002</issn><eissn>1878-1454</eissn><abstract>The major
Biomphalaria glabrata shell matrix protein of 19.6 kDa was isolated by preparative electrophoresis and sequenced. The sequence of 148 amino acids showed 32% sequence identity to mammalian dermatopontin sequences and 34–37% identity to two invertebrate dermatopontins described previously. A unique feature of the shell matrix dermatopontin was the presence of a single N-glycosylation consensus sequence, the asparagine of which was completely modified with a pentasaccharide. Sequence analysis of this short
N-glycan by mass spectrometry and carbohydrate composition analysis indicated that it was the ubiquitous
N-glycan core oligosaccharide with the exception that the terminal mannoses were 3-
O-methylated. Dermatopontin is widespread in mammalian extracellular matrices, including the matrix of biominerals such as bone and teeth. Its occurrence in an invertebrate biomineral indicates that such phylogenetically distant biomineral-forming systems as vertebrate bone and mollusk shell share components which have undergone surprisingly few changes during a long evolution.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>12922172</pmid><doi>10.1016/S1570-9639(03)00203-6</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Biomineralization Biomphalaria - metabolism Carrier Proteins - isolation & purification Carrier Proteins - metabolism Cell Adhesion Molecules - isolation & purification Cell Adhesion Molecules - metabolism Chondroitin Sulfate Proteoglycans Dermatopontin Electrophoresis, Polyacrylamide Gel Extracellular Matrix Proteins Freshwater Glycosylation Humans Molecular Sequence Data Mollusk shell N-glycan |
| title | The major soluble 19.6 kDa protein of the organic shell matrix of the freshwater snail Biomphalaria glabrata is an N-glycosylated dermatopontin |
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