Gla-rich protein (GRP), a new vitamin K-dependent protein identified from sturgeon cartilage and highly conserved in vertebrates.
Identifieur interne : 000441 ( PubMed/Checkpoint ); précédent : 000440; suivant : 000442Gla-rich protein (GRP), a new vitamin K-dependent protein identified from sturgeon cartilage and highly conserved in vertebrates.
Auteurs : Carla S B. Viegas [Portugal] ; Dina C. Simes ; Vincent Laizé ; Matthew K. Williamson ; Paul A. Price ; M Leonor CancelaSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Binding Sites, Cartilage (metabolism), Conserved Sequence, Fish Proteins (chemistry), Fish Proteins (metabolism), Fishes, Gene Expression Regulation, Humans, Hydrogen-Ion Concentration, Models, Biological, Molecular Sequence Data, Phylogeny, Sequence Homology, Amino Acid, Tissue Distribution, Vitamin K (metabolism).
- MESH :
- chemical , chemistry : Fish Proteins.
- metabolism : Cartilage, Fish Proteins, Vitamin K.
- Amino Acid Sequence, Animals, Binding Sites, Conserved Sequence, Fishes, Gene Expression Regulation, Humans, Hydrogen-Ion Concentration, Models, Biological, Molecular Sequence Data, Phylogeny, Sequence Homology, Amino Acid, Tissue Distribution.
Abstract
We report the isolation of a novel vitamin K-dependent protein from the calcified cartilage of Adriatic sturgeon (Acipenser nacarii). This 10.2-kDa secreted protein contains 16 gamma-carboxyglutamic acid (Gla) residues in its 74-residue sequence, the highest Gla percent of any known protein, and we have therefore termed it Gla-rich protein (GRP). GRP has a high charge density (36 negative+16 positive=20 net negative) yet is insoluble at neutral pH. GRP has orthologs in all taxonomic groups of vertebrates, and a paralog (GRP2) in bony fish; no GRP homolog was found in invertebrates. There is no significant sequence homology between GRP and the Gla-containing region of any presently known vitamin K-dependent protein. Forty-seven GRP sequences were obtained by a combination of cDNA cloning and comparative genomics: all 47 have a propeptide that contains a gamma-carboxylase recognition site and a mature protein with 14 highly conserved Glu residues, each of them being gamma-carboxylated in sturgeon. The protein sequence of GRP is also highly conserved, with 78% identity between sturgeon and human GRP. Analysis of the corresponding gene structures suggests a highly constrained organization, particularly for exon 4, which encodes the core Gla domain. GRP mRNA is found in virtually all rat and sturgeon tissues examined, with the highest expression in cartilage. Cells expressing GRP include chondrocytes, chondroblasts, osteoblasts, and osteocytes. Because of its potential to bind calcium through Gla residues, we suggest that GRP may regulate calcium in the extracellular environment.
DOI: 10.1074/jbc.M802761200
PubMed: 18836183
Affiliations:
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Simes</name></author><author><name sortKey="Laize, Vincent" sort="Laize, Vincent" uniqKey="Laize V" first="Vincent" last="Laizé">Vincent Laizé</name></author><author><name sortKey="Williamson, Matthew K" sort="Williamson, Matthew K" uniqKey="Williamson M" first="Matthew K" last="Williamson">Matthew K. Williamson</name></author><author><name sortKey="Price, Paul A" sort="Price, Paul A" uniqKey="Price P" first="Paul A" last="Price">Paul A. 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Viegas</name><affiliation wicri:level="1"><nlm:affiliation>Centre of Marine Sciences (CCMAR), University of Algarve, 8005-139 Faro, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>Centre of Marine Sciences (CCMAR), University of Algarve, 8005-139 Faro</wicri:regionArea><wicri:noRegion>8005-139 Faro</wicri:noRegion></affiliation></author><author><name sortKey="Simes, Dina C" sort="Simes, Dina C" uniqKey="Simes D" first="Dina C" last="Simes">Dina C. Simes</name></author><author><name sortKey="Laize, Vincent" sort="Laize, Vincent" uniqKey="Laize V" first="Vincent" last="Laizé">Vincent Laizé</name></author><author><name sortKey="Williamson, Matthew K" sort="Williamson, Matthew K" uniqKey="Williamson M" first="Matthew K" last="Williamson">Matthew K. Williamson</name></author><author><name sortKey="Price, Paul A" sort="Price, Paul A" uniqKey="Price P" first="Paul A" last="Price">Paul A. Price</name></author><author><name sortKey="Cancela, M Leonor" sort="Cancela, M Leonor" uniqKey="Cancela M" first="M Leonor" last="Cancela">M Leonor Cancela</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Cartilage (metabolism)</term><term>Conserved Sequence</term><term>Fish Proteins (chemistry)</term><term>Fish Proteins (metabolism)</term><term>Fishes</term><term>Gene Expression Regulation</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Models, Biological</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Sequence Homology, Amino Acid</term><term>Tissue Distribution</term><term>Vitamin K (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fish Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cartilage</term><term>Fish Proteins</term><term>Vitamin K</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Conserved Sequence</term><term>Fishes</term><term>Gene Expression Regulation</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Models, Biological</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Sequence Homology, Amino Acid</term><term>Tissue Distribution</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report the isolation of a novel vitamin K-dependent protein from the calcified cartilage of Adriatic sturgeon (Acipenser nacarii). This 10.2-kDa secreted protein contains 16 gamma-carboxyglutamic acid (Gla) residues in its 74-residue sequence, the highest Gla percent of any known protein, and we have therefore termed it Gla-rich protein (GRP). GRP has a high charge density (36 negative+16 positive=20 net negative) yet is insoluble at neutral pH. GRP has orthologs in all taxonomic groups of vertebrates, and a paralog (GRP2) in bony fish; no GRP homolog was found in invertebrates. There is no significant sequence homology between GRP and the Gla-containing region of any presently known vitamin K-dependent protein. Forty-seven GRP sequences were obtained by a combination of cDNA cloning and comparative genomics: all 47 have a propeptide that contains a gamma-carboxylase recognition site and a mature protein with 14 highly conserved Glu residues, each of them being gamma-carboxylated in sturgeon. The protein sequence of GRP is also highly conserved, with 78% identity between sturgeon and human GRP. Analysis of the corresponding gene structures suggests a highly constrained organization, particularly for exon 4, which encodes the core Gla domain. GRP mRNA is found in virtually all rat and sturgeon tissues examined, with the highest expression in cartilage. Cells expressing GRP include chondrocytes, chondroblasts, osteoblasts, and osteocytes. Because of its potential to bind calcium through Gla residues, we suggest that GRP may regulate calcium in the extracellular environment.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18836183</PMID><DateCreated><Year>2008</Year><Month>12</Month><Day>22</Day></DateCreated><DateCompleted><Year>2009</Year><Month>03</Month><Day>13</Day></DateCompleted><DateRevised><Year>2016</Year><Month>10</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>52</Issue><PubDate><Year>2008</Year><Month>Dec</Month><Day>26</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Gla-rich protein (GRP), a new vitamin K-dependent protein identified from sturgeon cartilage and highly conserved in vertebrates.</ArticleTitle><Pagination><MedlinePgn>36655-64</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M802761200</ELocationID><Abstract><AbstractText>We report the isolation of a novel vitamin K-dependent protein from the calcified cartilage of Adriatic sturgeon (Acipenser nacarii). This 10.2-kDa secreted protein contains 16 gamma-carboxyglutamic acid (Gla) residues in its 74-residue sequence, the highest Gla percent of any known protein, and we have therefore termed it Gla-rich protein (GRP). GRP has a high charge density (36 negative+16 positive=20 net negative) yet is insoluble at neutral pH. GRP has orthologs in all taxonomic groups of vertebrates, and a paralog (GRP2) in bony fish; no GRP homolog was found in invertebrates. There is no significant sequence homology between GRP and the Gla-containing region of any presently known vitamin K-dependent protein. Forty-seven GRP sequences were obtained by a combination of cDNA cloning and comparative genomics: all 47 have a propeptide that contains a gamma-carboxylase recognition site and a mature protein with 14 highly conserved Glu residues, each of them being gamma-carboxylated in sturgeon. The protein sequence of GRP is also highly conserved, with 78% identity between sturgeon and human GRP. Analysis of the corresponding gene structures suggests a highly constrained organization, particularly for exon 4, which encodes the core Gla domain. GRP mRNA is found in virtually all rat and sturgeon tissues examined, with the highest expression in cartilage. Cells expressing GRP include chondrocytes, chondroblasts, osteoblasts, and osteocytes. Because of its potential to bind calcium through Gla residues, we suggest that GRP may regulate calcium in the extracellular environment.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Viegas</LastName><ForeName>Carla S B</ForeName><Initials>CS</Initials><AffiliationInfo><Affiliation>Centre of Marine Sciences (CCMAR), University of Algarve, 8005-139 Faro, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Simes</LastName><ForeName>Dina C</ForeName><Initials>DC</Initials></Author><Author ValidYN="Y"><LastName>Laizé</LastName><ForeName>Vincent</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Williamson</LastName><ForeName>Matthew K</ForeName><Initials>MK</Initials></Author><Author ValidYN="Y"><LastName>Price</LastName><ForeName>Paul A</ForeName><Initials>PA</Initials></Author><Author ValidYN="Y"><LastName>Cancela</LastName><ForeName>M 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Leonor" sort="Cancela, M Leonor" uniqKey="Cancela M" first="M Leonor" last="Cancela">M Leonor Cancela</name><name sortKey="Laize, Vincent" sort="Laize, Vincent" uniqKey="Laize V" first="Vincent" last="Laizé">Vincent Laizé</name><name sortKey="Price, Paul A" sort="Price, Paul A" uniqKey="Price P" first="Paul A" last="Price">Paul A. Price</name><name sortKey="Simes, Dina C" sort="Simes, Dina C" uniqKey="Simes D" first="Dina C" last="Simes">Dina C. Simes</name><name sortKey="Williamson, Matthew K" sort="Williamson, Matthew K" uniqKey="Williamson M" first="Matthew K" last="Williamson">Matthew K. Williamson</name></noCountry><country name="Portugal"><noRegion><name sortKey="Viegas, Carla S B" sort="Viegas, Carla S B" uniqKey="Viegas C" first="Carla S B" last="Viegas">Carla S B. Viegas</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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