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Cloning of a fibrillar collagen gene expressed in the mesenchymal cells of the developing sea urchin embryo
We have cloned and characterized several overlapping cDNAs that specify a large portion of a Paracentrotus lividus fibrillar collagen molecule. Our conclusions are based on sequencing data, which showed that the clones code for a 786-amino acid collagenous domain composed of an uninterrupted series...
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Published in: | The Journal of biological chemistry 1990-04, Vol.265 (12), p.7050-7054 |
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creator | D'ALESSIO, M RAMIREZ, F SUZUKI, H. R SOLURSH, M GAMBINO, R |
description | We have cloned and characterized several overlapping cDNAs that specify a large portion of a Paracentrotus lividus fibrillar
collagen molecule. Our conclusions are based on sequencing data, which showed that the clones code for a 786-amino acid collagenous
domain composed of an uninterrupted series of Gly-X-Y repeats and for a 265-amino acid carboxyl-terminal globular extension.
The latter domain exhibits features highly reminiscent of those of the vertebrate counterparts, notably a putative carboxyl-peptidase
cleavage site, a series of similarly arranged cysteinyl residues, and an N-linked glycosylation attachment site. In situ and
Northern blot hybridizations have established the size, time of appearance, and tissue localization of the collagen mRNA during
sea urchin development. The collagen transcript, 9 kilobases in length, is first detected in the primary and, more predominantly,
in the secondary mesenchyme cells of late gastrulae where it progressively accumulates thereafter. This and other work (D'Alessio,
M., Ramirez, F., Suzuki, H.R., Solursh, M., and Gambino, R. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 9303-9307) provide
evidence of a genetic heterogeneity of fibrillar collagens in the sea urchin embryo and suggest that the two genes are activated
in the same cell lineages at distinct developmental stages. |
doi_str_mv | 10.1016/s0021-9258(19)39257-9 |
format | article |
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collagen molecule. Our conclusions are based on sequencing data, which showed that the clones code for a 786-amino acid collagenous
domain composed of an uninterrupted series of Gly-X-Y repeats and for a 265-amino acid carboxyl-terminal globular extension.
The latter domain exhibits features highly reminiscent of those of the vertebrate counterparts, notably a putative carboxyl-peptidase
cleavage site, a series of similarly arranged cysteinyl residues, and an N-linked glycosylation attachment site. In situ and
Northern blot hybridizations have established the size, time of appearance, and tissue localization of the collagen mRNA during
sea urchin development. The collagen transcript, 9 kilobases in length, is first detected in the primary and, more predominantly,
in the secondary mesenchyme cells of late gastrulae where it progressively accumulates thereafter. This and other work (D'Alessio,
M., Ramirez, F., Suzuki, H.R., Solursh, M., and Gambino, R. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 9303-9307) provide
evidence of a genetic heterogeneity of fibrillar collagens in the sea urchin embryo and suggest that the two genes are activated
in the same cell lineages at distinct developmental stages.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)39257-9</identifier><identifier>PMID: 2324112</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Cloning, Molecular - methods ; Collagen - genetics ; DNA - genetics ; Embryo, Nonmammalian - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Genes ; Humans ; Marine ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Paracentrotus lividus ; Procollagen - genetics ; Restriction Mapping ; Sea Urchins - embryology ; Sea Urchins - genetics ; Sequence Homology, Nucleic Acid ; Software</subject><ispartof>The Journal of biological chemistry, 1990-04, Vol.265 (12), p.7050-7054</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-40b11bbf9db1733fe67fb84f158193b5d5b133226d5d4f8b5645473e17fa646a3</citedby><cites>FETCH-LOGICAL-c505t-40b11bbf9db1733fe67fb84f158193b5d5b133226d5d4f8b5645473e17fa646a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6875539$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2324112$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>D'ALESSIO, M</creatorcontrib><creatorcontrib>RAMIREZ, F</creatorcontrib><creatorcontrib>SUZUKI, H. R</creatorcontrib><creatorcontrib>SOLURSH, M</creatorcontrib><creatorcontrib>GAMBINO, R</creatorcontrib><title>Cloning of a fibrillar collagen gene expressed in the mesenchymal cells of the developing sea urchin embryo</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have cloned and characterized several overlapping cDNAs that specify a large portion of a Paracentrotus lividus fibrillar
collagen molecule. Our conclusions are based on sequencing data, which showed that the clones code for a 786-amino acid collagenous
domain composed of an uninterrupted series of Gly-X-Y repeats and for a 265-amino acid carboxyl-terminal globular extension.
The latter domain exhibits features highly reminiscent of those of the vertebrate counterparts, notably a putative carboxyl-peptidase
cleavage site, a series of similarly arranged cysteinyl residues, and an N-linked glycosylation attachment site. In situ and
Northern blot hybridizations have established the size, time of appearance, and tissue localization of the collagen mRNA during
sea urchin development. The collagen transcript, 9 kilobases in length, is first detected in the primary and, more predominantly,
in the secondary mesenchyme cells of late gastrulae where it progressively accumulates thereafter. This and other work (D'Alessio,
M., Ramirez, F., Suzuki, H.R., Solursh, M., and Gambino, R. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 9303-9307) provide
evidence of a genetic heterogeneity of fibrillar collagens in the sea urchin embryo and suggest that the two genes are activated
in the same cell lineages at distinct developmental stages.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular - methods</subject><subject>Collagen - genetics</subject><subject>DNA - genetics</subject><subject>Embryo, Nonmammalian - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Genes</subject><subject>Humans</subject><subject>Marine</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Hybridization</subject><subject>Paracentrotus lividus</subject><subject>Procollagen - genetics</subject><subject>Restriction Mapping</subject><subject>Sea Urchins - embryology</subject><subject>Sea Urchins - genetics</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Software</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><recordid>eNqFkUGLFDEQhYMo6-zqT1gIKKKHXlNJJ-kcZdB1YcHDKngLSXdlOpruHpMZdf693c4w1w2ECryvXoVXhFwDuwEG6n1hjENluGzegnkn5oeuzBOyAtaISkj4_pSszshzclnKDzaf2sAFueCC1wB8RX6u0zTGcUOnQB0N0eeYksu0neaywZHOFyn-3WYsBTsaR7rrkQ5YcGz7w-ASbTGlsvQvQoe_MU3bxbGgo_vc9nMLDj4fphfkWXCp4MtTvSLfPn38uv5c3X-5vVt_uK9ayeSuqpkH8D6YzoMWIqDSwTd1ANmAEV520oMQnKtOdnVovFS1rLVA0MGpWjlxRd4cfbd5-rXHsrNDLMsv3YjTvlhtNBgtzaMgSDU7KzmD8gi2eSolY7DbHAeXDxaYXbZhH5ao7RK1BWP_b8MuA65PA_Z-wO7cdYp_1l-fdFdal0J2YxvLGVONllIsNq-OWB83_Z-Y0fo4tT0OlitpgVvNJBP_AH7CngM</recordid><startdate>19900425</startdate><enddate>19900425</enddate><creator>D'ALESSIO, M</creator><creator>RAMIREZ, F</creator><creator>SUZUKI, H. 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R ; SOLURSH, M ; GAMBINO, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-40b11bbf9db1733fe67fb84f158193b5d5b133226d5d4f8b5645473e17fa646a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular - methods</topic><topic>Collagen - genetics</topic><topic>DNA - genetics</topic><topic>Embryo, Nonmammalian - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Genes</topic><topic>Humans</topic><topic>Marine</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Hybridization</topic><topic>Paracentrotus lividus</topic><topic>Procollagen - genetics</topic><topic>Restriction Mapping</topic><topic>Sea Urchins - embryology</topic><topic>Sea Urchins - genetics</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Software</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>D'ALESSIO, M</creatorcontrib><creatorcontrib>RAMIREZ, F</creatorcontrib><creatorcontrib>SUZUKI, H. 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collagen molecule. Our conclusions are based on sequencing data, which showed that the clones code for a 786-amino acid collagenous
domain composed of an uninterrupted series of Gly-X-Y repeats and for a 265-amino acid carboxyl-terminal globular extension.
The latter domain exhibits features highly reminiscent of those of the vertebrate counterparts, notably a putative carboxyl-peptidase
cleavage site, a series of similarly arranged cysteinyl residues, and an N-linked glycosylation attachment site. In situ and
Northern blot hybridizations have established the size, time of appearance, and tissue localization of the collagen mRNA during
sea urchin development. The collagen transcript, 9 kilobases in length, is first detected in the primary and, more predominantly,
in the secondary mesenchyme cells of late gastrulae where it progressively accumulates thereafter. This and other work (D'Alessio,
M., Ramirez, F., Suzuki, H.R., Solursh, M., and Gambino, R. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 9303-9307) provide
evidence of a genetic heterogeneity of fibrillar collagens in the sea urchin embryo and suggest that the two genes are activated
in the same cell lineages at distinct developmental stages.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2324112</pmid><doi>10.1016/s0021-9258(19)39257-9</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Cloning, Molecular - methods Collagen - genetics DNA - genetics Embryo, Nonmammalian - metabolism Fundamental and applied biological sciences. Psychology Gene Expression Genes Humans Marine Molecular and cellular biology Molecular genetics Molecular Sequence Data Nucleic Acid Hybridization Paracentrotus lividus Procollagen - genetics Restriction Mapping Sea Urchins - embryology Sea Urchins - genetics Sequence Homology, Nucleic Acid Software |
title | Cloning of a fibrillar collagen gene expressed in the mesenchymal cells of the developing sea urchin embryo |
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