Loading…

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...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1990-04, Vol.265 (12), p.7050-7054
Main Authors: D'ALESSIO, M, RAMIREZ, F, SUZUKI, H. R, SOLURSH, M, GAMBINO, R
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c505t-40b11bbf9db1733fe67fb84f158193b5d5b133226d5d4f8b5645473e17fa646a3
cites cdi_FETCH-LOGICAL-c505t-40b11bbf9db1733fe67fb84f158193b5d5b133226d5d4f8b5645473e17fa646a3
container_end_page 7054
container_issue 12
container_start_page 7050
container_title The Journal of biological chemistry
container_volume 265
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
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79719759</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>15654765</sourcerecordid><originalsourceid>FETCH-LOGICAL-c505t-40b11bbf9db1733fe67fb84f158193b5d5b133226d5d4f8b5645473e17fa646a3</originalsourceid><addsrcrecordid>eNqFkUGLFDEQhYMo6-zqT1gIKKKHXlNJJ-kcZdB1YcHDKngLSXdlOpruHpMZdf693c4w1w2ECryvXoVXhFwDuwEG6n1hjENluGzegnkn5oeuzBOyAtaISkj4_pSszshzclnKDzaf2sAFueCC1wB8RX6u0zTGcUOnQB0N0eeYksu0neaywZHOFyn-3WYsBTsaR7rrkQ5YcGz7w-ASbTGlsvQvQoe_MU3bxbGgo_vc9nMLDj4fphfkWXCp4MtTvSLfPn38uv5c3X-5vVt_uK9ayeSuqpkH8D6YzoMWIqDSwTd1ANmAEV520oMQnKtOdnVovFS1rLVA0MGpWjlxRd4cfbd5-rXHsrNDLMsv3YjTvlhtNBgtzaMgSDU7KzmD8gi2eSolY7DbHAeXDxaYXbZhH5ao7RK1BWP_b8MuA65PA_Z-wO7cdYp_1l-fdFdal0J2YxvLGVONllIsNq-OWB83_Z-Y0fo4tT0OlitpgVvNJBP_AH7CngM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15654765</pqid></control><display><type>article</type><title>Cloning of a fibrillar collagen gene expressed in the mesenchymal cells of the developing sea urchin embryo</title><source>ScienceDirect</source><creator>D'ALESSIO, M ; RAMIREZ, F ; SUZUKI, H. R ; SOLURSH, M ; GAMBINO, R</creator><creatorcontrib>D'ALESSIO, M ; RAMIREZ, F ; SUZUKI, H. R ; SOLURSH, M ; GAMBINO, R</creatorcontrib><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><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&amp;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. R</creator><creator>SOLURSH, M</creator><creator>GAMBINO, R</creator><general>American Society for Biochemistry and Molecular Biology</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>7TM</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19900425</creationdate><title>Cloning of a fibrillar collagen gene expressed in the mesenchymal cells of the developing sea urchin embryo</title><author>D'ALESSIO, M ; RAMIREZ, F ; SUZUKI, H. 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. R</creatorcontrib><creatorcontrib>SOLURSH, M</creatorcontrib><creatorcontrib>GAMBINO, R</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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) 1: Biological Sciences &amp; Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>D'ALESSIO, M</au><au>RAMIREZ, F</au><au>SUZUKI, H. R</au><au>SOLURSH, M</au><au>GAMBINO, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning of a fibrillar collagen gene expressed in the mesenchymal cells of the developing sea urchin embryo</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-04-25</date><risdate>1990</risdate><volume>265</volume><issue>12</issue><spage>7050</spage><epage>7054</epage><pages>7050-7054</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>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.</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>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 1990-04, Vol.265 (12), p.7050-7054
issn 0021-9258
1083-351X
language eng
recordid cdi_proquest_miscellaneous_79719759
source ScienceDirect
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
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T21%3A42%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cloning%20of%20a%20fibrillar%20collagen%20gene%20expressed%20in%20the%20mesenchymal%20cells%20of%20the%20developing%20sea%20urchin%20embryo&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=D'ALESSIO,%20M&rft.date=1990-04-25&rft.volume=265&rft.issue=12&rft.spage=7050&rft.epage=7054&rft.pages=7050-7054&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/s0021-9258(19)39257-9&rft_dat=%3Cproquest_cross%3E15654765%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c505t-40b11bbf9db1733fe67fb84f158193b5d5b133226d5d4f8b5645473e17fa646a3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=15654765&rft_id=info:pmid/2324112&rfr_iscdi=true