Ehlers-Danlos syndrome type IV: a multi-exon deletion in one of the two COL3A1 alleles affecting structure, stability, and processing of type III procollagen
We have studied a patient with severe, dominantly inherited Ehlers-Danlos syndrome type IV. The results indicate that this patient carries a deletion of 3.3 kilo-base pairs in the triple helical coding domain of one of the two alleles for the pro-alpha-chains of type III collagen (COL3A1). His cultu...
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| Veröffentlicht in: | The Journal of biological chemistry 1988-05, Vol.263 (13), p.6226-6232 |
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| creator | Superti-Furga, A Gugler, E Gitzelmann, R Steinmann, B |
| description | We have studied a patient with severe, dominantly inherited Ehlers-Danlos syndrome type IV. The results indicate that this patient carries a deletion of 3.3 kilo-base pairs in the triple helical coding domain of one of the two alleles for the pro-alpha-chains of type III collagen (COL3A1). His cultured skin fibroblasts contain equal amounts of normal length mRNA and of mRNA shortened by approximately 600 bases, and synthesize both normal and shortened pro-alpha 1(III)-chains. In procollagen molecules containing one or more shortened chains, a triple helix is formed with a length of only about 780 amino acids. The mutant procollagen molecules have decreased thermal stability, are less efficiently secreted, and are not processed as their normal counterpart. The deletion in this family is the first mutation to be described in COL3A1. |
| doi_str_mv | 10.1016/S0021-9258(18)68776-9 |
| format | Article |
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The results indicate that this patient carries a deletion of 3.3 kilo-base pairs in the triple helical coding domain of one of the two alleles for the pro-alpha-chains of type III collagen (COL3A1). His cultured skin fibroblasts contain equal amounts of normal length mRNA and of mRNA shortened by approximately 600 bases, and synthesize both normal and shortened pro-alpha 1(III)-chains. In procollagen molecules containing one or more shortened chains, a triple helix is formed with a length of only about 780 amino acids. The mutant procollagen molecules have decreased thermal stability, are less efficiently secreted, and are not processed as their normal counterpart. The deletion in this family is the first mutation to be described in COL3A1.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)68776-9</identifier><identifier>PMID: 2834369</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Adult ; Alleles ; Autoradiography ; Biological and medical sciences ; Chromosome Deletion ; DNA Restriction Enzymes - metabolism ; Ehlers-Danlos Syndrome - genetics ; Electrophoresis, Polyacrylamide Gel ; Fibroblasts - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Humans ; Male ; Molecular and cellular biology ; Molecular genetics ; Peptide Mapping ; Phenotype ; Procollagen - analysis ; RNA, Messenger - analysis ; Skin - ultrastructure</subject><ispartof>The Journal of biological chemistry, 1988-05, Vol.263 (13), p.6226-6232</ispartof><rights>1988 © 1988 ASBMB. 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The results indicate that this patient carries a deletion of 3.3 kilo-base pairs in the triple helical coding domain of one of the two alleles for the pro-alpha-chains of type III collagen (COL3A1). His cultured skin fibroblasts contain equal amounts of normal length mRNA and of mRNA shortened by approximately 600 bases, and synthesize both normal and shortened pro-alpha 1(III)-chains. In procollagen molecules containing one or more shortened chains, a triple helix is formed with a length of only about 780 amino acids. The mutant procollagen molecules have decreased thermal stability, are less efficiently secreted, and are not processed as their normal counterpart. The deletion in this family is the first mutation to be described in COL3A1.</description><subject>Adult</subject><subject>Alleles</subject><subject>Autoradiography</subject><subject>Biological and medical sciences</subject><subject>Chromosome Deletion</subject><subject>DNA Restriction Enzymes - metabolism</subject><subject>Ehlers-Danlos Syndrome - genetics</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fibroblasts - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Humans</subject><subject>Male</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Peptide Mapping</subject><subject>Phenotype</subject><subject>Procollagen - analysis</subject><subject>RNA, Messenger - analysis</subject><subject>Skin - ultrastructure</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkduKFDEQhoMo6-zoIywEFFHY1k4nnU57I8u46sDAXnjAu5BOqmci6WRMut2dh_FdzRyYW3OTouqr-ov6Eboi5VtSEv7ua1lWpGirWrwm4g0XTcOL9hGakVLQgtbk52M0OyNP0WVKv8r8WEsu0EUlKKO8naG_txsHMRUflXch4bTzJoYB8LjbAl7-eI8VHiY32gIegscGHIw2B9bj4AGHHo-bDN8HvLhb0RuClXOZSVj1PejR-jVOY5z0OEW4zqHqrLPj7horb_A2Bg0p7aH9oIPicnlIB-fUGvwz9KRXLsHz0z9H3z_dflt8KVZ3n5eLm1WhGa_aAsq6U7XmRggGhlVCGy0aoLRRXBPBW94IaEH0RNSiKTUzXdWrjvSsNgYaRufo1XFu1v49QRrlYJOGvISHMCVJWEtZvnoG6yOoY0gpQi-30Q4q7iQp5d4WebBF7m8uiZAHW2Sb-65OAlM3gDl3nXzI9ZenukpauT4qr206Y42oGKvrjL04Yhu73tzbCLKzQW9gkBWnklDJqxzM0YcjBflkfyxEmbQFr8HkDj1KE-x_1v0Hd8O2jQ</recordid><startdate>19880505</startdate><enddate>19880505</enddate><creator>Superti-Furga, A</creator><creator>Gugler, E</creator><creator>Gitzelmann, R</creator><creator>Steinmann, B</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19880505</creationdate><title>Ehlers-Danlos syndrome type IV: a multi-exon deletion in one of the two COL3A1 alleles affecting structure, stability, and processing of type III procollagen</title><author>Superti-Furga, A ; Gugler, E ; Gitzelmann, R ; Steinmann, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4629-e05ba5c6d884ed428cdc87e337a6c1869678e9e8f185870c4db2fab1f45dde743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Adult</topic><topic>Alleles</topic><topic>Autoradiography</topic><topic>Biological and medical sciences</topic><topic>Chromosome Deletion</topic><topic>DNA Restriction Enzymes - metabolism</topic><topic>Ehlers-Danlos Syndrome - genetics</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fibroblasts - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Humans</topic><topic>Male</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Peptide Mapping</topic><topic>Phenotype</topic><topic>Procollagen - analysis</topic><topic>RNA, Messenger - analysis</topic><topic>Skin - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Superti-Furga, A</creatorcontrib><creatorcontrib>Gugler, E</creatorcontrib><creatorcontrib>Gitzelmann, R</creatorcontrib><creatorcontrib>Steinmann, B</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Superti-Furga, A</au><au>Gugler, E</au><au>Gitzelmann, R</au><au>Steinmann, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ehlers-Danlos syndrome type IV: a multi-exon deletion in one of the two COL3A1 alleles affecting structure, stability, and processing of type III procollagen</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-05-05</date><risdate>1988</risdate><volume>263</volume><issue>13</issue><spage>6226</spage><epage>6232</epage><pages>6226-6232</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have studied a patient with severe, dominantly inherited Ehlers-Danlos syndrome type IV. The results indicate that this patient carries a deletion of 3.3 kilo-base pairs in the triple helical coding domain of one of the two alleles for the pro-alpha-chains of type III collagen (COL3A1). His cultured skin fibroblasts contain equal amounts of normal length mRNA and of mRNA shortened by approximately 600 bases, and synthesize both normal and shortened pro-alpha 1(III)-chains. In procollagen molecules containing one or more shortened chains, a triple helix is formed with a length of only about 780 amino acids. The mutant procollagen molecules have decreased thermal stability, are less efficiently secreted, and are not processed as their normal counterpart. The deletion in this family is the first mutation to be described in COL3A1.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2834369</pmid><doi>10.1016/S0021-9258(18)68776-9</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adult Alleles Autoradiography Biological and medical sciences Chromosome Deletion DNA Restriction Enzymes - metabolism Ehlers-Danlos Syndrome - genetics Electrophoresis, Polyacrylamide Gel Fibroblasts - metabolism Fundamental and applied biological sciences. Psychology Gene expression Humans Male Molecular and cellular biology Molecular genetics Peptide Mapping Phenotype Procollagen - analysis RNA, Messenger - analysis Skin - ultrastructure |
| title | Ehlers-Danlos syndrome type IV: a multi-exon deletion in one of the two COL3A1 alleles affecting structure, stability, and processing of type III procollagen |
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