Characterization of the human lysyl oxidase gene locus
Lysyl oxidase (EC 1.4.3.13) is a copper-dependent enzyme acting principally on collagen and elastin catalyzing the formation of aldehyde cross-links. It is also believed to possess a tumor suppressor activity as the anti-oncogene of ras. While rat, human, and mouse lysyl oxidase cDNAs have been clon...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-07, Vol.267 (20), p.14382-14387 |
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| container_title | The Journal of biological chemistry |
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| creator | SVINARICH, D. M TWOMEY, T. A MACAULEY, S. P KREBS, C. J YANG, T. P KRAWETZ, S. A |
| description | Lysyl oxidase (EC 1.4.3.13) is a copper-dependent enzyme acting principally on collagen and elastin catalyzing the formation
of aldehyde cross-links. It is also believed to possess a tumor suppressor activity as the anti-oncogene of ras. While rat,
human, and mouse lysyl oxidase cDNAs have been cloned, little is known about the structure of the gene, its organization,
or regulation. This paper describes the cloning of an intronic segment of the human lysyl oxidase gene. Sequence analysis
defined the location of an intron that separates the prepro-coding segments from the segment encoding the catalytic domain.
Genomic restriction mapping and gene copy number data established that multiple lysyl oxidase mRNA transcripts originate from
a single gene and thus are products of alternative splicing. Northern analysis of adult and fetal fibroblast RNA showed a
dominant approximately 4.3-kilobase lysyl oxidase mRNA transcript that varied in abundance as a function of cell line. These
data are consistent with a complex mechanism regulating the expression of the lysyl oxidase gene. |
| doi_str_mv | 10.1016/S0021-9258(19)49723-8 |
| format | Article |
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of aldehyde cross-links. It is also believed to possess a tumor suppressor activity as the anti-oncogene of ras. While rat,
human, and mouse lysyl oxidase cDNAs have been cloned, little is known about the structure of the gene, its organization,
or regulation. This paper describes the cloning of an intronic segment of the human lysyl oxidase gene. Sequence analysis
defined the location of an intron that separates the prepro-coding segments from the segment encoding the catalytic domain.
Genomic restriction mapping and gene copy number data established that multiple lysyl oxidase mRNA transcripts originate from
a single gene and thus are products of alternative splicing. Northern analysis of adult and fetal fibroblast RNA showed a
dominant approximately 4.3-kilobase lysyl oxidase mRNA transcript that varied in abundance as a function of cell line. These
data are consistent with a complex mechanism regulating the expression of the lysyl oxidase gene.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)49723-8</identifier><identifier>PMID: 1352776</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Adult ; Animals ; Base Sequence ; Biological and medical sciences ; Blotting, Northern ; Cells, Cultured ; Chromosome Mapping ; DNA - genetics ; DNA - isolation & purification ; Fetus ; Fibroblasts - enzymology ; Fundamental and applied biological sciences. Psychology ; Genes ; Genes, Tumor Suppressor ; Genes. Genome ; Humans ; Mice ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Protein-Lysine 6-Oxidase - genetics ; Rats ; Restriction Mapping ; RNA, Messenger - genetics ; Sequence Homology, Nucleic Acid ; Skin - enzymology ; Software ; Transcription, Genetic</subject><ispartof>The Journal of biological chemistry, 1992-07, Vol.267 (20), p.14382-14387</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-a8420d152ce3abc724870c381c9fd96c017d34f92e5d47150b9409c178b006c23</citedby><cites>FETCH-LOGICAL-c440t-a8420d152ce3abc724870c381c9fd96c017d34f92e5d47150b9409c178b006c23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5557896$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1352776$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SVINARICH, D. M</creatorcontrib><creatorcontrib>TWOMEY, T. A</creatorcontrib><creatorcontrib>MACAULEY, S. P</creatorcontrib><creatorcontrib>KREBS, C. J</creatorcontrib><creatorcontrib>YANG, T. P</creatorcontrib><creatorcontrib>KRAWETZ, S. A</creatorcontrib><title>Characterization of the human lysyl oxidase gene locus</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Lysyl oxidase (EC 1.4.3.13) is a copper-dependent enzyme acting principally on collagen and elastin catalyzing the formation
of aldehyde cross-links. It is also believed to possess a tumor suppressor activity as the anti-oncogene of ras. While rat,
human, and mouse lysyl oxidase cDNAs have been cloned, little is known about the structure of the gene, its organization,
or regulation. This paper describes the cloning of an intronic segment of the human lysyl oxidase gene. Sequence analysis
defined the location of an intron that separates the prepro-coding segments from the segment encoding the catalytic domain.
Genomic restriction mapping and gene copy number data established that multiple lysyl oxidase mRNA transcripts originate from
a single gene and thus are products of alternative splicing. Northern analysis of adult and fetal fibroblast RNA showed a
dominant approximately 4.3-kilobase lysyl oxidase mRNA transcript that varied in abundance as a function of cell line. These
data are consistent with a complex mechanism regulating the expression of the lysyl oxidase gene.</description><subject>Adult</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Cells, Cultured</subject><subject>Chromosome Mapping</subject><subject>DNA - genetics</subject><subject>DNA - isolation & purification</subject><subject>Fetus</subject><subject>Fibroblasts - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Genes, Tumor Suppressor</subject><subject>Genes. Genome</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Oligodeoxyribonucleotides</subject><subject>Protein-Lysine 6-Oxidase - genetics</subject><subject>Rats</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Skin - enzymology</subject><subject>Software</subject><subject>Transcription, Genetic</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1P3DAQhq2qiC7b_gSkHFAFh8CMP2L7iFZAKyFxaJF6sxzHIa7ysdiJ6PLrybIr6I25zGGed2b0EHKMcI6AxcUvAIq5pkKdoj7jWlKWq09kgaBYzgT--UwWb8gXcpTSX5iLazwkh8gElbJYkGLV2Gjd6GN4tmMY-myos7HxWTN1ts_aTdq02fAvVDb57MH3PmsHN6Wv5KC2bfLf9n1J7q-vfq9-5Ld3Nz9Xl7e54xzG3CpOoUJBnWe2dJJyJcExhU7XlS4coKwYrzX1ouISBZSag3YoVQlQOMqW5Ptu7zoOj5NPo-lCcr5tbe-HKRnJoFBSwIcgFkIrrreg2IEuDilFX5t1DJ2NG4NgtmLNq1iztWZQm1exRs254_2Bqex89Z7amZznJ_u5Tc62dbS9C-kNE0JIpf_DmvDQPIXoTRkG1_jO0EIaOr_AmaLsBZm2ik0</recordid><startdate>19920715</startdate><enddate>19920715</enddate><creator>SVINARICH, D. 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Genome</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Oligodeoxyribonucleotides</topic><topic>Protein-Lysine 6-Oxidase - genetics</topic><topic>Rats</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Skin - enzymology</topic><topic>Software</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SVINARICH, D. M</creatorcontrib><creatorcontrib>TWOMEY, T. A</creatorcontrib><creatorcontrib>MACAULEY, S. P</creatorcontrib><creatorcontrib>KREBS, C. J</creatorcontrib><creatorcontrib>YANG, T. P</creatorcontrib><creatorcontrib>KRAWETZ, S. 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of aldehyde cross-links. It is also believed to possess a tumor suppressor activity as the anti-oncogene of ras. While rat,
human, and mouse lysyl oxidase cDNAs have been cloned, little is known about the structure of the gene, its organization,
or regulation. This paper describes the cloning of an intronic segment of the human lysyl oxidase gene. Sequence analysis
defined the location of an intron that separates the prepro-coding segments from the segment encoding the catalytic domain.
Genomic restriction mapping and gene copy number data established that multiple lysyl oxidase mRNA transcripts originate from
a single gene and thus are products of alternative splicing. Northern analysis of adult and fetal fibroblast RNA showed a
dominant approximately 4.3-kilobase lysyl oxidase mRNA transcript that varied in abundance as a function of cell line. These
data are consistent with a complex mechanism regulating the expression of the lysyl oxidase gene.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1352776</pmid><doi>10.1016/S0021-9258(19)49723-8</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-07, Vol.267 (20), p.14382-14387 |
| issn | 0021-9258 1083-351X |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adult Animals Base Sequence Biological and medical sciences Blotting, Northern Cells, Cultured Chromosome Mapping DNA - genetics DNA - isolation & purification Fetus Fibroblasts - enzymology Fundamental and applied biological sciences. Psychology Genes Genes, Tumor Suppressor Genes. Genome Humans Mice Molecular and cellular biology Molecular genetics Molecular Sequence Data Oligodeoxyribonucleotides Protein-Lysine 6-Oxidase - genetics Rats Restriction Mapping RNA, Messenger - genetics Sequence Homology, Nucleic Acid Skin - enzymology Software Transcription, Genetic |
| title | Characterization of the human lysyl oxidase gene locus |
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