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The structure of the human tissue-type plasminogen activator gene: correlation of intron and exon structures to functional and structural domains.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
1984 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 81, no 17, 5355-9 p.Article in journal (Refereed) Published
Abstract [en]

A genomic clone carrying the human tissue-type plasminogen activator (t-PA) gene was isolated from a cosmid library, and the gene structure was elucidated by restriction mapping, Southern blotting, and DNA sequencing. The cosmid contained all the coding parts of the mRNA, except for the first 58 bases in the 5' end of the mRNA, and had a total length of greater than 20 kilobases. It was separated into at least 14 exons by at least 13 introns, and the exons seemed to code for structural or functional domains. Thus, the signal peptide, the propeptide, and the domains of the heavy chain, including the regions homologous to growth factors, and to the "finger" structure of fibronectin, are all encoded by separate exons. In addition, the two kringle regions of t-PA were both coded for by two exons and were cleaved by introns at identical positions. The region coding for the light chain, comprising the serine protease part of the molecule was split by four introns, revealing a gene organization similar to other serine proteases.

Place, publisher, year, edition, pages
1984. Vol. 81, no 17, 5355-9 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:umu:diva-59761PubMedID: 6089198OAI: oai:DiVA.org:umu-59761DiVA: diva2:556436
Available from: 2012-09-25 Created: 2012-09-25 Last updated: 2017-12-07

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