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J. Biol. Chem., Vol. 265, Issue 11, 6104-6111, 04, 1990
TE Petersen, MR Martzen, A Ichinose and EW Davie
The organization and structure of the gene coding for plasminogen has been
determined by a combination of in vitro amplification of leukocyte DNA from
normal individuals and isolation of unique clones from three different
human genomic libraries. These clones were characterized by restriction
mapping, Southern blotting, and DNA sequencing. The gene for human
plasminogen spanned about 52.5 kilobases of DNA and consisted of 19 exons
separated by 18 introns. DNA sequence analysis revealed that the five
kringle structures in plasminogen were coded by two exons. The nucleotides
in the introns at the intron-exon boundaries were GT-AG analogous to those
found in other eukaryotic genes. Three polyadenylation sites for
plasminogen mRNA were also identified. When the amino acid sequences
deduced from the genomic DNA and cDNAs of plasminogen were compared with
that of the plasma protein determined by amino acid sequence analysis, an
apparent amino acid polymorphism was observed in several positions of the
polypeptide chain. Nucleotide sequence analysis of the amplified genomic
DNAs and genomic clones also revealed that the plasminogen gene was very
closely related to several other proteins, including apolipoprotein(a).
This protein may have evolved via duplication and exon shuffling of the
plasminogen gene. The presence of another plasminogen-related gene(s) in
the human genomic library was also observed.
Characterization of the gene for human plasminogen, a key proenzyme in the fibrinolytic system
Department of Biochemistry, University of Washington, Seattle 98195.
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