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Effect of fibrin binding on plasminogen activation
272
ABSTRACTS;
CHINESE-JAPANESE
SYMP. 1990
Vol. 63, No. 2
MOLECULAR CLONING AND RFLP STUDIES OF HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-l (PAI-1) GENE. 7.hu Chen. Gmuna. Yu Wu. Weic&ng Wana. Yangig Yelu Department of Pathophysiology, Shanghai Second Medical University and Shanghai Institute of Hematology, Shanghai 200025, China Plasminogen Activator Inhibitor-l (PAI-1) plays an important regulatory role in the control of the fibrinolytic activity in blood. By screening a human genomic library with human PAI- cDNA probe, we isolated a group of phage clones containing PAIgene (12kb) its 5' and and 3' flanking sequences about 12kb respectively. These clones are helpful to the further research of PA1 gene's regulation of expression. We also performed a study on the restriction fragment length polymorphisms (RFLPs) for the PAI1 gene among 35 unrelated Chinese individuals. The results were shown as follows: (1) Taq I detected allelic 2.7kb and 1.8kb fragments, with the frequencies of 0.97 and 0.03 respectively. 2.7kb homozygotes and 2.7kb/1.8kb heterozygotes appeared with the frequencies of 94% and 6%. (2) Sac1 identified an invariant 4.8kb band and a two-allele polymorphism with fragments of either 23kb or 16kb, with the frequencies of 0.96 and 0.04. 23kb homozygotes and 23kb/16kb heterozygotes appeared with the frequencies of 91% and 9%. (3) Hind111 revealed a single two-allele polymorphism with bands either at 25kb or at 14kb, with the frequencies of 0.34 and 0.66. According to our own restriction map of the PA1 gene, this polymorphic site was mapped to the gene's 3'flanking region. 25kb homozygotes, 25kb/14kb heterozygotes and 14kb homozygotes appeared with the frequencies of 23%, 46% and 31% respectively. EFFECT OF FIBRIN BINDING ON PLASMINOGEN ACTIVATION n.I.J.Wu andY. Shi Department of. Biochemistry, Medical College, National Cheng-Kung University, Tainan, .Taiwan, ROC Fragments of plasminogen consisting of various domains were applied to study the plasminogen binding onto fibrin and the effect of domains and fibrin on the plasminogen activation. The order of affinity of plasminogen fragments to fibrin clot is kringle l-5, miniplasminogen > kringle l-3 > kringle 4, Kringle l-5, not kringle l-3, can effectively microplasminogen. inhibit the binding of plasminogen onto fibrin. Kringle l-3 and kringle 5 bind on the same locations of fibrin and kringle 5 has the higher affinity to fibrin. Kringle 4 and active site domain of plasminogen are not essential in the interaction of plasminogen and fibrin. Microplasminogen, which consists mainly active site domain, can be activated by urokinase and streptokinase at similar rate as Glu-plasminogen. Tissue-type plasminogen activator can activate Glu-plasminogen and microplasminogen at similar slow rate in the absence of fibrinogen degradation products (FDP) as stimulant. In the presence of FDP, the rate of Glu-plasminogen activation increased several folds. However, the activation of microplasminogen remained the same with or without FDP. The interaction of FDP and kringle domains of plasminogen is essential in FDP enhancement on plasminogen.
ABSTRACTS;
CHINESE-JAPANESE
SYMP. 1990
Vol. 63, No. 2
MOLECULAR CLONING AND RFLP STUDIES OF HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-l (PAI-1) GENE. 7.hu Chen. Gmuna. Yu Wu. Weic&ng Wana. Yangig Yelu Department of Pathophysiology, Shanghai Second Medical University and Shanghai Institute of Hematology, Shanghai 200025, China Plasminogen Activator Inhibitor-l (PAI-1) plays an important regulatory role in the control of the fibrinolytic activity in blood. By screening a human genomic library with human PAI- cDNA probe, we isolated a group of phage clones containing PAIgene (12kb) its 5' and and 3' flanking sequences about 12kb respectively. These clones are helpful to the further research of PA1 gene's regulation of expression. We also performed a study on the restriction fragment length polymorphisms (RFLPs) for the PAI1 gene among 35 unrelated Chinese individuals. The results were shown as follows: (1) Taq I detected allelic 2.7kb and 1.8kb fragments, with the frequencies of 0.97 and 0.03 respectively. 2.7kb homozygotes and 2.7kb/1.8kb heterozygotes appeared with the frequencies of 94% and 6%. (2) Sac1 identified an invariant 4.8kb band and a two-allele polymorphism with fragments of either 23kb or 16kb, with the frequencies of 0.96 and 0.04. 23kb homozygotes and 23kb/16kb heterozygotes appeared with the frequencies of 91% and 9%. (3) Hind111 revealed a single two-allele polymorphism with bands either at 25kb or at 14kb, with the frequencies of 0.34 and 0.66. According to our own restriction map of the PA1 gene, this polymorphic site was mapped to the gene's 3'flanking region. 25kb homozygotes, 25kb/14kb heterozygotes and 14kb homozygotes appeared with the frequencies of 23%, 46% and 31% respectively. EFFECT OF FIBRIN BINDING ON PLASMINOGEN ACTIVATION n.I.J.Wu andY. Shi Department of. Biochemistry, Medical College, National Cheng-Kung University, Tainan, .Taiwan, ROC Fragments of plasminogen consisting of various domains were applied to study the plasminogen binding onto fibrin and the effect of domains and fibrin on the plasminogen activation. The order of affinity of plasminogen fragments to fibrin clot is kringle l-5, miniplasminogen > kringle l-3 > kringle 4, Kringle l-5, not kringle l-3, can effectively microplasminogen. inhibit the binding of plasminogen onto fibrin. Kringle l-3 and kringle 5 bind on the same locations of fibrin and kringle 5 has the higher affinity to fibrin. Kringle 4 and active site domain of plasminogen are not essential in the interaction of plasminogen and fibrin. Microplasminogen, which consists mainly active site domain, can be activated by urokinase and streptokinase at similar rate as Glu-plasminogen. Tissue-type plasminogen activator can activate Glu-plasminogen and microplasminogen at similar slow rate in the absence of fibrinogen degradation products (FDP) as stimulant. In the presence of FDP, the rate of Glu-plasminogen activation increased several folds. However, the activation of microplasminogen remained the same with or without FDP. The interaction of FDP and kringle domains of plasminogen is essential in FDP enhancement on plasminogen.