Functional analogy between lipoprotein(a) and plasminogen in the binding to the kringle 4 binding protein, tetranectin.
Apolipoprotein(a), apo(a), contains 37 repeats structurally homologous to kringle 4 structures of the fibrinolysis zymogen plasminogen. The aim of the study was to explore the functional analogy between apolipoprotein(a) and plasminogen in the binding to the kringle-4-binding plasma protein, tetranectin. With a modified crossed immunoelectrophoresis technique, reversible binding between lipoprotein(a) and tetranectin could be demonstrated with an apparent Kd of 0.013 muMol/l. Lys- and Glu-plasminogen showed an apparent Kd of 0.5 muMol/l. Binding of lipoprotein(a) to fibrin and to fibrin-bound tetranectin was found to be negligible. The absence of fibrin binding of lipoprotein(a) excludes a potential mechanism of coexistence of fibrin and lipid deposits in arterial diseases and does not provide for a link between lipoprotein and the clotting system. Plasminogen and lipoprotein(a) show functional analogy in their binding to tetranectin, but tetranectin primarily targets at lipoprotein(a).
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Gaubius Institute TNO, Leiden, The Netherlands.
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Havekes
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D001798:Blood Proteins / Q000378:metabolism*; D005337:Fibrin / Q000378:metabolism; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D066298:In Vitro Techniques; D037181:Lectins, C-Type; D017270:Lipoprotein(a); D008074:Lipoproteins / Q000378:metabolism* / Q000648:ultrastructure; D008077:Lipoproteins, LDL / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D012995:Solubility; D013329:Structure-Activity Relationship
D001798:Blood Proteins; D037181:Lectins, C-Type; D017270:Lipoprotein(a); D008074:Lipoproteins; D008077:Lipoproteins, LDL; C048648:tetranectin; D005337:Fibrin; D010958:Plasminogen