Activation of fibrinolysis by SMTP-7 and -8, novel staplabin analogs with a pseudosymmetric structure.
Two novel staplabin analogs, SMTP-7 and -8, have been isolated from cultures of Stachybotrys microspora IFO 30018. Spectroscopic analyses showed that the SMTP-7 molecule consisted of two identical staplabin core structures and ornithine which bridges the two partial structures. In the SMTP-8 molecule, the bridging unit was lysine. At concentrations of 80 approximately 150 microM, the two compounds caused 2- to 12-fold increase in urokinase-catalyzed plasminogen activation, fibrin binding of plasminogen, and urokinase- and plasminogen-mediated fibrinolysis. These activities of SMTP-7 and -8 were two to ten times higher than those of staplabin and previously isolated SMTPs, which exerted such effects at concentrations ranging from 150 to 800 microM.
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Department of Applied Biological Science, Tokyo Noko University, Fuchu, Japan.
Ohyama
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Hasumi
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D001578:Benzopyrans / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D005342:Fibrinolysis; D005343:Fibrinolytic Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D015394:Molecular Structure; D010960:Plasminogen Activators / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D011760:Pyrrolidinones / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D013191:Stachybotrys / Q000254:growth & development / Q000378:metabolism*
D001578:Benzopyrans; D005343:Fibrinolytic Agents; D011760:Pyrrolidinones; C409191:SMTP 7; C409192:SMTP 8; C103026:staplabin; D010960:Plasminogen Activators