fibrin and staplabin
fibrin has been researched along with staplabin* in 3 studies
Other Studies
3 other study(ies) available for fibrin and staplabin
| Article | Year |
|---|---|
Isolation of SMTP-3, 4, 5 and -6, novel analogs of staplabin, and their effects on plasminogen activation and fibrinolysis.
Four novel triprenyl phenol metabolites, designated SMTP-3, -4, -5, and -6, have been isolated from cultures of Stachybotrys microspora IFO 30018 by solvent extraction and successive chromatographic fractionation using silica gel and silica ODS columns. A combination of spectroscopic analyses showed that SMTP-3, -4, -5, and -6 are staplabin analogs, containing a serine, a phenylalanine, a leucine or a tryptophan moiety in respective molecules in place of the N-carboxybutyl portion of the staplabin molecule. SMTP-4, -5, and -6 were active at 0.15 to 0.3 mM in enhancing urokinase-catalyzed plasminogen activation and plasminogen binding to fibrin, as well as plasminogen- and urokinase-mediated fibrinolysis. On the other hand, the concentration of staplabin required to exert such effects was 0.4 to 0.6 mM, and SMTP-3 was inactive at concentrations up to 0.45 mM. Topics: Benzopyrans; Chemical Phenomena; Chemistry, Physical; Fibrin; Fibrinolysis; Fibrinolytic Agents; Humans; In Vitro Techniques; Magnetic Resonance Spectroscopy; Molecular Structure; Plasminogen; Plasminogen Activators; Protein Binding; Pyrrolidinones; Stachybotrys; Urokinase-Type Plasminogen Activator | 1998 |
Enhancement of fibrin binding and activation of plasminogen by staplabin through induction of a conformational change in plasminogen.
Staplabin (0.3-0.6 mM), a fungal triprenyl phenol, enhanced 3-fold the plasminogen activator-catalyzed activation of Glu-plasminogen and Lys-plasminogen as well as their binding to fibrin. Staplabin was not stimulatory to the amidolytic activity of plasmin and plasminogen activators. Even in the presence of epsilon-aminocaproic acid (EACA) and fibrinogen fragments, allosteric effectors for Glu-plasminogen, staplabin increased the activation of both forms of plasminogen. In size-exclusion chromatography of Glu-plasminogen and Lys-plasminogen, the molecular elution time, which varies as the conformation of a protein changes, was shortened by staplabin. These results suggest that staplabin causes plasminogens to be more susceptible to activation and fibrin binding by inducing a conformational change that is, at least in part, different from that induced by EACA and fibrinogen fragments. Topics: Allosteric Regulation; Aminocaproic Acid; Benzopyrans; Enzyme Activation; Fibrin; Fibrinogen; Fibrinolysin; Humans; Kinetics; Peptide Fragments; Plasminogen; Plasminogen Activators; Protein Conformation; Pyrrolidinones; Thrombin | 1997 |
Staplabin, a novel fungal triprenyl phenol which stimulates the binding of plasminogen to fibrin and U937 cells.
A novel triprenyl phenol, designated staplabin, has been isolated from a culture of Stachybotrys microspora IFO 30018 by solvent extraction and successive chromatographic fractionation using silica gel, Sephadex LH-20 and silica ODS columns. By a combination of spectroscopic analyses, the structure of staplabin is proposed to be 5-(2-(5,7-dihydroxy-8-methyl-8-(4,8-dimethyl-3,7-nonadienyl)-3-oxo -7, 8-dihydro-6H-pyrano[2,3-e][1,3]dihydroisoindolyl)pentanoic acid. Staplabin stimulated the binding of plasminogen, the zymogen of the fibrinolytic serine protease plasmin, to both fibrin and U937 cells. Binding was elevated 2-fold at a concentration of 0.3 approximately 0.5 mM. Topics: Benzopyrans; Cell Line; Fibrin; Humans; Iodine Radioisotopes; Plasminogen; Plasminogen Activators; Protein Binding; Pyrrolidinones; Radioligand Assay; Stachybotrys | 1996 |