Lysis of surface-localized fibrin clots by adsorbed plasminogen in the presence of tissue plasminogen activator.
The ability of plasminogen adsorbed from buffer onto sulphonated silica glass or lysine-derivatized silica glass to lyse fibrin I clots has been investigated. Clots were formed around the test surface by adding reptilase to fibrinogen solutions in which the surfaces were immersed. Tissue plasminogen activator (t-PA) was then added and the extent of clot lysis was determined by measuring the levels of the specific plasmin cleavage product of fibrinogen, B beta 1-42 peptide. The data indicate that in the presence of t-PA, B beta 1-42 generation per mole of bound plasminogen on the lysinized material is approximately two-fold higher than on the sulphonated material. It is concluded that a preformed clot may be lysed by adsorbed plasminogen in the presence of t-PA, and that clot lysis is significantly enhanced when the plasminogen is adsorbed via its lysine binding sites.
Woodhouse
K A
KA
Department of Chemical Engineering, McMaster University, Hamilton, Ontario, Canada.
Weitz
J I
JI
Brash
J L
JL
D000327:Adsorption; D005337:Fibrin / Q000378:metabolism*; D005898:Glass / Q000737:chemistry; D008239:Lysine / Q000737:chemistry; D010958:Plasminogen / Q000494:pharmacology*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D017640:Silicates / Q000737:chemistry; D013499:Surface Properties; D010959:Tissue Plasminogen Activator / Q000494:pharmacology*
D011956:Receptors, Cell Surface; D017640:Silicates; D005337:Fibrin; D010958:Plasminogen; C067262:PLAT protein, human; D010959:Tissue Plasminogen Activator; D008239:Lysine