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Literature summary for 3.4.21.68 extracted from

  • Longstaff, C.; Thelwell, C.; Williams, S.C.; Silva, M.M.; Szabo, L.; Kolev, K.
    The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies (2011), Blood, 117, 661-668.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens both plasminogen activation and fibrin lysis by tPA. Lysis of fibrin clots performed using confocal microscopy in conjunction with tPA-GFP added to clots formed of fibrin100 and fibrin5. The front of the fibrin clot moves faster in fibrin5 than in fibrin100. There are also morphologic differences that develop in the 2 fibrins as indicated by the pattern of fluorescence, which reflects tPA distribution. Specifically, it can be seen that a granular pattern develops in the fibrin5 lysis series in contrast to the homogeneous fluorescence pattern that is maintained in the fibrin100 series. Binding analysis of tPA to aggregates formed in fibrin5, using orange fluorescent fibrinogen converted to fluorescent fibrin100 and fibrin5 ?
-
 ?
plasminogen + H2O Homo sapiens
-
 plasmin + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information tPA is strongly associated with agglomerates. Fine fibrin is a better surface for plasminogen activation but more resistant to lysis Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information both plasminogen activation and fibrin lysis by tPA. Lysis of fibrin clots performed using confocal microscopy in conjunction with tPA-GFP added to clots formed of fibrin100 and fibrin5. The front of the fibrin clot moves faster in fibrin5 than in fibrin100. There are also morphologic differences that develop in the 2 fibrins as indicated by the pattern of fluorescence, which reflects tPA distribution. Specifically, it can be seen that a granular pattern develops in the fibrin5 lysis series in contrast to the homogeneous fluorescence pattern that is maintained in the fibrin100 series. Binding analysis of tPA to aggregates formed in fibrin5, using orange fluorescent fibrinogen converted to fluorescent fibrin100 and fibrin5 Homo sapiens ?
-
 ?
plasminogen + H2O
-
 Homo sapiens plasmin + ?
-
 ?

Synonyms

Synonyms Comment Organism
Tissue-type plasminogen activator
-
 Homo sapiens
tPA
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Homo sapiens

General Information

General Information Comment Organism
physiological function the interplay between tissue plasminogen activator domains and fibrin structures plays a role in the regulation of fibrinolysis, kinetics, overview. The regulation of fibrinolysis depends on the starting nature of fibrin fibers and complex dynamic interaction between tPA and fibrin structures that vary over time. Fine fibrin is a better surface for plasminogen activation but more resistant to lysis Homo sapiens