Title
Substrate specificity of tissue-type and urokinase-type plasminogen activators
Author
Rijken, D.C.
Groeneveld, E.
Gaubius Instituut TNO
Publication year
1991
Abstract
Recent studies suggest that plasminogen activators not only hydrolyse a specific arginine-valine bond in plasminogen, but may also cleave other proteins such as fibronectin. We studied the substrate specificity, particularly the preference for arginyl over lysyl peptide bonds, of tissue-type plasminogen activator (t-PA) as well as of two-chain urokinase-type plasminogen activator (u-PA). The arginine/lysine preference was determined with three pairs of tripeptidyl-p-nitroanilide substrates having either arginine or lysine in the P1 position and varied from 5.2 to 14.1 for u-PA and from 55.6 to 99.8 for t-PA. It was concluded that both t-PA and u-PA preferred arginyl to lysyl peptide bonds. However, u-PA had a significantly lower arginine/lysine preference than t-PA, indicating that u-PA represents a less specific proteinase. This may point to functions of u-PA other than plasminogen activation, which involve cleavage of lysyl bonds.
Subject
Biology
Amino Acid Sequence
Binding Sites
Cells, Cultured
Enzyme Precursors
Human
Hydrogen-Ion Concentration
Kidney
Kinetics
Melanoma
Molecular Sequence Data
Plasminogen Activators
Substrate Specificity
Support, Non-U.S. Gov't
Tissue Plasminogen Activator
Tumor Cells, Cultured
Urinary Plasminogen Activator
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TNO identifier
231514
ISSN
0006-291X
Source
Biochemical and Biophysical Research Communications, 174 (2), 432-438
Document type
article