PMID: 6403038Mar 30, 1983Paper

A critical role of lysine residues in the stimulation of tissue plasminogen activator by denatured proteins and fibrin clots

Biochimica Et Biophysica Acta
R Radcliffe

Abstract

Two-chain 70 000-dalton plasminogen activator of tissue origin displays only weak activity toward plasminogen in a two-component system. The rate of activation is enhanced a minimum of 50-fold by the presence of fibrin clots or denatured proteins. The stimulation must depend on both chemical determinants and spatial configuration, since native proteins, including fibrinogen, lack significant stimulatory activity. These studies employed chemical modifications of four stimulatory proteins (fibrin, denatured fibrinogen, denatured IgG and denatured ovalbumin) to identify a critical role for lysine residues. Arginine, aspartic acid, cysteine, cystine, glutamic acid, histidine, methionine, tyrosine and tryptophan were found not to be essential. The critical spatial determinant(s) remain(s) unknown.

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Citations

Oct 1, 1991·Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research·G LeloupG Vaes
Jan 1, 1986·Critical Reviews in Oncology/hematology·D Collen, H R Lijnen
Jan 28, 2006·Biochemical and Biophysical Research Communications·Rita GalántaiRaymund Machovich
Aug 15, 1997·Archives of Biochemistry and Biophysics·R Machovich, W G Owen

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