## Abstract Plasminogen activator secretion by 39 primary or earlyβpassage cultures of malignant human neoplasms has been compared with that of 16 similar cultures of benign neoplasms and 39 cultures of normal or reactive tissue. While normal cells of mesenchymal or neural origin secreted considera
Plasminogen activator content of neoplastic and benign human prostate tissues; fibrin augmentation of an activator activity
β Scribed by S. M. Camiolo; G. Markus; J. L. Evers; H. Hobika; J. L. Depasquale; S. Beckley; J. P. Grimaldi
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- French
- Weight
- 732 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0020-7136
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β¦ Synopsis
Abstract
The plasminogen activator content of the extracts of excised prostate cancers (25 specimens) was determined with an azocasein assay and found to be on the average 1.7 times higher than that of extracts of excised prostate benign hyperplasias (29 specimens). Both groups contained the same average percentage of human urokinase type activator (βΌ45%) as determined by the inhibition of activity when antiβhuman urokinase antibody was included in the assay system. The two types of activators were partially purified and found to have distinctly different properties. The most striking difference was the large augmentation of activity of the nonβurokinase enzyme in fibrinolysis. The implications of an enhanced fibrinolysis relative to azocaseinolysis (or other) is discussed, particularly with respect to its importance in the quantitation and characterization of activators by different investigators. Highly purified urokinaseβlike activator was found to be similar to commercial urokinase preparation with respect to molecular weight, isoelectric point, inhibition by the antibody, and inhibition by placenta inhibitor.
π SIMILAR VOLUMES
Molecular assembly of plasminogen and tissue-type plasminogen actwator (t-PA) at the surface of fibrin results in the generation of fibrin-bound plasmin and thereby in the dissolution of a clot. This mechanism is triggered by specific interactions of intra-chain surface lysine residues in fibrin wit