Enzyme systems: better reception for urokinase

Article Abstract:

Fibrinolytic agents have achieved wide recognition for their therapeutic application to dissolving clots and the reduction of mortality related to acute myocardial infarction. In general, this action involves the activation of serum plasminogen by enzymes such as plasminogen activator or urokinase. However, these enzymes play a role in other processes as well, including tissue remodelling and the migration of both normal and cancerous cells. Until recently, the relationship between the concentration of these enzymes and their activity was poorly understood, but now it is recognized that plasminogen activator binds plasminogen much more effectively when the activator has bound to fibrin, a major protein component of clots. The activation, therefore, tends to occur precisely where it is needed. Now it has been found that many cells possess urokinase receptors on their surface. The human urokinase receptor has now been cloned, and it appears to be a unique protein sharing little or no sequence homology with other receptors. The cloning of this receptor will aid in the elucidation of the process by which cells regulate urokinase activity and control the enzymatic digestion of their immediate surroundings. (Consumer Summary produced by Reliance Medical Information, Inc.)

Editorial, Cell receptors, Fibrinolytic agents, Thrombolytic drugs, Urokinase

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A human RNA polymerase II complex associated with SRB and DNA-repair proteins

Article Abstract:

A human polymerase II (RNAPII) complex isolated by chromatography contains transcriptional coactivators and the human homologues of the yeast suppressors of RNA polymerase B proteins. The complex stimulates transcription and a part of it is involved in DNA repair. The amount of transcription factors (TF) IIE and TFIIF is similar to that of the RNAPII subunits, while TFIIH is present in smaller amounts. The relative molecular mass of the complex is about 2000K.

Physiological aspects, RNA polymerases

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Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity

Article Abstract:

Virion proteinase activity of human adenovirus (Ad2) was analyzed in vitro using fluorogenic substrate. Proteinase activity, necessary for the virus to produce infectious particles, has three cofactors: recombinant endoprotease protein; a peptide made up of 11 amino acids; and adenovirus DNA. This is the first time that viral DNA has been found to be involved in proteinase activity.

Proteases, Peptides, Adenoviruses, Human, Human adenoviruses, Viral genetics

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