Protease cellular

Langer T. AAA proteases Cellular machines for degrading membrane prorans. Trends Biochem Sci... 

These serine and cysteine protease cellular pathways are both preferentially targeted by virus-engineered serpins which are now known to block protease activity in the thrombotic/thrombolytic and apoptotic pathways and exhibit amazingly potent anti-inflammatory activities. 

FIGURE 16.28 HIV mRNA provides the genetic information for synthesis of a polyprotein. Proteolytic cleavage of this polyprotein by HIV protease produces the individnal proteins required for viral growth and cellular infection. 

Apoptotic executioner caspases (caspase-3, -6, -7) constitute a subgroup of the caspase family. These proteases are the workhorses of the apoptotic process as they are responsible for cleaving many down-stream substrates important for cellular morphology, organelle homeostasis, cell cycle arrest, and regulation of transcription and translation. 

In higher organisms, calpain superfamily contains 16 independent genes that modulate cellular function. Out of them, 14 are Ca2+-dependent cysteine proteases. The other two encode smaller regulatory proteins that... 

Fibrinolytic enzymes (proteases) are used to dissolve thrombus, the insoluble aggregate of fibrin and platelet including several additional cellular and molecular components of the blood. 

Enzymology of proteases in a water-phase is well known, but its alteration in a compartment is poorly understood. There are dramatical changes in reaction rates, in enzyme contractions and in enzyme sensitivity to inhibitors, which are not exactly described. In addition, besides fibrin and platelets there are several cellular and molecular components present in a thrombus compartment, where their influence on the basic fibrinolytic reactions is not known. To study this aspect of fibrinolysis is a task of the near future [4]. 

The serine proteases are the most extensively studied class of enzymes. These enzymes are characterized by the presence of a unique serine amino acid. Two major evolutionary families are presented in this class. The bacterial protease subtilisin and the trypsin family, which includes the enzymes trypsin, chymotrypsin, elastase as well as thrombin, plasmin, and others involved in a diverse range of cellular functions including digestion, blood clotting, hormone production, and complement activation. The trypsin family catalyzes the reaction ... 

With the death of the bean, cellular structure is lost, allowing the mixing of water-soluble components that normally would not come into contact with each other. The complex chemistry that occurs during fermentation is not fully understood, but certain cocoa enzymes such as glycosidase, protease, and polyphenol oxidase are active. In general, proteins are hydrolyzed to smaller proteins and amino acids, complex glycosides are split, polyphenols are partially transformed, sugars are hydrolyzed, volatile acids are formed, and purine alkaloids diffuse into the bean shell. The chemical composition of both unfermented and fermented cocoa beans is compared in Table 1. 

Baker J. B Low D. A., Simmer R. L. Protease nexin A cellular component that links thrombin and plasminogen activator and mediates their binding to cells. Cell 1980 21, 37-45. 

Prion diseases resulting in encephalopathy can be transmitted between individuals within species (more rarely between species) [26-28], A conformational variant of the normal cellular protein PrPs (PrPc) (protease-sensitive or cellular) is believed to catalyze [29] or nucleate [30-33] conversion to the pathological form, PrPR (protease-resistant). This highly unusual nongenetic mode of transmission of an infectious agent has been strongly debated [29]. The observation of multiple examples of nucleated catalysis of aberrant polymerization of protein subunits has... 

Saborio GP, Soto C, Kascsak RJ, Levy E, Kascsak R, Harris DA, Frangione B. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem Biophys Res Commun 1999 258 470-475. 

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