Fibrinolytic Bacterial Enzymes with Thrombolytic Activity (SpringerBriefs in Microbiology)

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Fibrinolytic Bacterial Enzymes with Thrombolytic Activity

Item s unavailable for purchase. Please review your cart. It is derived from its soluble protein precursor, fibrinogen. Fibrin is laid down inside blood vessels that have been compromised by disease or injury. Fibrin forms minuscule strands that eventually dry and harden, capturing blood vessel components effectively.

Certainly, fibrin occupies a vital role in health and healing; however, fibrin may also be responsible for an overzealous propensity to form inappropriate clots in the body. Inappropriate clotting, of course, is a major risk factor for myocardial infarction and stroke. When correctly balanced, deposition and removal of fibrin maintains avoidance of blood loss and adverse viscosity in the vascular system.

A balance tipped in favor of fibrin overproduction leads to dangerous clotting. Various types of thrombosis are responsible for an increasing number of deaths each year. In the USA alone, lung blood clots affect an estimated 1,, patients annually Lopez-Sendon et al. The formation of a blood clot in a blood vessel intravascular thrombosis is one of the main causes of CVDs. Meanwhile, fibrin clots can be hydrolyzed by plasmin to avoid thrombosis in blood vessels. In an unbalanced situation due to some disorders, the clots are not hydrolyzed, and thus thrombosis occurs Lopez-Sendon et al.

So, several investigations are being pursued to enhance the efficacy and spec- ificity of fibrinolytic therapy, and microbial fibrinolytic enzymes have attracted much more medical interest in recent decades Goldhaber and Bounameaux ; Tough Based on their different working mechanisms, thrombolytic agents are classi- fied into two types. One is plasminogen activators, such as tissue-type plasmino- gen activator t-PA Collen and Lijnen and urokinase Duffy , which activate plasminogen into active plasmin to degrade fibrin. The other type is plasmin-like proteins, which directly degrade fibrin, thereby dissolving thrombi rapidly and completely.

Although plasminogen activators and urokinase are still widely used in thrombolytic therapy today, their expensive prices and undesirable side-effects, such as the risk for internal hemorrhage within the intestinal tract when orally administrated, have prompted researchers to search for cheaper and safer resources Ismail ; Nakajima et al. Therefore, microbial fibrinolytic enzymes have also attracted much more medical interest during recent decades Bode et al.

Fibrinolytic enzymes were successively discovered from different microor- ganisms, the most important among which is the genus Bacillus from traditional fermented foods Mine et al. The physiochemical properties of these enzymes have been characterized, and their effectiveness in thrombolysis in vivo has been further identified. Therefore, microbial fibrinolytic enzymes, especially those from food-grade microorganisms, have potential to be developed as functional food additives and drugs to prevent or cure thrombosis and other related diseases Ambrus et al.

Fibrinolytic enzymes are mainly proteases. These catalyze total hydrolysis of proteins and specifically act on interior peptide bonds Bayoudh et al. All living cells produce different types of proteases, but the majority are pro- duced by microorganisms. Many workers have reported that bacteria are high protease producers Kalisz Proteases are grossly subdivided into two major groups, namely exopeptidases and endopeptidases, depending on their site of action.

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Exopeptidases cleave the peptide bond proximal to the amino or carboxy termini of the substrate, whereas endopeptidases cleave peptide bonds distant from the termini of the substrate International Union of Biochemistry and Molecular Biology Based on the functional group present at the active site, proteases are further classified into four families: Fibrinolytic proteases are mainly serine or metalloproteases Sharma et al.

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