The Detection and Differentiation of Fibrinolytic Enzymes in Bacteria

Jeffries, Leonard

doi:10.1111/j.1365-2672.1980.tb04723.x

Cited by 15 publications

(15 citation statements)

References 13 publications

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“…Instead, we chose to incorporate an actively growing bacterial culture in the fibrin clot. This approach is similar to the one described by Jeffries and Buckley [5], who used a sus pension of bacteria in nutrient broth.…”

Section: Discussionmentioning

confidence: 99%

Bacterial Lysis of Fibrin Seal in vitro

Hoffmann

Moesgaard²

1988

Eur Surg Res

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We performed an in vitro study to determine whether certain bacteria may lyse a commercially available fibrin seal (Beriplast®, Behringwerke, Marburg, FRG). Fibrinogen solution was mixed with actively growing bacterial cultures, and thrombin was added. During 20 days of incubation at 37 °C complete lysis was observed with a number of different bacteria, however, at different rates. Complete lysis within 1–5 days was observed for the following species (number of strains in parentheses): Streptococcus faecalis (3), Pseudomonas aeruginosa (2), Serratia marcescens (2), and Serratia liquefaciens (1). Lysis was observed after 6–10 days for Enterobacter cloacae (2), Morganella morganii (2), Escherichia coli (2), S. marcescens (1), and Klebsiella pneumoniae (2). Lysis after 11–16 days was observed for Streptococcus pyogenes (2), S. faecalis (2), and Staphylococcus aureus (2). Rapid lysis was associated with the ability of the strain to liquefy gelatin, i.e. the production of a protease.

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Section: Discussionmentioning

confidence: 99%

Bacterial Lysis of Fibrin Seal in vitro

Hoffmann

Moesgaard²

1988

Eur Surg Res

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“…Microorganisms like bacteria exhibit fibrinolytic activity [30,53]. For fibrin-trapped bacteria, it may be useful to initiate tissue invasion.…”

Section: Fibrinolytic Activity In Cancer Cellsmentioning

confidence: 99%

Fibrinolytic mechanisms in tumor growth and spreading

Südhoff

Schneider

1992

Clin Investig

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The high prevalence of hypercoagulative states in cancer patients has been known for more than a century. Venous thrombosis in gastric cancer was described by Trousseau in 1865 [55]. In 1878, Billroth observed intravascular thrombus formation in association with metastasis [4]. Thrombohemorrhagic complications regularly occur in patients with disseminated malignancy and are related to an increase in fibrinogen and fibrin turnover. During the past decade, clinicians have witnessed considerable advances in the understanding of fibrinolysis. Initially centered on the role as part of a dynamic, hemostatic balance, research began to unravel the pathophysiological contribution of fibrinolysis to tumor progression. The mechanisms of tumor invasion and metastasis formation in cancer are of critical importance, since metastasis is the major cause of treatment failure and death. It has been suggested that cell-associated proteolytic enzymes contribute to tumor aggressiveness [11, 22, 23]. Fibrinolytic mechanisms are involved in a number of physiological processes in which tissue degradation and remodeling occurs. These include disruption of the ovarian follicle during ovulation and blastocyst implantation. These events in part resemble the invasive growth of cancer [37, 47]. Inspired by this hypothesis, the role of fibrinolytic processes in tumor invasion is under intensive study.

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“…clavuligerus produces exocellular proteases (8,27). An exocellular protease could give the appearance of 3-lactamase inhibition in an enzyme-based assay by causing proteolytic degradation of the P-lactamase.…”

Section: I8-lactamase Inhibition Assays (I) Agar Diffusion Bioassaymentioning

confidence: 99%

“…Protease activity was monitored with azocasein as substrate as previously described (29). Fibrinolytic activity was measured with the specific plasmin substrate D-valyl-L-leucyl-L-lysine-p-nitroanilide dihydrochloride as described by Jeffries and Buckley (27).…”

Section: I8-lactamase Inhibition Assays (I) Agar Diffusion Bioassaymentioning

confidence: 99%

“…Protein contents of BLIP and ,3-lactamase preparations were measured by the dye-binding assay of Bradford (7) 27,000 x g, and the supernatant was used as a source of crude 13-lactamase. This 3-lactamase preparation showed cephalosporinase activity predominantly and is presumed to be the product of the chromosomal ampC gene (26).…”

Section: I8-lactamase Inhibition Assays (I) Agar Diffusion Bioassaymentioning

confidence: 99%

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Isolation and characterization of a beta-lactamase-inhibitory protein from Streptomyces clavuligerus and cloning and analysis of the corresponding gene

et al. 1990

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,B-Lactam compounds account for more than 60% of worldwide consumption of antibiotics as a result of the high selectivity, low toxicity, and versatility of these compounds. However, the chemotherapeutic application of ,-lactam antibiotics has been continually threatened by the development of bacterial resistance. The most common mechanism of resistance among both gram-positive and gram-negative bacteria involves the production of 3-lactamases, enzymes which cleave the p-lactam ring. The fact that some ,Blactamases are encoded on transferable plasmids or transposable elements has contributed substantially to the incidence of clinically significant P-lactam resistance (12). While chemical modification has helped to improve the resistance of the naturally occurring P-lactam antibiotics to cleavage, the need for further improvement resulted in an effort to find useful ,-lactamase inhibitors. Several effective, mechanismbased, low-molecular-weight P-lactamase inhibitors have been developed, but only clavulanic acid, a clavam-type P-lactam compound, has been used clinically (33). Clavulanic acid is one of several P-lactam compounds produced by Streptomyces clavuligerus, a filamentous gram-positive bacterium which also produces penicillin N, desacetoxycephalosporin C, and cephamycin C (28). The significance of the production of ,-lactamase inhibitors to S. clavuligerus is unclear, but this is also true of the production of ,-lactam antibiotics. No consensus exists as to how antibiotic-producing organisms benefit from the production of antibiotics (1,14). Although the majority of Streptomyces species produce ,-lactamases (43) (Preliminary results of this study were presented at the

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The Detection and Differentiation of Fibrinolytic Enzymes in Bacteria

Cited by 15 publications

References 13 publications

Bacterial Lysis of Fibrin Seal in vitro

Bacterial Lysis of Fibrin Seal in vitro

Fibrinolytic mechanisms in tumor growth and spreading

Isolation and characterization of a beta-lactamase-inhibitory protein from Streptomyces clavuligerus and cloning and analysis of the corresponding gene

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