@article{mbs:/content/journal/micro/10.1099/mic.0.2008/017095-0, author = "Candela, Marco and Miccoli, Giacomo and Bergmann, Simone and Turroni, Silvia and Vitali, Beatrice and Hammerschmidt, Sven and Brigidi, Patrizia", title = "Plasminogen-dependent proteolytic activity in Bifidobacterium lactis", journal= "Microbiology", year = "2008", volume = "154", number = "8", pages = "2457-2462", doi = "https://doi.org/10.1099/mic.0.2008/017095-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.2008/017095-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "uPA, urokinase", keywords = "GIT, gastrointestinal tract", keywords = "Fn, fibronectin", keywords = "tPA, tissue-type PA", keywords = "EACA, ϵ-aminocaproic acid", keywords = "ECM, extracellular matrix", keywords = "PA, plasminogen activator", keywords = "Plg, plasminogen", keywords = "Fg, fibrinogen", abstract = "Bifidobacteria represent one of the most important health-promoting bacterial groups of the intestinal microbiota. The binding of plasminogen to species of Bifidobacterium has been recently reported. To further explore the interaction between bifidobacteria and plasminogen, we investigated the role of Bifidobacterium lactis BI07 plasminogen-dependent proteolytic activity in the degradation of host-specific substrates. Our experimental data demonstrate that the recruitment of plasminogen on the bacterial cell surface and its subsequent conversion into plasmin by host-derived plasminogen activators provide B. lactis BI07 with a surface-associated plasmin activity effective in degradation of physiological substrates such as extracellular matrix, fibronectin and fibrinogen. The ability of bifidobacteria to intervene in the host plasminogen/plasmin system may contribute to facilitating colonization of the host gastrointestinal tract.", }