Suppression of Inflammatory Responses by Surfactin, 11Surfactin was formerly referred to as PI-003. a Selective Inhibitor of Platelet Cytosolic Phospholipase A2

Kim, KwangPyo; Jung, Sung Yun; Lee, Duk Keun; Jung, Jae‐Kyung; Park, Jong Koo; Kim, Dae Kyong; Lee, Chul-Hoon

doi:10.1016/s0006-2952(97)00613-8

Cited by 89 publications

(49 citation statements)

References 34 publications

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“…As mentioned above, surfactin is a known inhibitor of PLA 2 . Surfactin inhibited cytosolic PLA 2 purified from bovine platelets with an IC 50 of 8.5 mM (8.8 mg/ml) [27]. PLA 2 was reported to be activated by inflammatory stimuli such as LPS in endothelial cells, and activated PLA 2 was shown to lead to increased leukemic cell adhesion via the expression of adhesion molecules [30].…”

Section: Discussionmentioning

confidence: 99%

“…It is an amphiphilic compound and known to be one of the most powerful biosurfactants [22,26]. Surfactin was also reported to inhibit phospholipase A 2 (PLA 2 ) [27], and to enhance plasminogen activation [28]. In addition, it is less toxic than other surfactants as judged from the results of an acute toxicity study in mice (LD 50 value at Ͼ100 mg/kg, i.v.)…”

Section: Discussionmentioning

confidence: 99%

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Inhibition of Lipopolysaccharide Activity by a Bacterial Cyclic Lipopeptide Surfactin

et al. 2006

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Compounds that inactivate lipopolysaccharide (LPS) activity have the potential of being new antiinflammatory agents. Therefore, we searched among microbial secondary metabolites for compounds that inhibited LPS-stimulated adhesion between human umbilical vein endothelial cells (HUVEC) and HL-60 cells. By this screening, we found a cyclic lipopeptide surfactin from the culture broth of Bacillus sp. BML752-121F2 to be inhibitory. The addition of the surfactin prior to the LPS stimulation decreased HL-60 cell-HUVEC adhesion without showing any cytotoxicity. We confirmed that surfactin inhibited LPS-induced expression of ICAM-1 and VCAM-1 in HUVEC. It also inhibited the cellular adhesion induced by lipid A, the active component of LPS; but it did not inhibit TNF-a or IL-1b -induced cell adhesion. Then, surfactin was shown to suppress the interaction of lipid A with LPS-binding protein (LBP) that mediates the transport of LPS to its receptors. Finally, surface plasmon resonance (SPR) analysis revealed the surfactin to interact reversibly with lipid A. Thus, this Bacillus surfactin was shown to be an inhibitor of LPS-induced signal transduction, directly interacting with LPS.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Inhibition of Lipopolysaccharide Activity by a Bacterial Cyclic Lipopeptide Surfactin

et al. 2006

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“…Besides its antifungal and antibacterial effect [31], surfactin can also inhibit fibrin clot formation [5], induces the formation of ion channels in lipid bilayer membranes [54], blocks the activity of cyclic adenosine monophosphate [32], inhibits platelet and spleen cytosolic phospholipase A2 (PLA2) [55] and exhibits antiviral [56] and antitumor activities [57].…”

Section: Potential Applications Of Surfactinsmentioning

confidence: 99%

Review of surfactin chemical properties and the potential biomedical applications

2008

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AbstractSurfactin, a highly powerful biosurfactant produced by various strains of the genus Bacillus, exhibits antibacterial, antiviral, antitumor and hemolytic action. This anionic cyclic lipopeptide is constituted by a heptapeptide interlinked with a β-hydroxy fatty acid. Due to its amhipathic nature surfactin incorporates into the phospholipid bilayer and induces permeabilization and perturbation of target cells. The rising antibiotic resistance as well as a number of remarkable surfactin activities shows that it deserves special interest and is considered as a candidate compound for combating several health related issues. In this review, the current state of knowledge of surfactin properties, biomedical potential and limitations for its application is presented.

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“…Surfactin exhibits a wide range of interactions with target cell membranes and has potential for various medical applications. Besides its antifungal and antibacterial effects (Thimon et al, 1992), surfactin can also inhibit fibrin clot formation (Arima et al, 1968), inhibits platelet and spleen cytosolic phospholipase A2 (PLA2) (Kim et al, 1998) and exhibits antiviral (Kracht et al, 1999) and antitumor activities (Kameda et al, 1974). Another interesting property of surfactin is that high surfactin concentration affects the aggregation of amyloid ǐ-peptide (Aǐ (1-40)) into fibrils, a key pathological process associated with Alzheimer's disease (Han et al, 2008).…”

Section: Potential Biomedical Applicationsmentioning

confidence: 99%

Surfactin - Novel Solutions for Global Issues

Seydlová¹,

Čabala²,

Svobodová³

2011

Biomedical Engineering, Trends, Research and Technologies

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Suppression of Inflammatory Responses by Surfactin, 11Surfactin was formerly referred to as PI-003. a Selective Inhibitor of Platelet Cytosolic Phospholipase A2

Cited by 89 publications

References 34 publications

Inhibition of Lipopolysaccharide Activity by a Bacterial Cyclic Lipopeptide Surfactin

Inhibition of Lipopolysaccharide Activity by a Bacterial Cyclic Lipopeptide Surfactin

Review of surfactin chemical properties and the potential biomedical applications

Surfactin - Novel Solutions for Global Issues

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