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Journal ArticleDOI

Suppression of inflammatory responses by surfactin, a selective inhibitor of platelet cytosolic phospholipase A2.

TLDR
In this paper, a linear regression analysis of the linear portion of a concentration response curve reveals an IC50 of 8.5 microM with an inhibition constant of Ki = 4.7 microM in 50 mM Tris-HCl buffer.
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This article is published in Biochemical Pharmacology.The article was published on 1998-04-01. It has received 88 citations till now. The article focuses on the topics: Surfactin & Phospholipase A2.

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Citations
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Journal ArticleDOI

Biosurfactants: potential applications in medicine

TL;DR: Biosurfactants utility as suitable anti-adhesive coating agents for medical insertional materials leading to a reduction in a large number of hospital infections without the use of synthetic drugs and chemicals is indicated.
Journal ArticleDOI

Potential applications of microbial surfactants in biomedical sciences

TL;DR: Some of the new and exciting applications and related developments of various microbial surfactants in the field of biomedical sciences are discussed.
Journal ArticleDOI

Review of surfactin chemical properties and the potential biomedical applications

TL;DR: 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.
Journal ArticleDOI

Lipopeptides: from self-assembly to bioactivity.

TL;DR: Several classes of lipopeptide with important biomedical applications as antimicrobial and antifungal agents, in immune therapies and in personal care applications among others are discussed, with a particular focus on self-assembly.
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Biological activity of lipopeptides from Bacillus

TL;DR: Understanding the natural function of these structurally diverse lipopeptides in Bacillus provides insight into microbial regulatory programs and is required for efficient development of more effective products.
References
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Journal ArticleDOI

cPLA2 is phosphorylated and activated by MAP kinase.

TL;DR: Treatment of cells with agents that stimulate the release of arachidonic acid causes increased serine phosphorylation and activation of cytosolic phospholipase A2 (cPLA2).
Journal ArticleDOI

A novel arachidonic acid-selective cytosolic PLA2 contains a Ca2+-dependent translocation domain with homology to PKC and GAP

TL;DR: The cloning and expression of a cDNA encoding a high molecular weight cytosolic phospholipase A2 (cPLA2) that has no detectable sequence homology with the secreted forms of PLA2 is reported and it is demonstrated that cPLA2 selectively cleaves arachidonic acid from natural membrane vesicles and translocates to membrane vESicles in response to physiologically relevant changes in free calcium.
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