منابع مشابه
Perforin-2/Mpeg1 and other pore-forming proteins throughout evolution.
Development of the ancient innate immune system required not only a mechanism to recognize foreign organisms from self but also to destroy them. Pore-forming proteins containing the membrane attack complex Perforin domain were one of the first triumphs of an innate immune system needing to eliminate microbes and virally infected cells. Membrane attack complex of complement and Perforin domain p...
متن کاملThe membrane attack complex, perforin and cholesterol-dependent cytolysin superfamily of pore-forming proteins.
The membrane attack complex and perforin proteins (MACPFs) and bacterial cholesterol-dependent cytolysins (CDCs) are two branches of a large and diverse superfamily of pore-forming proteins that function in immunity and pathogenesis. During pore formation, soluble monomers assemble into large transmembrane pores through conformational transitions that involve extrusion and refolding of two α-he...
متن کاملDiarylthiophenes as inhibitors of the pore-forming protein perforin
Evolution from a furan-containing high-throughput screen (HTS) hit (1) resulted in isobenzofuran-1(3H)-one (2) as a potent inhibitor of the function of both isolated perforin protein and perforin delivered in situ by intact KHYG-1 NK cells. In the current study, structure-activity relationship (SAR) development towards a novel series of diarylthiophene analogues has continued through the use of...
متن کاملDissociation of membrane binding and lytic activities of the lymphocyte pore-forming protein (perforin)
Granules isolated from CTL and NK cells contain a cytolytic pore-forming protein (PFP/perforin). At low temperatures (on ice), PFP binds to erythrocyte membranes without producing hemolysis. Hemolysis occurs when the PFP-bound erythrocytes are warmed up to 37 degrees C, which defines a temperature-dependent, lytic (pore-formation) step distinct from the membrane-binding event. Ca2+ and neutral ...
متن کاملEvolution of the Cytolytic Pore-Forming Proteins (Actinoporins) in Sea Anemones
Sea anemones (Cnidaria, Anthozoa, and Actiniaria) use toxic peptides to incapacitate and immobilize prey and to deter potential predators. Their toxin arsenal is complex, targeting a variety of functionally important protein complexes and macromolecules involved in cellular homeostasis. Among these, actinoporins are one of the better characterized toxins; these venom proteins form a pore in cel...
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ژورنال
عنوان ژورنال: Journal of Leukocyte Biology
سال: 2015
ISSN: 0741-5400
DOI: 10.1189/jlb.4mr1114-523rr