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      Complex Intracellular Structures in Prokaryotes 

      Magnetosomes in Magnetotactic Bacteria

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      Springer Berlin Heidelberg

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          Genomic islands in pathogenic and environmental microorganisms.

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            Magnetosome formation in prokaryotes.

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              The extra domain A of fibronectin activates Toll-like receptor 4.

              Cellular fibronectin, which contains an alternatively spliced exon encoding type III repeat extra domain A (EDA), is produced in response to tissue injury. Fragments of fibronectin have been implicated in physiological and pathological processes, especially tissue remodeling associated with inflammation. Because EDA-containing fibronectin fragments produce cellular responses similar to those provoked by bacterial lipopolysaccharide (LPS), we examined the ability of recombinant EDA to activate Toll-like receptor 4 (TLR4), the signaling receptor stimulated by LPS. We found that recombinant EDA, but not other recombinant fibronectin domains, activates human TLR4 expressed in a cell type (HEK 293 cells) that normally lacks this Toll-like receptor. EDA stimulation of TLR4 was dependent upon co-expression of MD-2, a TLR4 accessory protein. Unlike LPS, the activity of EDA was heat-sensitive and persisted in the presence of the LPS-binding antibiotic polymyxin B and a potent LPS antagonist, E5564, which completely suppressed LPS activation of TLR4. These observations provided a mechanism by which EDA-containing fibronectin fragments promote expression of genes involved in the inflammatory response.
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                Book Chapter
                2006
                June 13 2006
                : 167-191
                10.1007/7171_024
                015d1941-7e08-4adb-a4d6-b11a4d9b1578
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