Th e CD14 gene consists of two exons which code for a single mRNA that is translated into a protein of 375 amino acids. Th e CD14 protein is composed of eleven leucin-rich repeats, which are also found in TLR and which are important in PAMP binding. Moreover, the crystal structure of CD14 revealed that the protein has a `horseshoe' shape, similar to TLR4, and that LPS is bound within the pocket [4] . In contrast to TLR, however, CD14 lacks a transmembrane domain, and thus cannot initiate intracellular signal transduction by itself. Th e CD14 protein is processed in the endoplasmatic reticu lum and expressed as a 55 kDa glycoprotein on the cell surface via a glycosylphosphatidyl (GPI) anchor [5] . Like other GPIanchored proteins, CD14 accumulates on the cell surface in microdomains known as lipid rafts, which are fairly rich in cholesterol and accumulate several kinases at the intracellular site. CD14 is expressed pre dominantly on the surface of `myeloid' cells, such as mono cytes, macrophages and neutrophils, but at lower levels also on epithelial cells, endothelial cells and fi broblasts.