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More and more data is moving online. Employees and customers expect to view and modify online information. 24 7 e-commerce and customer care with lower budgets require online access to transactional information, support data, and so on. Information stored and moved on the network has been moved to increase employee productivity. E-learning and supply-chain information is driving media-rich and storage-hungry content to servers where it can be easily accessed.

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Strictly, adipokines are cytokines that are secreted by adipocytes into the extravascular space and/or the circulation, such as leptin and adiponectin. Other adipose tissue products include LPL (exported to the vascular endothelium), various binding proteins, prostaglandins and sterol hormones. The latter include oestrogens produced from circulating androgens under the in uence of the aromatase enzyme, which is located in mesenchymal cells and preadipocytes cells rather than in mature adipocytes (Simpson et al., 2002). In addition, numerous bioactive factors and cytokines are now known to be expressed and released by the SVF cells, not adipocytes (Fain, 2006) a distinction that has not always been made clear (Rajala and Scherer, 2003; Trayhurn and Wood, 2004). Some examples are shown in Figure 4.3. Mainly SVF-speci c products include various cytokines and other factors important in in ammation, such as the interleukins (IL-1 , IL-6, IL-8, IL-10 and IL-18), the interleukin receptor antagonist, IL1-Ra, and TNF- (Fain et al., 2004; Bruun et al., 2004; Curat et al., 2006). Some other products are released by both adipocytes and SVF cells, such as cathepsins, resistin, serum amyloid (SAA-1 and -2), haptoglobin, pentraxin-3 and macrophage migration inhibitory factor (MIF) (Fain, 2006). This account focuses on leptin and adiponectin. Other adipokines include resistin (Steppan et al., 2001); apelin, a peptide also secreted by hypothalamic neurones (Boucher et al., 2005); visfatin, which apparently has insulin-mimetic effects (Fukuhara et al., 2005, 2007); and retinolbinding protein-4 (RBP-4), which may induce insulin resistance in rodents (Yang et al., 2005), but remains of uncertain signi cance in humans (Graham et al., 2006; Vitkova et al., 2007).

2. Click the Trash button on the toolbar or choose Edit Clear (Mac) or Edit Delete (Windows). When in Navigation view or Links view, you can also press your keyboard s Delete/Backspace key. 3. A dialog box asks if you are sure you wish to move this file to the site trash. Click Move (Mac) or Yes (Windows). The page will move to the Site Trash folder. If you ve changed GoLive s default to have files go directly to your hard drive s trash, the dialog box will ask if you are sure you want to move this file to the Finder Trash (Mac) or the Recycle Bin (Windows). If you ve unchecked the Show Warning option, you will not see the Warning dialog box.

lysins that could serve as potential enzybiotics will only continue to grow. Whether viral or proviral, lysin sequences are additionally valuable in that they allow the construction of chimeric proteins that juxtapose the various domains of individual enzymes. The truly modular nature of Gram-positive lysins lends itself to such manipulation, allowing for the expression of enzymes with unique combinations of biochemical properties. Additionally, by fusing the binding domain of one lysin with the enzymatic domain of another, it is possible to construct enzymes with cross-engineered bacterial speci city. The concept of chimeric lysins has actually existed for some time, although relatively few examples have been tested experimentally. D az et al. (1990, 1991) rst exchanged the modular domains of several of pneumococcal lytic enzymes (including phage enzymes and the LytA autolysin) and demonstrated preserved enzymatic and binding function. Sheehan et al. (1996) later fused the enzymatic domain of a Lactococcus lactis phage

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