Page 69 - Veterinary Immunology, 10th Edition
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VetBooks.ir  Soluble Pattern-Recognition




               Receptors



               Although the TLRs, NLRs, and RLRs are expressed on cell surfaces,
               soluble PRRs also bind PAMPs. Because these molecules function in
               the extracellular fluid, they generally serve to promote destruction
               (phagocytosis) of any organisms they encounter. In general they do

               not induce the expression of inflammatory cytokines. That task is
               accomplished by the cell-surface PRRs.
                  Since many bacterial PAMPs are glycoproteins and
               polysaccharides, circulating carbohydrate-binding proteins called

               lectins play important roles in innate immunity. Three extracellular
               lectin families, the P-, S-, and C-type lectins, are involved in innate
               immunity.
                  P-type lectins are also called pentraxins. Pentraxins are formed by

               five protein subunits arranged in a ring. Two pentraxins, C-reactive
               protein (CRP) and serum amyloid P (SAP), are important acute-
               phase proteins (Chapter 7). (They are called acute-phase proteins
               because their blood levels climb greatly during acute infections or

               trauma.) Pentraxins have multiple biological functions, including
               activation of complement and stimulation of leukocytes. They bind
               to bacterial LPS in a calcium-dependent manner and activate the
               classical complement pathway by interacting with C1q (Chapter 4).

               They also interact with neutrophils, monocyte-macrophages, and
               NK cells and augment their activities.
                  Galectins are extracellular S-type lectins. Their name derives from
               their specificity for galactosides. They play a role in inflammation

               by binding leukocytes to the extracellular matrix.
                  C-type lectins (CLRs) are a large family of carbohydrate-binding
               proteins with many different roles. (At least 1000 have been
               identified.) All require calcium to bind to carbohydrates. Each end

               of a CLR has a distinct function; the C-terminal domain binds to
               carbohydrates, whereas the N-terminal domain interacts with cells
               or complement components, thereby exerting their biological effect.
               There are both soluble and membrane-bound CLRs. The most

               important of the soluble CLRs is mannose-binding lectin (MBL).





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