Page 94 - Veterinary Immunology, 10th Edition
P. 94

In addition to their antibacterial functions, granulysins attract and
  VetBooks.ir  activate macrophages. Two other important antibacterial proteins

               are bactericidal permeability-increasing protein (BPI) and
               calprotectin. BPI is a major constituent of the primary granules of

               human and rabbit neutrophils. It kills Gram-negative bacteria by
               binding to lipopolysaccharides and damaging their inner
               membrane. Calprotectin is found in neutrophils, monocytes,
               macrophages, and epidermal cells. It forms about 60% of neutrophil

               cytosolic protein and is released in large amounts into blood and
               tissue fluid in inflammation. It belongs to the S100 family of
               antimicrobial proteins. Calprotectin sequesters zinc and manganese
               during bacterial infections and thus makes them unavailable for

               bacterial growth.
                  The production of some antimicrobial proteins by epithelial cells
               is regulated by cytokines. In particular, the two cytokines produced
               by Th17 cells, IL-17 and IL-22, are crucial regulators of antimicrobial

               peptide production in the intestine and lungs (Chapter 22).
               Likewise, IL-1 stimulates epithelial cells to produce antimicrobial
               proteins. Antimicrobial peptides regulate cytokine production and
               can serve as immunomodulators. For example, lactoferrin

               stimulates macrophage production of IL-18, whereas some
               cathelicidins stimulate production of IL-6, IL-8, and IL-10.



               Lysozyme


               The enzyme lysozyme cleaves the bond between N-acetyl-
               muraminic acid and N-acetylglucosamine and destroys cell wall
               peptidoglycans in Gram-positive bacteria. Lysozyme is found in all
               body fluids except cerebrospinal fluid and urine. It is present in
               large amounts in inflammatory tissue fluid. While absent from

               bovine neutrophils and tears, it is present in high concentrations in
               the tears of other mammals. Although many of the bacteria killed
               by lysozyme are nonpathogenic, it might reasonably be pointed out

               that this susceptibility could account for their lack of pathogenicity.
               Lysozyme is found in high concentrations in neutrophil granules
               and accumulates in areas of acute inflammation, including sites of
               bacterial invasion. Lysozyme is also a potent opsonin, binding to
               bacterial surfaces and facilitating phagocytosis in the absence of






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