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WAP (whey acidic protein) is an important whey protein present in milk of mammals. This protein has characteristic domains, rich in cysteine residues, called 4-DSC (four-disulfide core domain). Other proteins, mainly present at mucosal surfaces, have been shown to also possess these characteristic WAP-4-DSC domains. The present review will focus on two WAP-4-DSC containing proteins, namely SIPI (secretory leucocyte protease inhibitor) and trappin-2/elafin. Although first described as antiproteases able to inhibit in particular host neutrophil proteases [NE (neutrophil elastase), cathepsin-G and proteinase-3] and as such, able to limit maladaptive tissue damage during inflammation, it has become apparent that these molecules have a variety of other functions (direct antimicrobial activity, bacterial opsonization, induction of adaptive immune responses, promotion of tissue repair, etc.). After providing information about the 'classical' antiproteasic role of these molecules, we will discuss the evidence pertaining to their pleiotropic functions in inflammation and immunity.
Author(s): Wilkinson TS, Roghanian A, Simpson AJ, Sallenave JM
Publication type: Article
Publication status: Published
Journal: Biochemical Society Transactions
Year: 2011
Volume: 39
Pages: 1409-1415
Print publication date: 01/10/2011
ISSN (print): 0300-5127
ISSN (electronic): 1470-8752
Publisher: Portland Press Ltd.
URL: http://dx.doi.org/10.1042/BST0391409
DOI: 10.1042/BST0391409
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