Abstract
Members of the whey acidic protein (WAP) or WAP four-disulfide-core (WFDC) family of proteins are a relatively under-explored family of low molecular weight proteins. The two most prominent WFDC proteins, secretory leukocyte protease inhibitor (SLPI) and elafin (or the precursor, trappin-2), have been shown to possess multiple functions including anti-protease, anti-bacterial, anti-viral and anti-inflammatory properties. It is therefore of no surprise that both SLPI and elafin/trappin-2 have been developed as potential therapeutics. Given the abundance of SLPI and elafin/trappin-2 in the human lung, most work in the area of WFDC research has focused on the role of WFDC proteins in protecting the lung from proteolytic attack. In this review, we will outline the current evidence regarding the expanding role of WFDC protein function with a focus on WFDC activity in lung disease as well as emerging data regarding the function of some of the more recently described WFDC proteins.
Acknowledgments
Cystic Fibrosis Foundation (WELDON15G0), the European Union Seventh Framework Program (FP7/2007-2011) under grant agreement no. 603038 (CF Matters), and the Department for Employment and Learning (Northern Ireland).
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©2017 Walter de Gruyter GmbH, Berlin/Boston
Articles in the same Issue
- Frontmatter
- Reviews
- The structural and functional changes of blood cells and molecular components in diabetes mellitus
- The role of whey acidic protein four-disulfide-core proteins in respiratory health and disease
- Substrate processing in intramembrane proteolysis by γ-secretase – the role of protein dynamics
- Human and rodent aryl hydrocarbon receptor (AHR): from mediator of dioxin toxicity to physiologic AHR functions and therapeutic options
- Research Articles/Short Communications
- Protein Structure and Function
- Analysis of anticoagulants for blood-based quantitation of amyloid β oligomers in the sFIDA assay
- Stability and aggregation propensity do not fully account for the association of various germline variable domain gene segments with light chain amyloidosis
- The insect-derived antimicrobial peptide metchnikowin targets Fusarium graminearum β(1,3)glucanosyltransferase Gel1, which is required for the maintenance of cell wall integrity
- Cell Biology and Signaling
- Hypoxia-induced microRNA-146a represses Bcl-2 through Traf6/IRAK1 but not Smad4 to promote chondrocyte autophagy
- Characterization of the subcellular localization and nuclear import molecular mechanisms of herpes simplex virus 1 UL2
Articles in the same Issue
- Frontmatter
- Reviews
- The structural and functional changes of blood cells and molecular components in diabetes mellitus
- The role of whey acidic protein four-disulfide-core proteins in respiratory health and disease
- Substrate processing in intramembrane proteolysis by γ-secretase – the role of protein dynamics
- Human and rodent aryl hydrocarbon receptor (AHR): from mediator of dioxin toxicity to physiologic AHR functions and therapeutic options
- Research Articles/Short Communications
- Protein Structure and Function
- Analysis of anticoagulants for blood-based quantitation of amyloid β oligomers in the sFIDA assay
- Stability and aggregation propensity do not fully account for the association of various germline variable domain gene segments with light chain amyloidosis
- The insect-derived antimicrobial peptide metchnikowin targets Fusarium graminearum β(1,3)glucanosyltransferase Gel1, which is required for the maintenance of cell wall integrity
- Cell Biology and Signaling
- Hypoxia-induced microRNA-146a represses Bcl-2 through Traf6/IRAK1 but not Smad4 to promote chondrocyte autophagy
- Characterization of the subcellular localization and nuclear import molecular mechanisms of herpes simplex virus 1 UL2