Elafin, also known as peptidase inhibitor 3 or skin-derived antileukoprotease (SKALP), is a protein that in humans is encoded by the PI3gene.[3][4][5]
Function
This gene encodes an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. This gene belongs to the centromeric cluster.[5]
Clinical significance
Elafin has been found to have utility in serving as a biomarker for graft versus host disease of the skin.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Molhuizen HO, Zeeuwen PL, Olde Weghuis D, Geurts van Kessel A, Schalkwijk J (Feb 1994). "Assignment of the human gene encoding the epidermal serine proteinase inhibitor SKALP (PI3) to chromosome region 20q12→q13". Cytogenet Cell Genet. 66 (2): 129–31. doi:10.1159/000133683. PMID8287685.
Saheki T, Ito F, Hagiwara H, et al. (1992). "Primary structure of the human elafin precursor preproelafin deduced from the nucleotide sequence of its gene and the presence of unique repetitive sequences in the prosegment". Biochem. Biophys. Res. Commun. 185 (1): 240–5. doi:10.1016/S0006-291X(05)80981-7. PMID1339270.
Sallenave JM, Marsden MD, Ryle AP (1992). "Isolation of elafin and elastase-specific inhibitor (ESI) from bronchial secretions. Evidence of sequence homology and immunological cross-reactivity". Biol. Chem. Hoppe-Seyler. 373 (1): 27–33. doi:10.1515/bchm3.1992.373.1.27. PMID1536690.
Schalkwijk J, de Roo C, de Jongh GJ (1991). "Skin-derived antileukoproteinase (SKALP), an elastase inhibitor from human keratinocytes. Purification and biochemical properties". Biochim. Biophys. Acta. 1096 (2): 148–54. doi:10.1016/0925-4439(91)90053-c. PMID2001428.
Sallenave JM, Ryle AP (1991). "Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor". Biol. Chem. Hoppe-Seyler. 372 (1): 13–21. doi:10.1515/bchm3.1991.372.1.13. PMID2039600.
Zhang M, Zou Z, Maass N, Sager R (1995). "Differential expression of elafin in human normal mammary epithelial cells and carcinomas is regulated at the transcriptional level". Cancer Res. 55 (12): 2537–41. PMID7780965.
Sallenave JM, Silva A (1993). "Characterization and gene sequence of the precursor of elafin, an elastase-specific inhibitor in bronchial secretions". Am. J. Respir. Cell Mol. Biol. 8 (4): 439–45. doi:10.1165/ajrcmb/8.4.439. PMID8476637.
Tsunemi M, Matsuura Y, Sakakibara S, Katsube Y (1996). "Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 A resolution". Biochemistry. 35 (36): 11570–6. doi:10.1021/bi960900l. PMID8794736.
Francart C, Dauchez M, Alix AJ, Lippens G (1997). "Solution structure of R-elafin, a specific inhibitor of elastase". J. Mol. Biol. 268 (3): 666–77. doi:10.1006/jmbi.1997.0983. PMID9171290.
Sumi Y, Inoue N, Azumi H, et al. (2002). "Expression of tissue transglutaminase and elafin in human coronary artery: implication for plaque instability". Atherosclerosis. 160 (1): 31–9. doi:10.1016/S0021-9150(01)00542-1. PMID11755920.
External links
Overview of all the structural information available in the PDB for UniProt: P19957 (Elafin) at the PDBe-KB.