The trappin gene family: proteins defined by an N-terminal transglutaminase substrate domain and a C-terminal four-disulphide core
| Autor: | Joost Schalkwijk, Oliver Wiedow, Shigehisa Hirose |
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| Rok vydání: | 1999 |
| Předmět: |
Protein Conformation
Molecular Sequence Data The role of proteinases and proteinase inhibitors in epidermal differentiation and inflammation Proteinase Inhibitory Proteins Secretory Biology Biochemistry Evolution Molecular Protein structure Consensus sequence Gene family Animals Humans Amino Acid Sequence Disulfides Molecular Biology Gene Peptide sequence Genomic organization Genetics Inflammation Transglutaminases De rol van proteasen en proteaseremmers bij epidermale differentiatie en ontstekingsprocessen Proteins Cell Biology biology.protein Whey Acidic Protein Elafin Research Article |
| Zdroj: | Biochemical Journal, 340, 569-77 Biochemical Journal, 340, pp. 569-77 |
| ISSN: | 0264-6021 |
| Popis: | Recently, several new genes have been discovered in various species which are homologous to the well-characterized human epithelial proteinase inhibitor elafin/SKALP (skin-derived anti-leukoproteinase). Because of the high degree of conservation and the similarities in genomic organization, we propose that these genes belong to a novel gene family. At the protein level, the family members are defined by: (1) an N-terminal domain consisting of a variable number of repeats with the consensus sequence Gly-Gln-Asp-Pro-Val-Lys that can act as an anchoring motif by transglutaminase cross-linking, and (2) a C-terminal four-disulphide core or whey acidic protein (WAP) domain, which harbours a functional motif involved in binding of proteinases and possibly other proteins. We have proposed the name trappin gene family as a unifying nomenclature for this group of proteins (trappin is an acronym for TRansglutaminase substrate and wAP domain containing ProteIN, and refers to its functional property of ‘getting trapped’ in tissues by covalent cross-linking). Analysis of the trappin family members shows extensive diversification in bovidae and suidae, whereas the number of primate trappins is probably limited. Recent biochemical and cell biological data on the human trappin family member elafin/SKALP suggest that this molecule is induced in epidermis by cellular stress. We hypothesize that trappins play an important role in the regulation of inflammation and in protection against tissue damage in stratified epithelia. |
| Databáze: | OpenAIRE |
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