作者: Elisabeth E. L. Nyström , Liisa Arike , Erik Ehrencrona , Gunnar C. Hansson , Malin E. V. Johansson
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摘要: Calcium-activated chloride channel regulator 1 (CLCA1) is one of the major nonmucin proteins found in intestinal mucus. It part a larger family CLCA that share highly conserved features and domain architectures. The arrangement similar to belonging ADAM (a disintegrin metalloproteinase) family, known process extracellular matrix proteins. Therefore, CLCA1 an interesting candidate search for proteases Here, we investigated CLCA1's biochemical properties both vitro mucus from mouse human colon biopsy samples. Using immunoblotting with CLCA1-specific antibodies recombinant proteins, observed C-terminal self-cleavage product forms disulfide-linked dimer noncovalently interacts N-terminal CLCA1, which further form oligomers. We also characterized second, more catalytically active, encompassing catalytic together its von Willebrand type A (VWA). This fragment was unstable but could be identified freshly prepared Furthermore, can cleave structural component MUC2. propose regulates thereby takes regulation processing.