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Calcium-activated chloride channel regulator 1 (CLCA1) forms non-covalent oligomers in colonic mucus and has mucin 2-processing properties

Journal article
Authors Elisabeth E. L. Nyström
Liisa Arike
Erik Ehrencrona
Gunnar C. Hansson
Malin E V Johansson
Published in Journal of Biological Chemistry
Volume 294
Issue 45
Pages 17075-17089
ISSN 0021-9258
Publication year 2019
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 17075-17089
Language en
Links dx.doi.org/10.1074/jbc.RA119.009940
Keywords mucin, intestine, colitis, protease, metalloprotease, gastrointestinal, tract, Gob-5, mouse Clca3, mucin-2 (MUC2), von Willebrand type D domain, (VWD), o-glycosylation, mclca3 protein, family, identification, cleavage, domain, metalloprotease, terminus, biopsies, release, Biochemistry & Molecular Biology
Subject categories Biochemistry and Molecular Biology

Abstract

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

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