Key result
Murine goblet cell protein mCLCA3 acts as a zinc-dependent metalloprotease with intermolecular autoproteolytic activity.
Why the study?
The mechanism by which CLCA proteins modulate chloride conductance and their potential metalloprotease activity were unclear.
Population
Transfected HEK293 cells expressing murine mCLCA3 and porcine pCLCA1
Comparison
E157Q mutation in HEXXH motif and metalloprotease inhibitors vs wild-type mCLCA3
Design
Preclinical biochemical and molecular characterization study
Authors
Loading...
Establishes mCLCA3 as zinc-dependent metalloprotease in murine goblet cells; leaves open relevance to human airway disease.
The murine goblet cell protein mCLCA3 functions as a zinc-dependent metalloprotease with intermolecular autoproteolytic activity.
Bothe et al. (2011) studied this question. mCLCA3 E157Q mutation vs. Wild-type mCLCA3 was evaluated on mCLCA3 cleavage and autoproteolytic activity. The murine goblet cell protein mCLCA3 is a zinc-dependent metalloprotease with intermolecular autoproteolytic activity that cleaves at a single site between amino acids 695 and 696.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: