Chitinases belonging to 18
glycosyl hydrolase family is an ancient gene family that is widely expressed from
prokaryotes to eukaryotes. In humans,
despite the absence of endogenous chitin, a number of Chitinases and Chitinase-like Proteins (C/CLPs) have been identified. Chitinases with
enzymatic activity have a
chitin binding domain containing six
cysteine
residues responsible for their binding to chitin.
In contrast, CLPs do
not contain such typical chitin-binding domains, but still can bind to
chitin with high affinity. Molecular phylogenetic analyses suggest that
active Chitinases result from an early
gene duplication
event. Further duplication events, followed by mutations leading to
loss of chitinase activity, allowed evolution of the chi-lectins. For
the majority of the mammalian chitinases the last decades have witnessed
the appearance of a substantial number of studies describing
their
expression differentially regulated during more specific immunologic
activities. It is becoming increasingly clear that their function is not
exclusive to catalyse the hydrolysis of chitin producing pathogens, but
include crucial role in bacterial infections and
inflammatory diseases. Here we provide an overview of all family members to shed light on the mechanisms and
molecular interactions
of Chitinases and CLPs in relation to immune response regulation, in
order to delineate their future utilization as diagnostic and prognostic
markers for numerous diseases.
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