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J Biol Chem, Vol. 274, Issue 19, 13681-13689, May 7, 1999
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From the Departments of Collectins are a C-lectin family with
collagen-like sequences and carbohydrate recognition domains. These
proteins can bind to carbohydrate antigens of microorganisms and
inhibit their infection by direct neutralization and agglutination, the
activation of complement through the lectin pathway, and opsonization
by collectin receptors. Here we report the cloning of a cDNA
encoding human collectin from liver (CL-L1
(collectin liver 1))
that has typical collectin structural characteristics, consisting of an
N-terminal cysteine-rich domain, a collagen-like domain, a neck domain,
and a carbohydrate recognition domain. The cDNA has an insert of
831 base pairs coding for a protein of 277 amino acid residues. The deduced amino acid sequence shows that this collectin has a unique repeat of four lysine residues in its C-terminal area. Northern blot,
Western blot, and reverse transcription-polymerase chain reaction
analyses showed that CL-L1 is present mainly in liver as a cytosolic
protein and at low levels in placenta. More sensitive analyses by
reverse transcription-polymerase chain reactions showed that most
tissues (except skeletal muscle) have CL-L1 mRNA. Zoo-blot analysis
indicated that CL-L1 is limited to mammals and birds. A chromosomal
localization study indicated that the CL-L1 gene localizes
to chromosome 8q23-q24.1, different from chromosome 10 of other human
collectin genes. Expression studies of fusion proteins lacking the
collagen and N-terminal domains produced in Escherichia
coli affirmed that CL-L1 binds mannose weakly. CL-L1 and
recombinant CL-L1 fusion proteins do not bind to mannan columns.
Analysis of the phylogenetic tree of CL-L1 and other collectins
indicated that CL-L1 belongs to a fourth subfamily of collectins
following the mannan-binding protein, surfactant protein A, and
surfactant protein D subfamilies including bovine conglutinin and
collectin-43 (CL-43). These findings indicate that CL-L1 may be
involved in different biological functions.
Pathology, ¶ Food
Microbiology, Virology, and ** Pharmaceutical Affairs,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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