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From the Collagen Research Unit, Biocenter and Department of
Medical Biochemistry,*
Department of
Dermatology,
and Department of
Pathology,
University of Oulu, Finland
Two N-terminal ends of human type XVIII collagen chains have
recently been identified. The two chains have different signal peptides
and variant N-terminal noncollagenous NC1 domains of 493 (NC1-493) and
303 (NC1-303) amino acid residues, respectively, but
share 301 residues of their NC1 domains as well as the collagenous and
C-terminal noncollagenous portions of the molecule. Antibodies were
produced against the NC1 region common to both human 
1(XVIII) chain
variants and against NC1 sequences specific to the long variant and
were used in combination with in situ hybridization to
localize this collagen in a number of human tissues. They were also
used for Western blotting, which resulted in detection of
overlapping high-molecular weight bands above the 200-kd standard in a
kidney extract. Heparin lyase II and heparin lyase III digestions of
kidney and placenta extracts indicated that at least in these
tissues, type XVIII collagen contains heparin sulfate
glycosaminoglycan side chains. Type XVIII collagen was found to be a
ubiquitous basement membrane component, occurring prominently
at vascular and epithelial basement membranes throughout the body.
Comparison of the expression of the NC1-493 and NC1-303 variants
revealed marked differences. The short variant was found in most
conventional basement membranes, including blood vessels and
the various epithelial structures, and around muscular
structures. The long variant was expressed very strongly in
liver, where it was virtually the only variant in the liver
sinusoids, and it occurred only in minor amounts elsewhere.
Thus, the 192 N-terminal residues specific to the long variant
apparently confer some functional property needed above all in the
liver sinusoids, but also at certain other
locations.
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