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Northwestern University Medical School, Department of Cell and Molecular Biology, Chicago, Illinois 60611
Type IV collagen in Caenorhabditis elegans
is produced by two essential genes, emb-9 and let-2,
which encode
1- and
2-like chains, respectively. The
distribution of EMB-9 and LET-2 chains has been characterized using chain-specific antisera. The chains colocalize, suggesting that they may function in a single heterotrimeric collagen molecule. Type IV collagen is
detected in all basement membranes except those on
the pseudocoelomic face of body wall muscle and on
the regions of the hypodermis between body wall muscle quadrants, indicating that there are major structural
differences between some basement membranes in C. elegans. Using lacZ/green fluorescent protein (GFP) reporter constructs, both type IV collagen genes were
shown to be expressed in the same cells, primarily body
wall muscles, and some somatic cells of the gonad. Although the pharynx and intestine are covered with
basement membranes that contain type IV collagen,
these tissues do not express either type IV collagen
gene. Using an epitope-tagged emb-9 construct, we
show that type IV collagen made in body wall muscle
cells can assemble into the pharyngeal, intestinal, and
gonadal basement membranes. Additionally, we show
that expression of functional type IV collagen only in
body wall muscle cells is sufficient for C. elegans to
complete development and be partially fertile. Since
type IV collagen secreted from muscle cells only assembles into some of the basement membranes that it has
access to, there must be a mechanism regulating its assembly. We propose that interaction with a cell surface-associated molecule(s) is required to facilitate type IV collagen assembly.
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