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J. Cell Biol.,
Volume 145, Number 3, May 3, 1999 605-618
3 Chain: A Novel,
Non-Basement Membrane-associated, Laminin Chain
* The Cutaneous Biology Research Center, Massachusetts General Hospital, and the Department of Dermatology, Harvard
Medical School, Charlestown, Massachusetts 02129; and Laminins are heterotrimeric molecules composed of an Studies of the tissue distribution of The Departments of Neuroscience, Anatomy and Cell Biology, and
Ophthalmology, Tufts University School of Medicine, Boston, Massachusetts 02111
, a 
, and a 
chain; they have broad functional roles in development and in stabilizing epithelial
structures. Here, we identified a novel laminin, composed of known and chains but containing a novel
chain, 3. We have cloned gene encoding this chain, LAMC3, which maps to chromosome 9 at q31-34. Protein and cDNA analyses demonstrate that 3 contains
all the expected domains of a chain, including two
consensus glycosylation sites and a putative nidogen-binding site. This suggests that 3-containing laminins
are likely to exist in a stable matrix.
3 chain show
that it is broadly expressed in: skin, heart, lung, and the
reproductive tracts. In skin, 3 protein is seen within
the basement membrane of the dermal-epidermal junction at points of nerve penetration. The 3 chain is also
a prominent element of the apical surface of ciliated
epithelial cells of: lung, oviduct, epididymis, ductus deferens, and seminiferous tubules. The distribution of
3-containing laminins on the apical surfaces of a variety of epithelial tissues is novel and suggests that they
are not found within ultrastructurally defined basement
membranes. It seems likely that these apical laminins
are important in the morphogenesis and structural stability of the ciliated processes of these cells.
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