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© The Rockefeller University Press, 0021-9525/1999//605 $5.00
The Journal of Cell Biology, Volume 145, Number 3, , 1999 605-618

Characterization and Expression of the Laminin 3 Chain: A Novel, Non-Basement Membrane–associated, Laminin Chain

Manuel Koch^*, Pamela F. Olson^*, Anne Albus^*, William Jin^*, Dale D. Hunter, William J. Brunken^*, Robert E. Burgeson^*, and Marie-France Champliaud^*

^* The Cutaneous Biology Research Center, Massachusetts General Hospital, and the Department of Dermatology, Harvard Medical School, Charlestown, Massachusetts 02129; and The Departments of Neuroscience, Anatomy and Cell Biology, and Ophthalmology, Tufts University School of Medicine, Boston, Massachusetts 02111

Laminins are heterotrimeric molecules composed of an , a β, 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 β 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.

Studies of the tissue distribution of 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.

Key Words: laminin • testis • oviduct • lung • chromosome 9q31-34

Abbreviations used in this paper: FCMD, Fukuyama congenital muscular dystrophy; FISH, fluorescent in situ hybridization; G, globular.

Dr. Brunken is on leave from the Department of Biology, Boston College.

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