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Laminin-311 (Laminin-6) Fiber Assembly by Type I-like Alveolar Cells

Phillip J. DeBiase¹, Kimberly Lane¹, Scott Budinger, Karen Ridge, Mindy Wilson and Jonathan C.R. Jones

Division of Pulmonary Medicine and Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois

Correspondence to: Jonathan C.R. Jones, Division of Pulmonary Medicine, Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Tarry 8-715, 303 E. Chicago Avenue, Chicago, IL 60611. E-mail: j-jones3{at}northwestern.edu

Two epithelial cell types cover the alveolar surface of the lung. Type II alveolar epithelial cells produce surfactant and, during development or following wounding, give rise to type I cells that are involved in gas exchange and alveolar fluid homeostasis. In culture, freshly isolated alveolar type II cells assume a more squamous (type I-like) appearance within 4 days after plating. They assemble numerous focal adhesions that associate with the actin cytoskeleton at the cell margins. These alveolar epithelial cells lose expression of type II cell markers including SP-C and after 4 days in culture express the type I cell marker T1. Those cells that express T1 also deposit fibers of laminin-311 in their matrix. The latter appears to be related to their development of a type I phenotype because freshly isolated, primary type I cells also assemble laminin-311-rich fibers in vitro. A ß1 integrin antibody antagonist inhibits the assembly of laminin-311 matrix fibers. Moreover, the formation of laminin fibers is dependent on the activity of the small GTPases and is perturbed by ML-7, a myosin light chain kinase inhibitor. In summary, our data indicate that assembly of laminin-311 fibers by lung epithelial cells is integrin and actin cytoskeleton dependent, and that these fibers are characteristic of type I alveolar cells. (J Histochem Cytochem 54:665–672, 2006)

Key Words: matrix adhesion • cytoskeleton • differentiation

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