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Am. J. Respir. Cell Mol. Biol., Volume 19, Number 2, August, 1998 237-244

Expression of Laminin alpha 3, alpha 4, and alpha 5 Chains by Alveolar Epithelial Cells and Fibroblasts

Richard A. Pierce, Gail L. Griffin, M. Susan Mudd, Michael A. Moxley, William J. Longmore, Joshua R. Sanes, Jeffrey H. Miner, and Robert M. Senior

Departments of Internal Medicine, Cell Biology and Physiology, and Anatomy and Neurobiology, Washington University School of Medicine, St. Louis; and the Doisy Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, St. Louis, Missouri

Laminins are principal components of basement membranes. Eleven laminin isoforms are known, each a heterotrimer composed of polypeptide chains designated alpha , beta , and gamma . Five alpha  chains have been identified to date: alpha 1, alpha 2, alpha 3, alpha 4, and alpha 5. Recent studies of fetal and adult mouse lung show prominence of alpha 3, alpha 4, and alpha 5 in alveolar tissue, and point to differences in the cellular expression of these alpha  chains in the developing alveolus. We examined isolated rat alveolar type II cells and lung fibroblasts for expression of laminins alpha 3, alpha 4, and alpha 5. We found that laminin alpha 3 was expressed only by alveolar epithelial cells, that laminin alpha 4 was expressed only by lung fibroblasts, and that laminin alpha 5 was expressed primarily by alveolar epithelial cells. Metabolic labeling and immunoprecipitation confirmed the production of laminin alpha 4 by fibroblasts and laminin alpha 5 by alveolar epithelial cells in culture. These studies indicate that different alveolar cell types contribute different laminin alpha  chains to the laminin isoforms in alveolar basement membranes. Immunohistochemistry showed colocalization of these laminin alpha chains with the laminin beta 1, beta 2, and gamma 1 chains, indicating the likelihood that laminins 6 to 11 are present in alveolar basement membranes.




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