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Basal lamina glycoproteins laminin and type IV collagen are assembled into a fine-fibered matrix in cultures of a teratocarcinoma-derived endodermal cell line

1982; Elsevier BV; Volume: 137; Issue: 1 Linguagem: Inglês

10.1016/0014-4827(82)90002-7

1090-2422

Ilmo Leivo, Kari Alitalo, Leila Risteli, Antti Vaheri, Rupert Timpl, Jorma Wartiovaara,

Cellular Mechanics and Interactions

Extracellular matrix glycoproteins synthesized and deposited by a mouse teratocarcinoma-derived endodermal cell line (PYS-2) in culture were analysed by metabolic labelling and immunochemical methods, and the matrix structure was studied by immunofluorescence and electron microscopy. PYS-2 cells secreted two major high-molecular weight glycoproteins, laminin and type IV collagen, which were deposited in apparently unprocessed form under the cells into a lamellar matrix composed of a loose network of fine fibrils and attached dense grains. The cells did not synthesize detectable amounts of fibronectin, but the matrix was found to bind fibronectin from the culture medium. The matrix structure was sensitive to bacterial collagenase indicating a role for type IV collagen in matrix integrity. The PYS-2 matrix which contains defined basal lamina glycoproteins provides possibilities for in vitro studies on the organization of deposited basal lamina components.