Abstract
A large variety of cells in the body are exposed to extracellular matrices which affect cell function and behavior. Basement membranes are prominent matrix structures and have been shown to consist of several collagenous and non-collagenous glycoproteins and proteoglycans (Martin and Timpl, 1987). Laminin is one of the major and ubiquitous components that was originally isolated and characterized from a tumor basement membrane as a cross-shaped, multidomain protein (Timpl et al., 1979; Engel et al., 1981). It is considered to be one of the important cell-binding proteins present in basement membranes and in addition possesses binding potentials for other matrix components. Another non-collagenous glycoprotein, nidogen/entactin, was initially discovered as a sulfated 158kD polypeptide (Carlin et al., 1981) and shown to have a characteristic dumb-bell structure (Paulsson et al., 1986; 1987). Even though nidogen is also an ubiquitous constituent of basement membranes its function is not immediately apparent. However, several pieces of indirect evidence from cell culture and tissue studies (Dziadek and Timpl, 1985) provided initial clues about the possible role of nidogen, by showing that it forms tight, stoichiometric, noncovalent complexes with laminin in situ.
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© 1989 Springer-Verlag Berlin Heidelberg
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Timpl, R. et al. (1989). Structure and Biology of the Laminin-Nidogen Complex. In: Aebi, U., Engel, J. (eds) Cytoskeletal and Extracellular Proteins. Springer Series in Biophysics, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73925-5_18
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DOI: https://doi.org/10.1007/978-3-642-73925-5_18
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