The role of laminins in basement membrane function. J Anat

Institut für Biochemie II, Medical Faculty, Cologne, Germany.
Journal of Anatomy (Impact Factor: 2.1). 08/1998; 193 ( Pt 1)(01):1-21. DOI: 10.1046/j.1469-7580.1998.19310001.x
Source: PubMed


Laminins are a family of multifunctional macromolecules, ubiquitous in basement membranes, and represent the most abundant structural noncollagenous glycoproteins of these highly specialised extracellular matrices. Their discovery started with the difficult task of isolating molecules produced by cultivated cells or extracted from tissues. The development of molecular biology techniques has facilitated and accelerated the identification and the characterisation of new laminin variants making it feasible to identify full-length polypeptides which have not been purified. Further, genetically engineered laminin fragments can be generated for studies of their structure-function relationship, permitting the demonstration that laminins are involved in multiple interactions with themselves, with other components of the basal lamina, and with cells. It endows laminins with a central role in the formation, the architecture, and the stability of basement membranes. In addition, laminins may both separate and connect different tissues, i.e. the parenchymal and the interstitial connective tissues. Laminins also provide adjacent cells with a mechanical scaffold and biological information either directly by interacting with cell surface components, or indirectly by trapping growth factors. In doing so they trigger and control cellular functions. Recently, the structural and biological diversity of the laminins has started to be elucidated by gene targeting and by the identification of laminin defects in acquired or inherited human diseases. The consequent phenotypes highlight the pivotal role of laminins in determining heterogeneity in basement membrane functions.

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    • "Laminins are composed of one alpha (α), one beta (β) and one gamma (γ) chain that are twisted together to form either a cruciform or a T-shaped structure. Currently, at least 15 different combinations (αβγ) of laminins are known [9-11]. "
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    • "Extracellular matrix (ECM) molecules are known to contribute to the neural differentiation of stem cells and complement the regeneration of the peripheral nervous system [3]. Combinations of synthetic or natural biomaterials with neuralinteracting laminin proteins have been shown to influence cellular attachment, migration, proliferation and differentiation and is promising as an extracellular matrix platform for regeneration [4]. Materials functionalized with laminin or laminin-derived peptides have been shown to increase neurite extension [5e7]. "
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    • "Fibronectins connect cells with collagens and other ECM components via cell-surface integrin receptors (reviewed in Teti, 1992). Laminins are glycoproteins that modulate adhesion and signaling through integrin binding; additionally, they adhere to other ECM molecules, including other laminins, to form a network that strengthens the membrane by resisting tensile force (reviewed in Aumailley and Smyth, 1998). "
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