title: Laminins of the dermo-epidermal junction.
abstract: Laminins are the most abundant structural non-collagenous glycoproteins ubiquitously present in basement membranes. They are multidomain molecules constituting a family of possibly more than 50 members. Some members such as laminins 5, 6 and 10 are specific of the basal lamina present under stratified epithelia. Although only few intact laminin isoforms have been purified from cultivated cells or tissues, genetic engineering has opened the way for a rapid development of laminin structural biology. Moreover, the phenotypes resulting from gene targeting in mouse or from laminin defects in acquired or inherited human diseases highlight the pivotal role of laminins in morphogenesis, development, and physiology. Indeed, the laminins display a remarkable repertoire of functions, most importantly as structural elements forming a network throughout the basement membrane to which other collagenous or non-collagenous glycoproteins and proteoglycans attach. Furthermore, they are signaling molecules providing adjacent cells with diverse information by interacting with cell surface components.
authors.affiliation: Institut II für Biochemie, Medical Faculty, Cologne, Germany. aumailley@uni-koeln.de
authors.forename: M
authors.initials: M
authors.lastname: Aumailley
authors.forename: P
authors.initials: P
authors.lastname: Rousselle
mesh_terms: D000818:Animals; D020405:Dermis / Q000378:metabolism / Q000502:physiology*; D004817:Epidermis / Q000378:metabolism / Q000502:physiology*; D015870:Gene Expression; D006801:Humans; D007797:Laminin / Q000096:biosynthesis / Q000378:metabolism*; D051379:Mice; D011499:Protein Processing, Post-Translational; D014018:Tissue Distribution
chemical_list: D007797:Laminin