A truncating mutation in the laminin-332&#945; chain highlights the role of the LG45 proteolytic domain in regulating keratinocyte adhesion and migration.

Di Zenzo, G; El Hachem, M; Diociaiuti, A; Boldrini, R; Calabresi, V; Cianfarani, F; Fortugno, P; Piccinni, E; Zambruno, G; Castiglia, D

A truncating mutation in the laminin-332α chain highlights the role of the LG45 proteolytic domain in regulating keratinocyte adhesion and migration.

Di Zenzo, G; El Hachem, M; Diociaiuti, A; Boldrini, R; Calabresi, V; Cianfarani, F; Fortugno, P; Piccinni, E; Zambruno, G; Castiglia, D.

Affiliation

Di Zenzo G; Laboratory of Molecular and Cell Biology, Istituto Dermopatico dell'Immacolata-IRCCS, via dei Monti di Creta 104, 00167, Rome, Italy.

Br J Dermatol ; 170(5): 1056-64, 2014 May.

Article in En | MEDLINE | ID: mdl-24387836

Subject(s)

Cell Adhesion Molecules/genetics; Epidermolysis Bullosa, Junctional/genetics; Frameshift Mutation/genetics; Laminin/genetics; Cell Adhesion/genetics; Cell Migration Assays; Cell Movement/genetics; Humans; Keratinocytes/physiology; Male; Middle Aged; Kalinin

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cell Adhesion Molecules / Epidermolysis Bullosa, Junctional / Frameshift Mutation / Laminin Type of study: Prognostic_studies Limits: Humans / Male / Middle aged Language: En Journal: Br J Dermatol Year: 2014 Type: Article Affiliation country: Italy

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