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Laminin-332 and Integrins: Signaling Platform for Cell Adhesion and Migration and its Regulation by N-Glycosylation (pp. 29-52) $0.00
Authors:  (Yoshinobu Kariya, Yukiko Kariya, Jianguo Gu, Departments of Biochemistry and Diagnostic Pathology, Fukushima Medical University School of Medicine, Hikarigaoka, Fukushima, Japan, and others)
Abstract:
Laminin-332 (formerly known as laminin-5) is a major component of basement
membranes in the skin and other stratified squamous epithelial tissues. Laminin-332 has
attracted much attention from both physicians and researchers as a disease-related and
functional molecule. The study of human genetic disorders and a knockout mouse model
has provided the evidence that laminin-332 is indispensable for adhesive structures in the
skin. In wound healing and cancer invasion, overexpression of laminin-332 accelerates
cell migration by activating PI3K, PKC, and MAPK signaling pathways. These
functional activities of laminin-332 are through interactions with several cell surface
receptors including integrins 3 1 and 6 4, and syndecans. In addition, recent studies
revealed that posttranslational modifications, such as proteolytic processing and Nglycosylation,
of laminin-332 and of integrins 3 1 and 6 4 are important for the
laminin-332 activities. This review summarizes the molecular mechanisms and
significance of cellular adhesion and migration through laminin-332 as well as integrins
3 1 and 6 4. Understanding of these regulatory mechanisms could lead to
development of new molecular targeted therapies, particularly in oncology. 


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Laminin-332 and Integrins: Signaling Platform for Cell Adhesion and Migration and its Regulation by <i>N</i>-Glycosylation (pp. 29-52)