Deletion of integrin α7 subunit does not aggravate the phenotype of laminin α2 chain-deficient mice.

ABSTRACT: Laminin-211 is a major constituent of the skeletal muscle basement membrane, exerting its biological functions by binding to cell surface receptors integrin α7β1 and dystroglycan (the latter is part of the dystrophin-glycoprotein complex). The importance of these molecules for normal muscle function is underscored by the fact that their respective deficiency leads to different forms of muscular dystrophy with different severity in humans and animal models. We recently demonstrated that laminin α2 chain and members of the dystrophin-glycoprotein complex have overlapping but non-redundant roles despite being part of the same adhesion complex. To analyse whether laminin-211 and integrin α7 subunit have non-redundant functions we generated mice deficient in laminin α2 chain and integrin α7 sub

SUBMITTER: Gawlik KI 

PROVIDER: S-EPMC4564817 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature