The beta-delta-core of sarcoglycan is essential for deposition at the plasma membrane.

Mutations of any of the sarcoglycan complex subunits (alpha, beta, delta, and gamma) cause limb-girdle muscular dystrophy. Furthermore, individual mutations lead to a reduction or loss of all other members of the complex. In some cases of limb-girdle muscular dystrophies, however, residual sarcoglycan expression has been documented.

Alpha-sarcoglycan is recycled from the plasma membrane in the absence of sarcoglycan complex assembly.

The sarcoglycan complex consists of four subunits in skeletal muscle (alpha, beta, gamma, and delta-SG). Mutations in alpha-sarcoglycan (alpha-SG) result in the most common form of limb girdle muscular dystrophy. However, the function of alpha-SG remains unknown.

Mini-dystrophin efficiently incorporates into the dystrophin protein complex in living cells.

Dystrophin is a critical muscle cell structural protein which when deficient results in Duchenne muscular dystrophy. Recently miniature versions of the dystrophin gene have been constructed that ameliorate the pathology in mouse models. To characterize mini-dystrophin's incorporation into the dystrophin protein complex in living cells, two fusion proteins were constructed where mini-dystrophin is fused to the N- or C-terminus of an enhanced green fluorescent protein reporter gene.

Amelioration of laminin-alpha2-deficient congenital muscular dystrophy by somatic gene transfer of miniagrin.

Congenital muscular dystrophy (CMD) is characterized by severe muscle wasting, premature death in early childhood, and lack of effective treatment. Most of the CMD cases are caused by genetic mutations of laminin-alpha2, which is essential for the structural integrity of muscle extracellular matrix. Here, we report that somatic gene delivery of a structurally unrelated protein, a miniature version of agrin, functionally compensates for laminin-alpha2 deficiency in the murine models of CMD.

Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite.

Programmed cell death occurs after ischemic, excitotoxic, and traumatic brain injury (TBI). Recently, a caspase-independent pathway involving intranuclear translocation of mitochondrial apoptosis-inducing factor (AIF) has been reported in vitro; but whether this occurs after acute brain injury was unknown. To address this question adult rats were sacrificed at various times after TBI.