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The syntrophins are a family of structurally related proteins that contain multiple protein interaction motifs. Syntrophins associate directly with dystrophin, the product of the Duchenne muscular dystrophy locus, and its homologues. We have generated alpha-syntrophin null mice by targeted gene disruption to test the function of this association. The(More)
Aging is a major risk factor for metabolic disease and loss of skeletal muscle mass and strength, a condition known as sarcopenia. Both conditions present a major health burden to the elderly population. Here, we analyzed the effect of mildly increased PGC-1alpha expression in skeletal muscle during aging. We found that transgenic MCK-PGC-1alpha animals had(More)
Formation of the synaptic basal lamina at vertebrate neuromuscular junction involves the accumulation of numerous specialized extracellular matrix molecules including a specific form of acetylcholinesterase (AChE), the collagenic-tailed form. The mechanisms responsible for its localization at sites of nerve- muscle contact are not well understood. To(More)
The collagen-tailed form of acetylcholinesterase (AChE) is concentrated at the vertebrate neuromuscular junction (NMJ), where it is responsible for rapidly terminating neurotransmission. This unique oligomeric form of AChE, consisting of three tetramers covalently attached to a collagen-like tail, is more highly expressed in innervated regions of skeletal(More)
Asymmetric forms of acetylcholinesterase (AChE) are thought to be the predominant forms of this enzyme at vertebrate neuromuscular junctions where they attach to the synaptic basal lamina via a collagen-like tail. High salt and heparin-containing buffers are capable of solubilizing asymmetric AChE molecules from skeletal muscle; however, detachment of AChE(More)
Tissue-cultured chicken embryo muscle cells synthesize several molecular forms of acetylcholinesterase (AChE) which differ in oligomeric structure and fate as membrane-bound or secreted molecules. Using irreversible inhibitors to inactivate AChE molecules we show that muscle cells rapidly synthesize and assemble catalytically active oligomers which transit(More)
Acetylcholinesterase (AChE) was the first identified synaptic component, characterized by its catalytic affinity for choline esters, and for a long time provided the conceptual scaffold for studies of the neuromuscular junction (NMJ). AChE was the first protein localized to the NMJ, in the 1930s, and its local expression shown to be regulated by the(More)
The highly organized pattern of acetylcholinesterase (AChE) molecules attached to the basal lamina of the neuromuscular junction (NMJ) suggests the existence of specific binding sites for their precise localization. To test this hypothesis we immunoaffinity purified quail globular and collagen-tailed AChE forms and determined their ability to attach to frog(More)
Heparin is capable of solubilizing a subset of collagen-tailed (A12) acetylcholinesterase (AChE) molecules from skeletal basal lamina (Rossi, S. G., and Rotundo, R. L. (1993) J. Biol. Chem. 268, 19152-19159). In the present study, we used tissue-cultured quail myotubes to show that, like adult fibers, neither heparin- nor high salt-containing buffers(More)
The major molecular form of acetylcholinesterase (AChE) from chicken brain is a membrane-bound glycoprotein with an apparent sedimentation coefficient of 11.4 S. Analysis of the purified protein by gel filtration, velocity sedimentation, and sodium dodecyl sulfate-gel electrophoresis shows that the solubilized enzyme is a globular tetramer with an apparent(More)