Dystroglycan is a binding protein of laminin and merosin in peripheral nerve

  title={Dystroglycan is a binding protein of laminin and merosin in peripheral nerve},
  author={Hiroki Yamada and Teruo Shimizu and Takeshi Tanaka and Kevin P. Campbell and Kiichiro Matsumura},
  journal={FEBS Letters},

Characterization of Dystroglycan‐Laminin Interaction in Peripheral Nerve

The dystroglycan‐laminin interaction in peripheral nerve is characterized and a role for glycosylation of α‐dystrogycan in the interaction with laminin is suggested.

Expression of Dystroglycan and the Laminin-α2 Chain in the Rat Peripheral Nerve during Development

The hypothesis that the dystroglycan complex functions as an adhesion apparatus, binding the Schwann cell outer membrane with the basal lamina, is supported and a role in Schwanncell myelination through its interaction with laminin-2 is suggested.

The role of dystroglycan, a novel receptor of laminin and agrin, in cell differentiation.

Findings point to the fundamental role of dystroglycan in the cellular differentiation process shared by many different cell types, as a laminin receptor, that contributes to sarcolemmal stabilization during contraction and stretch of striated muscle cells.

A Role of Dystroglycan in Schwannoma Cell Adhesion to Laminin*

A role for dystroglycan as a major cell adhesion molecule in the surface membrane of RT4 cells is characterized and shown to be a major laminin-binding protein complex.

Expression of dystroglycan and laminin-2 in peripheral nerve under axonal degeneration and regeneration

It is suggested that the dystroglycan complex may play a role in the process of Schwann cell ensheathment and myelination through the interaction with laminin-2.

Association of dystroglycan and laminin-2 coexpression with myelinogenesis in peripheral nerves

Results suggest that coexpression of dystroglycan and laminin-2 is associated with myelinogenesis in peripheral nerves, and these two proteins may function as an anchorage between the abaxonal membrane and the basal lamina, enabling myelin forma-tion to progress.

Characterization of the Transmembrane Molecular Architecture of the Dystroglycan Complex in Schwann Cells*

The results indicate 1) that Dp116 is a component of the submembranous cytoskeletal system that anchors the dystroglycan complex in Schwann cells, and 2) that this fragility may be attributable to the absence of the sarcoglycan complex.



A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin

The results support a role for the striated muscle dystrophin-glycoprotein complex in linking the actin- based cytoskeleton with the extracellular matrix and suggest that dystophin and dystroglycan may play substantially different functional roles in nonmuscle tissues.

Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse.

The dy mouse may provide a model for autosomal muscular dystrophies in humans and facilitate studies of functions of M-laminin, suggesting that a mutation in the M-chain gene causes the muscular dystrophy in dy/dy mice.

Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix

The hypothesis that the dramatic reduction in the 156K DAG in Duchenne muscular dystrophy leads to a loss of a linkage between the sarcolemma and extra-cellular matrix and that this may render muscle fibres more susceptible to necrosis is supported.

Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization.

The data suggest that muscle and non-muscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence, and hypothesize that variable glycosylation of the conserved protein core might modulate laminin binding.

Abnormal localization of laminin subunits in muscular dystrophies

Merosin, a tissue-specific basement membrane protein, is a laminin-like protein.

Intact merosin was isolated from placental extracts and shown to be covalently associated with the laminin B chains and to have a cross-like structure similar to that of laminIn, showing that both proteins are members of the same family of basement membrane proteins.