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The role of laminins in the organization and function of neuromuscular junctions.

Matrix Biol.2017 Jan;57-58:86-105. Epub 2016 Sep 07
Robert S Rogers 1 , Hiroshi Nishimune 2
Robert S Rogers 1 , Hiroshi Nishimune 2

[No authors listed]

Author information
  • 1 Department of Anatomy and Cell Biology, University of Kansas School of Medicine, Kansas City, Kansas, USA. Electronic address: rrogers3@kumc.edu.
  • 2 Department of Anatomy and Cell Biology, University of Kansas School of Medicine, Kansas City, Kansas, USA. Electronic address: hnishimune@kumc.edu.

摘要


The synapse between motor neurons and skeletal muscle is known as the neuromuscular junction (NMJ). Proper alignment of presynaptic and post-synaptic structures of motor neurons and muscle fibers, respectively, is essential for efficient motor control of skeletal muscles. The synaptic cleft between these two cells is filled with basal lamina. Laminins are heterotrimer extracellular matrix molecules that are key members of the basal lamina. Laminin α4, α5, and β2 chains specifically localize to NMJs, and these laminin isoforms play a critical role in maintenance of NMJs and organization of synaptic vesicle release sites known as active zones. These individual laminin chains exert their role in organizing NMJs by binding to their receptors including integrins, dystroglycan, and voltage-gated calcium channels (VGCCs). Disruption of these laminins or the laminin-receptor interaction occurs in neuromuscular diseases including Pierson syndrome and Lambert-Eaton myasthenic syndrome (LEMS). Interventions to maintain proper level of laminins and their receptor interactions may be insightful in treating neuromuscular diseases and aging related degeneration of NMJs.

KEYWORDS: Aged, Bassoon, Laminin, Neuromuscular junction, Voltage-gated calcium channels