Related Experiment Video
Updated: Jul 10, 2026

Dissection of Single Skeletal Muscle Fibers for Immunofluorescent and Morphometric Analyses of Whole-Mount Neuromuscular Junctions
Published on: August 14, 2021
Localization of the membrane-anchored MMP-regulator RECK at the neuromuscular junctions
Satoshi Kawashima1, Yukio Imamura, Ediriweera P S Chandana
1Department of Molecular Oncology, Kyoto University Graduate School of Medicine, Sakyo-ku, Kyoto, Japan. mnoda@virus.kyoto-u.ac.jp
Abstract:
Nerve apposition on nicotinic acetylcholine receptor clusters and invagination of the post-synaptic membrane (i.e. secondary fold formation) occur by embryonic day 18.5 at the neuromuscular junctions (NMJs) in mouse skeletal muscles. Finding the molecules expressed at the NMJ at this stage of development may help elucidating how the strong linkage between a nerve terminal and a muscle fiber is established. Immunohistochemical analyses indicated that the membrane-anchored matrix metalloproteinase regulator RECK was enriched at the NMJ in adult skeletal muscles. Confocal and electron microscopy revealed the localization of RECK immunoreactivity in secondary folds and subsynaptic intracellular compartments in muscles. Time course studies indicated that RECK immunoreactivity becomes associated with the NMJ in the diaphragm at around embryonic day 18.5 and thereafter. These findings, together with known properties of RECK, support the hypothesis that RECK participates in NMJ formation and/or maintenance, possibly by protecting extracellular components, such as synaptic basal laminae, from proteolytic degradation.
Related Concept Videos
The Neuromuscular Junction
Neuromuscular Junction And Blockade
Role of Matrix Metalloproteases in Degradation of ECM
A...
Cell-matrix's Response to Mechanical Forces
Anchoring junctions mechanically attach a cell to the...
Regulated mRNA Transport
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

