Introduction of GLDN
Gliomedin (GLDN), also known as COLM, is a protein that exists in both secreted and transmembrane forms, promoting the formation of the Ranvier nodes in the peripheral nervous system. The protein is encoded by the GLDN gene in humans. GLDN is an N-glycosylated trimeric molecule consisting of a transmembrane domain, two collagenous domains, and an olfactomedin (OLF) domain, and the extracellular domain can be released by proteloytic cleavage. It has been reported that the OLF domain is responsible for interaction with the FnIII domains of neurofascin and NrCAM and that these interactions are important for inducing the formation of the nodes of Ranvier. The disruption of such interactions may be responsible for several human neuropathies such as Guillain–Barré syndrome and chronic inflammatory demyelinating polyneuropathy. Mutations in this gene cause lethal congenital contracture syndrome in human patients. Autoantibodies of the protein have been identified in serum of patients with multifocal motor neuropathy.
|Basic Information of GLDN|
|Aliases||Gliomedin shedded ectodomain, COLM, UNQ9339/PRO34011|
|Organism||Homo sapiens (Human)|
Function of GLDN Membrane Protein
Gliomedin is one of the essential proteins in the development of the nodes of Ranvier in the vertebrate peripheral nervous system. An olfactomedin (OLF) domain is located at the extracellular C-terminus of gliomedin and participates in the accumulation of neuronal plasma membrane voltage-gated sodium channels in the nodes by interacting with neurofascin and NrCAM. Gliomedin has been reported to be one of the main players in the development of the nodes of Ranvier on myelinated axons. It is a glial ligand for neurofascin and NrCAM, two axonal immunoglobulin cell-adhesion molecules associated with VGSCs at the nodes of Ranvier. Gliomedin is expressed by myelinating Schwann cells in the peripheral nervous system and accumulates at the edges of each myelin segment during development.
Fig.1 Mutations in GLDN affect the surface localization of the protein. (Maluenda, 2016)
Application of GLDN Membrane Protein in Literature
The study demonstrates that the survival of children with "Lethal" congenital contracture syndrome 11 is due to novel mutations in the GLDN gene.
The article reports the expression, purification, crystallization and preliminary X-ray crystallographic analysis of the extracellular olfactomedin domain of gliomedin.
The article indicates that perlecan binds the clustering molecule gliomedin and enhances clustering of node of Ranvier components.
The article reveals that the primary immune reaction against gliomedin, a peripheral nervous system adhesion molecule, can be responsible for the initiation or progression of the demyelinating form of GBS.
This article reports that the olfactomedin domain from gliomedin is a β-propeller with unique structural properties, which provides a structural basis for the functions of gliomedin in Schwann cells.
GLDN Preparation Options
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