The functions of gangliosides in auto-immune reactions may depend on their carbohydrate and ceramide structures (3): the hydrophobic ceramide tail of gangliosides is embedded in the lipid bi-layer of the plasma membrane, usually in the cholesterol-enriched microdomains, while the extracellular hydrophilic oligosaccharide moiety is exposed to specific auto-antibodies, and its conformations can be varied to enhance or reduce the autoantibody binding affinity, depending on the binding requirements for a particular antibody (8,9). Guillain-Barr syndrome (GBS) is a broad term used to describe a number of acute inflammatory immune-mediated syndromes consisting of sensory dysfunction, autonomic dysfunction, progressive weakness and pain (10). failure. Testing of anti-gangliosides autoantibodies is helpful for diagnosis of autoimmune peripheral neuropathies or support the diagnosis of the subtypes. These anti-gangliosides antibodies are usually detected by several qualitative or quantitative methods, particularly enzyme-linked immunosorbent assay (ELISA) and immunodot assays, which have been commercialized or established in-house worldwide. Herein, we introduce the methods and clinical applications of these assays in the diagnosis of autoimmune peripheral neuropathies. Anti-gangliosides antibodies are diagnostic markers of GBS subtypes. We use GBS as an example to explain the role of anti-gangliosides antibodies in the pathogenesis and diagnostic classification of neuropathies. Keywords: Anti-gangliosides antibodies, TPOP146 Guillain-Barr syndrome (GBS), detection methods, clinical applications Introduction Gangliosides, mainly located in the outer layer of the bilayer structure of the neuronal cell membrane, play important functions in cellular growth and differentiation, signal transduction, and immune reactions (1,2). Primary gangliosides associated with nervous system autoimmune diseases are GM1, GD1a, GalNAc-GD1a, GM1b, GD3, CD1b, GT1a, and GQ1b (3-6). Anti-ganglioside antibodies binding to the corresponding gangliosides, activate the complement system and lead to neural damage, including axonal degeneration and loss of myelin (4). IgG and complement deposits around the axolemma at the nodes of Ranvier of motor fibers are found early in the course of the disease. Clinical manifestations are variable and electrophysiological features are axonal degeneration and block conduction (4,7). The functions of gangliosides in auto-immune reactions may depend on their carbohydrate and ceramide structures (3): the hydrophobic ceramide tail of gangliosides is usually embedded in the lipid bi-layer of the plasma membrane, usually in the cholesterol-enriched microdomains, while the extracellular hydrophilic oligosaccharide moiety is usually exposed to specific auto-antibodies, and its conformations can be varied to enhance or reduce the autoantibody binding affinity, depending on the binding requirements for a particular antibody (8,9). Guillain-Barr syndrome (GBS) is usually a broad term used to describe a number of acute inflammatory immune-mediated syndromes consisting of sensory dysfunction, autonomic dysfunction, progressive weakness and pain (10). By the clinical symptoms and nerve conduction test, GBS is usually classified into several subtypes: acute inflammatory demyelinating polyradiculoneuropathy (AIDP), acute motor and sensory axonal neuropathy (AMSAN); pharyngeal-cervical-brachial variant (PCB); Miller Fisher syndrome (MFS) and Bickerstaff brainstem encephalitis (BBE); and real motor GBS, which is usually subdivided into acute motor axonal neuropathy (AMAN) and acute motor demyelinating neuropathy (11,12). As a treatable rare disease, timely diagnosis and TPOP146 subtype-classification play crucial functions in GBS treatment (13). In this review, we discuss the different types of GBS and clinical features associated with anti-ganglioside antibodies (jejunijejuni(20). For the case of double-positivity, the reports mainly involved a large number of patients with TPOP146 GQ1b and GT1a double-positive, and it may be due to the cross-reaction between the antibodies and these structurally comparable antigens (51). However, in our study, serum neutralization analysis was performed on GD1b and GM1 double positive serum. For example, serum samples were mixed with GM1 answer (50 M) and incubated for 1 hour before detection of autoantibodies. Serum neutralization by the antigen GM1 did not affect the color development of anti-GD1b TPOP146 autoantibody and YY was supported by the National Natural Science Foundation of China (No. 81571596) and the Fundamental Research Funds for the Central Universities (No. GK201701009). Notes The authors are accountable for all aspects of the work in ensuring that questions related to the accuracy or integrity of any part of the work are appropriately investigated and resolved. Footnotes This article was commissioned by the Guest Editors (Hai-Feng Li and Xiangjun Chen) for the series Laboratory Investigations in Neuroimmunological Diseases and Their Clinical Significance published in Annals of Translational Medicine. The article has undergone Rabbit polyclonal to Caspase 8.This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family.Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. external peer review. Conflicts of Interest: All authors have completed the ICMJE uniform disclosure form (available at https://atm.amegroups.com/article/view/10.21037/atm-20-2285/coif). The series Laboratory Investigations in Neuroimmunological Diseases and Their Clinical Significance was commissioned by the editorial office without any funding or sponsorship. All authors report grants from the National Natural Science Foundation of China (No. 81571596), and grants from the Fundamental Research Funds for the Central Universities (No. GK201701009), during the conduct of the study. The authors have no other conflicts of interest to declare..
The functions of gangliosides in auto-immune reactions may depend on their carbohydrate and ceramide structures (3): the hydrophobic ceramide tail of gangliosides is embedded in the lipid bi-layer of the plasma membrane, usually in the cholesterol-enriched microdomains, while the extracellular hydrophilic oligosaccharide moiety is exposed to specific auto-antibodies, and its conformations can be varied to enhance or reduce the autoantibody binding affinity, depending on the binding requirements for a particular antibody (8,9)