A Neonatal Case of Congenital Myasthenic Syndrome with COLQ Mutation (P2.339)

CONCLUSION: COLQ is the collagenic tail that anchors a homotetramer of the catalytic subunit of AChE to the synaptic basal lamina. Over 30 mutations have been identified as a cause for COLQ deficiency (Engel). Absence of AChE from the endplate prolongs the life of ACh in the synaptic cleft so that each ACh can bind multiple AChRs before leaving the synaptic space. When the EPP outlasts the absolute refractory period of the muscle fiber, it generates a second MAP giving the characteristic EMG finding. Cholinergic over activity at the endplate results in cationic overloading and degeneration of the junctional folds with loss of AChR. Disease onset is variable from birth to late infancy and leads to generalized weakness with respiratory involvement. Some patients respond to ephedrine or albuterol (Liewluck et al).Disclosure: Dr. Imperioli has nothing to disclose. Dr. Ionita has nothing to disclose. Dr. Acsadi has received personal compensation for activities with Athena Diagnostics. Dr. Acsadi has received research support from the National Institutes of Health, Muscular Dystrophy Association, and FSMA as an investigator. Dr. Engel has received personal compensation in an editorial capacity for Neurology.
Source: Neurology - Category: Neurology Authors: Tags: Child Neurology and Developmental Neurology II Source Type: research