As an
autoimmune disease,
myasthenia gravis is caused by the dysfunction of neural transmission.
Acetylcholine is known to exert its function after entering into synaptic cleft through binding onto postsynaptic membrane. The role of
acetylcholine in binding
MuSK in
myasthenia gravis, however, remains unknown. A total of 38
myasthenia gravis patients and 27 healthy controls were included in this study for the detection of the expression of
MuSK using immunofluorescent method. Expression of both
MuSK and
interleukin-6 (IL-6) were measured by Western blot, followed by the correlation analysis between
heat shock protein 90 (HSP90) and
IL-6 which were measured by
enzyme-linked
immunosorbent assay (ELISA). In
myasthenia gravis patients,
MuSK was co-localized with
acetylcholine at the postsynaptic membrane. Such accumulation of
MuSK, however, did not occur in normal people. Meanwhile we also observed elevated expression of
IL-6 in
myasthenia gravis patients (p<0.05). ELISA assay showed higher expression of HSP90 in patients. Further signaling pathway screening revealed the activation of IL-6-mediated pathways including STAT3 and SPH2. In conclusion,
MuSK was co-localized with
acetylcholine in
myasthenia gravis patients, with elevated expression. HSP90 in disease people can activate
IL-6 mediated signaling pathways.