Objectives: We previously found that antibodies in Tourette's syndrome (TS) patients' sera reacted with a 120 kDa protein from rat brain tissue. Here, we sought to identify this protein and determine if it was involved in TS pathogenesis.
Methods: The 120 kDa protein was identified using immunoprecipitation, Western blotting, and mass spectrometry.
Osteoclasts (OCs) attach to the extracellular matrix via specialized attachment structures called podosomes, which form a prominent F-actin-rich ring that is thought to correspond to the sealing zone of resorbing OCs. Calcitonin (CT), a 32-amino acid polypeptide, inhibits bone resorption by decreasing motility, inducing retraction, disassembling podosome, and disrupting the actin-ring structure of OCs. However, the detailed mechanisms of how CT induces the disassembly of podosome and disruption of the adhesive structures in OCs are not well characterized.
View Article and Find Full Text PDFIt has been proposed that antineural antibodies were present in patients with Tourette's syndrome (TS) and other neuropsychiatric disorders. The purpose of our study was to investigate the presence of antineural antibodies in the individuals with Tourette's syndrome and the family members of TS patients. The sera of four TS patients with no current streptococcal infection, their tic-free family members including father, mother and sibling, and a age-matched control group who were tic free were assayed for antineural antibodies directed against rat tissue and neurons in primary cell culture.
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