New protein found mixed with amyloid deposits linked to spinal stenosis
Researchers discovered lysozyme alongside transthyretin amyloid in the spinal ligaments of patients with lumbar stenosis. While the proteins don't interact, lysozyme actually slows transthyretin fiber formation—a finding that could reshape understanding of age-related spine disease and inform drug development strategies targeting amyloid-driven disorders.
Originaltitel: Lysozyme as an amyloid fibril protein together with transthyretin in the ligamentum flavum in association with lumbar spinal stenosis
BACKGROUND: Transthyretin amyloid (ATTR) is frequently found in aging ligaments and may represent an early sign of systemic ATTR amyloidosis, particularly of wild-type origin. Amyloid deposits of other compositions are commonly observed alongside ATTR deposits. METHODS: fibril formation and potential cross-seeding by the two major proteins, transthyretin and lysozyme, were assessed with the thioflavin-T assay. RESULTS: , cross-seeding between TTR and lysozyme was not observed; however, lysozyme inhibited TTR fibrillation. CONCLUSION: In lumbar spinal stenosis, ATTR amyloid deposits are predominant but are often intermixed with other amyloid deposits, notably those of lysozyme origin.