Abstract
We present evidence for a structural homology between the amino acid sequence of calcitonin (CT) — the fibrillar protein of the amyloid deposits of medullary thyroid cancer — and that of other 12 amyloid-related proteins (ARP). Seven of the 32 residues of CT are conserved in at least five ARP, and five of these seven amino acids belong to the stretch Gly2-Gln14. Gln14 is conserved in all 12 ARP and Cys7 in all eight ARP containing cysteine. The concentration of the homology in the N-terminal half of CT goes along with the knowledge that is the C-terminal region the one more important for the hormonal action of CT. Since an imbalance between synthesis and catabolism of a given ARP is believed to be the general pathogenetic mechanism of amyloidosis, the intratumoral deposition of CT in the form of amyloid fibrils would be due to the overproduction of a protein structurally similar to the ARP.
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Benvenga, S., Trimarchi, F. & Facchiano, A. Homology of calcitonin with the amyloid-related proteins. J Endocrinol Invest 17, 119–122 (1994). https://doi.org/10.1007/BF03347697
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DOI: https://doi.org/10.1007/BF03347697