Homology of calcitonin with the amyloid-related proteins

S. Benvenga, Francesco Trimarchi, A. Facchiano

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)119-122
Number of pages4
JournalJournal of Endocrinological Investigation
Volume17
Issue number2
DOIs
Publication statusPublished - 1994

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Keywords

  • amyloidosis
  • Calcitonin
  • medullary thyroid cancer

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

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