Calcitonin-typical suppression of osteoclastic activity by amphioxus calcitonin superfamily peptides and insights into the evolutionary conservation and diversity of their structures

Calcitonin-typical suppression of osteoclastic activity by amphioxus calcitonin superfamily peptides and insights into the evolutionary conservation and diversity of their structures

Highlights • Amphioxus, Branchiostoma floridae, possesses three calcitonin (CT) family peptides designated as B. floridae CT family peptides 1–3 (Bf-CTFP1–3). • Bf-CTFPs suppress the ostoclastic activity of goldfish scales via the CT receptor. • Bf-CTFPs and salmon CT share common essential amino ac...

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Veröffentlicht in:General and comparative endocrinology 2017-05, Vol.246, p.294-300
Hauptverfasser: Sekiguchi, Toshio, Shiraishi, Akira, Satake, Honoo, Kuwasako, Kenji, Takahashi, Hiroki, Sato, Masayuki, Urata, Makoto, Wada, Shuichi, Endo, Masato, Ikari, Takahiro, Hattori, Atsuhiko, Srivastav, Ajai K, Suzuki, Nobuo
Format: Artikel
Sprache:eng
Schlagworte:
Alpha-helix
Amino Acid Sequence
Amphioxus
Animals
Calcitonin
Calcitonin - genetics
Endocrinology & Metabolism
Goldfish - metabolism
Goldfish scales
Peptides - genetics
Receptor Activity-Modifying Proteins - metabolism
Structure-Activity Relationship
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Zusammenfassung:Highlights • Amphioxus, Branchiostoma floridae, possesses three calcitonin (CT) family peptides designated as B. floridae CT family peptides 1–3 (Bf-CTFP1–3). • Bf-CTFPs suppress the ostoclastic activity of goldfish scales via the CT receptor. • Bf-CTFPs and salmon CT share common essential amino acids for ligand activity. • The alpha-helical structure of Bf-CTFP1 and 2 is conserved with that of teleost CT. • Bf-CTFP3 has a unique alpha-helical structure.
ISSN:0016-6480
1095-6840
DOI:10.1016/j.ygcen.2017.01.004