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In mammalian assay systems, calcitonin peptides of non-mammalian species exhibit stronger activity than those of mammals. Recently, comparative analyses of a wide-range of species revealed that platypus and opossum, which diverged early from other mammals, possess calcitonins that are more similar in amino acid sequence to those of non-mammals than mammals. We herein determined whether platypus and opossum calcitonins exhibit similar biological activities to those of non-mammalian calcitonins using an assay of actin ring formation in mouse osteoclasts. We also compared the dose-dependent effects of each calcitonin on cAMP production in osteoclasts. Consistent with the strong similarities in their primary amino acid sequences, platypus and opossum calcitonins disrupted actin rings with similar efficacies to that of salmon calcitonin. Human calcitonin exhibited the weakest inhibitory potency and required a 100-fold higher concentration (EC50=3×10-11M) than that of salmon calcitonin (EC50=2×10-13M). Platypus and opossum calcitonins also induced cAMP production in osteoclast cultures with the same efficacies as that of salmon calcitonin. Thus, platypus and opossum calcitonins exhibited strong biological activities, similar to those of the salmon. In addition, phylogenetic analysis revealed that platypus and opossum calcitonins clustered with the salmon-type group but not human- or porcine-type group. These results suggest that platypus and opossum calcitonins are classified into the salmon-type group, in terms of the biological activities and amino acid sequences. Copyright © 2017 Elsevier Inc. All rights reserved.


Teruhito Yamashita, Nobuyuki Udagawa, Gnanasagar Janardhanan Thirukonda, Shunsuke Uehara, Hirose Yamauchi, Nobuo Suzuki, Feng Li, Yasuhiro Kobayashi, Naoyuki Takahashi. Platypus and opossum calcitonins exhibit strong activities, even though they belong to mammals. General and comparative endocrinology. 2017 May 15;246:270-278

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PMID: 28062306

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