Experimental Physiology
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Experimental Physiology 75.4 pp 529-536
© The Physiological Society 1990
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Experimental Physiology, Vol 75, Issue 4, 529-536
Copyright © 1990 by The Physiological Society


Article

Amylin-amide: a new bone-conserving peptide from the pancreas

M Zaidi, HK Datta, PJ Bevis, SJ Wimalawansa, and I MacIntyre

Amylin-amide is a new member of the family of peptides encoded by the calcitonin multigene complex. In the present study, we have compared directly, the hypocalcaemic potency and duration of action of human amylin-amide and human calcitonin in an in vivo rat bioassay and an in vitro osteoclast bone resorption assay. Amylin-amide was found to have a potency approximately 40-fold lower than human calcitonin, whilst both peptides followed the same time course. This suggests that amylin-amide is the most potent non-calcitonin hypocalcaemic peptide so far reported. An important physiological implication follows. It would seem that amylin-amide can play a central role in the maintenance of the skeleton by virtue of its inhibitory influence on osteoclastic function.





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Copyright © 1990 by the The Physiological Society.