Affiliation:
1. Laboratoire d'Etude des Regulations Physiologiques, National de laRecherche Scientifique, Strasbourg, France.
Abstract
The coincidence of fast and molt in penguins is an interesting condition for investigating the factors controlling protein metabolism; avian molt involves the utilization of amino acids for synthesis of new feathers, whereas a major factor for adaptation to fasting in birds, as for mammals, is reduction in net protein breakdown. Hormonal and biochemical changes were studied in seven molting king penguins. Their initial body mass was 18 kg. It decreased by 58% over 41 days of fasting. Feather synthesis lasted for the first 3 wk of the fast. It was marked by plasma concentrations of alanine and uric acid 1.5 to 2 times those for nonmolting fast, and plasma thyroxine was increased five times. At the completion of molt all these values returned to levels comparable to those in nonmolting fast. As indicated by high plasma levels of beta-hydroxybutyrate, lipid stores were mobilized readily during molting. The fast ended by a phase of enhancement in protein utilization that was characterized by a fivefold increase in uricacidemia and coincided with an 80% drop in plasma beta-hydroxybutyrate and a fourfold increase in plasma corticosterone. These data suggest that two different hormones control the two successive periods marked by an increased protein mobilization during the molting fast, i.e., thyroxine during feather growth and corticosterone toward the end of the fast, when the molt is completed.
Publisher
American Physiological Society
Subject
Physiology (medical),Physiology
Cited by
81 articles.
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