Publication Date
2009
Document Type
Thesis
Committee Members
David Goldstein (Advisor), Barbara Hull (Committee Member), Roberta Pohlman (Committee Member)
Degree Name
Master of Science (MS)
Abstract
Previous studies show that aquaporin HC-3 in gray tree frogs, Hyla chrysoscelis, a homolog of mammalian AQP3 is an aqua glyceroporin also responsible for freeze tolerance. Our study tried to localize and compare the protein expression levels of aquaporin HC-3 in seven different organs of gray tree frogs under five different physiological conditions using immuno histofluorescence and western blot. HC-3 was immunolocalized in the epidermis and dermis of the skin, basolateral portion of the collecting ducts in the kidney, red blood cells in the liver and other tissues, muscle Schwann cells and the basolateral portion of the large intestine epithelial membrane. HC-3 cannot be immunolocalized in the stomach and the small intestine tissues. The basolateral expression of aquaporin HC-3 in the epidermis of the skin is similar to the expression in the mammalian skin. The intensity of the labeling was different in the various physiological conditions. There was a noticeable increase in the intensity of the HC-3 expression in warm (hydrated, 23° C, control) skin, kidney and liver compared to dehydrated (loss of 20% of standard body mass over one week at 23° C) and the cold ( hydrated 4° C). The intensity of labeling in large intestine had varied pattern with more expression in the warm, slightly less in the cold and absolutely negligible in the other conditions. The up-regulation of the aquaporin HC-3 protein expression in the dehydrated skin and the kidney may be due to its regulated role in the water conservation whereas its up-regulation in the cold liver can be due to synthesis and release of glycerol in this organ.
Page Count
87
Department or Program
Department of Biological Sciences
Year Degree Awarded
2009
Copyright
Copyright 2009, all rights reserved. This open access ETD is published by Wright State University and OhioLINK.