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Characterization of two genes involv...

Squire, Teresa Lynn.

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Characterization of two genes involved in the switch from carbohydrate to lipid metabolism in a hibernating mammal.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Characterization of two genes involved in the switch from carbohydrate to lipid metabolism in a hibernating mammal./
作者:	Squire, Teresa Lynn.
面頁冊數:	203 p.
附註:	Chair: Matthew T. Andrews.
Contained By:	Dissertation Abstracts International62-12B.
標題:	Biology, Genetics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3037993
ISBN:	0493510737

Characterization of two genes involved in the switch from carbohydrate to lipid metabolism in a hibernating mammal.
Squire, Teresa Lynn.

Characterization of two genes involved in the switch from carbohydrate to lipid metabolism in a hibernating mammal. - 203 p.

Chair: Matthew T. Andrews.

Thesis (Ph.D.)--North Carolina State University, 2002.

Hibernating mammals rely primarily on lipid catabolism to generate the energy necessary for survival. This switch from carbohydrate catabolism during the active state to lipid catabolism during the hibernating state is not completely understood at the genetic level. Recently, we undertook the task of characterizing those genes that were differentially expressed during hibernation in the thirteen-lined ground squirrel, <italic>Spermophilus tridecemlineatus</italic>. The mRNAs of two genes, pyruvate dehydrogenase kinase-4 (<italic>PDK-4</italic>) and pancreatic triacylglycerol lipase (<italic> PTL</italic>), were found at increased levels in the heart during hibernation. An increase in PTL mRNA expression in the heart was associated with an increase in PTL protein level and PTL-mediated lipolytic activity during hibernation. Amazingly, PTL enzyme present in soluble heart extracts from hibernating squirrels maintained 60% activity at 7°C, a typical hibernating temperature. A comparison of lipolytic activity using recombinant ground squirrel and human PTL proteins demonstrated that both enzymes retained approximately 40% activity under similar conditions. Because both enzymes were expressed in the yeast <italic>Pichia pastoris</italic>, their capacity to hydrolyze triacylglycerols at low temperatures appears to be a property inherent in the primary structure of the enzyme in these organisms and is not the result of mammalian- or hibernation-specific modifications.

ISBN: 0493510737Subjects--Topical Terms:

1017730
Biology, Genetics.

Characterization of two genes involved in the switch from carbohydrate to lipid metabolism in a hibernating mammal.
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245 1 0 $a Characterization of two genes involved in the switch from carbohydrate to lipid metabolism in a hibernating mammal.
300 $a 203 p.
500 $a Chair: Matthew T. Andrews.
500 $a Source: Dissertation Abstracts International, Volume: 62-12, Section: B, page: 5511.
502 $a Thesis (Ph.D.)--North Carolina State University, 2002.
520 $a Hibernating mammals rely primarily on lipid catabolism to generate the energy necessary for survival. This switch from carbohydrate catabolism during the active state to lipid catabolism during the hibernating state is not completely understood at the genetic level. Recently, we undertook the task of characterizing those genes that were differentially expressed during hibernation in the thirteen-lined ground squirrel, <italic>Spermophilus tridecemlineatus</italic>. The mRNAs of two genes, pyruvate dehydrogenase kinase-4 (<italic>PDK-4</italic>) and pancreatic triacylglycerol lipase (<italic> PTL</italic>), were found at increased levels in the heart during hibernation. An increase in PTL mRNA expression in the heart was associated with an increase in PTL protein level and PTL-mediated lipolytic activity during hibernation. Amazingly, PTL enzyme present in soluble heart extracts from hibernating squirrels maintained 60% activity at 7°C, a typical hibernating temperature. A comparison of lipolytic activity using recombinant ground squirrel and human PTL proteins demonstrated that both enzymes retained approximately 40% activity under similar conditions. Because both enzymes were expressed in the yeast <italic>Pichia pastoris</italic>, their capacity to hydrolyze triacylglycerols at low temperatures appears to be a property inherent in the primary structure of the enzyme in these organisms and is not the result of mammalian- or hibernation-specific modifications.
520 $a A search for <italic>PTL</italic> gene expression in organs and tissues other than the heart led to the discovery of a longer form of the PTL message expressed in white adipose tissue (WAT). Sequencing of full-length cDNAs from heart and WAT revealed no homology in the 5<super>′</super>-untranslated regions of these two messages. The coding regions, however, were virtually identical in nucleotide sequence and were identical in amino acid sequence. Differences in the 5<super>′</super>-untranslated regions were attributable to segments of retroviral sequence found in the WAT message that were not present in the heart message. Southern blot analysis and sequencing of two genomic clones established that one gene was sufficient to account for both gene products.
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