2016
DOI: 10.1007/s13105-016-0528-y
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PEPCK-C reexpression in the liver counters neonatal hypoglycemia in Pck1 del/del mice, unmasking role in non-gluconeogenic tissues

Abstract: Whole body cytosolic phosphoenolpyruvate carboxykinase knockout (PEPCK-C KO) mice die early after birth with profound hypoglycemia therefore masking the role of PEPCK-C in adult, non-gluconeogenic tissues where it is expressed. To investigate whether PEPCK-C deletion in the liver was critically responsible for the hypoglycemic phenotype, we reexpress this enzyme in the liver of PEPCK-C KO pups by early postnatal administration of PEPCK-C-expressing adenovirus. This maneuver was sufficient to partially rescue h… Show more

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Cited by 14 publications
(5 citation statements)
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“…PCK1 is involved in gluconeogenesis and is a crucial enzyme in glucose metabolism in the body [19]. Indeed, PCK1-knockout mice die early after birth with profound hypoglycemia [20], which was partially rescued by the overexpression of PCK1 in the liver [21]. Therefore, gluconeogenesis under the control of PCK1 in the liver is crucial to avoid hypoglycemia.…”
Section: Discussionmentioning
confidence: 99%
“…PCK1 is involved in gluconeogenesis and is a crucial enzyme in glucose metabolism in the body [19]. Indeed, PCK1-knockout mice die early after birth with profound hypoglycemia [20], which was partially rescued by the overexpression of PCK1 in the liver [21]. Therefore, gluconeogenesis under the control of PCK1 in the liver is crucial to avoid hypoglycemia.…”
Section: Discussionmentioning
confidence: 99%
“…PCK1 is involved in gluconeogenesis and is a crucial enzyme in glucose metabolism in the body [ 22 ]. Indeed, PCK1 -knockout mice die early after birth with profound hypoglycemia [ 23 ], which was partially rescued by the overexpression of PCK1 in the liver [ 24 ]. Therefore, gluconeogenesis under the control of PCK1 in the liver is crucial to avoid hypoglycemia.…”
Section: Discussionmentioning
confidence: 99%
“…PCK1 catalyzed oxaloacetate to phosphoenolpyruvate via GTP and then released GDP for energy metabolism [79]. This biological process could produce glycerol to regulate adipogenesis [80]. Additionally, PCK1 was a target gene of PPARγ and regulated phosphoenolpyruvate through the PPARγ signaling pathway to affect the production of FAs [81], indicating PCK1 could interact with PPARγ to participate in the processes concerning fat deposition [82].…”
Section: Discussionmentioning
confidence: 99%