scholarly journals Transition from ectothermy to endothermy: the development of metabolic capacity in a bird ( Gallus gallus )

2005 ◽  
Vol 273 (1586) ◽  
pp. 565-570 ◽  
Author(s):  
Frank Seebacher ◽  
Tonia S Schwartz ◽  
Michael B Thompson
Keyword(s):  
Gene Expression ◽  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Aerobic Capacity ◽  
Anaerobic Capacity ◽  
Internal Heat ◽  
Gallus Gallus ◽  
Metabolic Capacity ◽  
Lactate Dehydrogenase Activity ◽  
Evolutionary Innovation

The evolution of endothermy is one of the most significant events in vertebrate evolution. Adult mammals and birds are delineated from their early ontogenetic stages, as well as from other vertebrates, by high resting metabolic rates and consequent internal heat production. We used the embryonic development of a bird ( Gallus gallus ) as a model to investigate the metabolic transition between ectothermy and endothermy. Increases in aerobic capacity occur at two functional levels that are regulated independently from each other: (i) upregulation of gene expression; and (ii) significant increases in the catalytic activity of the main oxidative control enzymes. Anaerobic capacity, measured as lactate dehydrogenase activity, is extremely high during early development, but diminishes at the same time as aerobic capacity increases. Changes in lactate dehydrogenase activity are independent from its gene expression. The regulatory mechanisms that lead to endothermic metabolic capacity are similar to those of ectotherms in their response to environmental change. We suggest that the phylogenetic occurrence of endothermy is restricted by its limited selective advantages rather than by evolutionary innovation.

Molecular mechanisms underlying the development of endothermy in birds (Gallus gallus): a new role of PGC-1α?

2007 ◽  
Vol 293 (6) ◽  
pp. R2315-R2322 ◽  
Author(s):  
Isabel Walter ◽  
Frank Seebacher
Keyword(s):  
Gene Expression ◽  
Molecular Mechanisms ◽  
Environmental Variability ◽  
Citrate Synthase ◽  
Incubation Temperature ◽  
Internal Heat ◽  
Gallus Gallus ◽  
Peroxisome Proliferator ◽  
Metabolic Capacity ◽  
Peroxisome Proliferator Activated Receptor

In endotherms, plasticity of internal heat production in response to environmental variability is an important component of thermoregulation. During embryogenesis endotherms cannot regulate their body temperature metabolically and are therefore similar to ectotherms. The transition from ectothermy to endothermy occurs by the development of metabolic capacity during embryogenesis. Here we test the hypothesis that the development of metabolism during embryogenesis in birds is under transcriptional control and that metabolic capacity is upregulated in colder environments. The peroxisome proliferator-activated receptor-γ (PPARγ) coactivator-1α (PGC-1α) is the major metabolic regulator in mammals. PGC-1α and its target PPARγ were significantly elevated during development in pectoral muscle and liver of chickens ( Gallus gallus) compared with adults. However, the timing of upregulation of PGC-1α and PPARγ was not in synchrony. In cool incubation temperatures (35°C) both PGC-1α and PPARγ gene expression was increased in liver but not in skeletal muscle, compared with a 38°C incubation treatment. Cytochrome c oxidase and citrate synthase enzyme activities and ATP synthase gene expression increased during embryonic development in liver and muscle, and there was a significant effect of incubation temperature on these parameters. Our findings suggest that PGC-1α might be important for establishing endothermic metabolic capacity during embryogenesis in birds.

Controlling the highest lactate dehydrogenase activity known in nature

1978 ◽  
Vol 234 (3) ◽  
pp. R136-R140 ◽  
Author(s):  
M. Guppy ◽  
P. W. Hochachka
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
White Muscle ◽  
Aerobic Glycolysis ◽  
Anaerobic Capacity ◽  
Creatine Phosphate ◽  
Quiescent State ◽  
Lactate Dehydrogenase Activity ◽  
Glycerophosphate Dehydrogenase ◽  
Glycolysis Regulation

In the shipjack, Euthynnus pelamis, white muscle appears to possess a powerful anaerobic capacity as well as a significant carbohydrate based aerobic potential. Lactate dehydrogenase occurs at higher activities than found thus far anywhere else in nature and clearly functions in anaerobic glycolysis. Alpha-glycerophosphate dehydrogenase also occurs in unusually high activities and appears to play a role in aerobic glycolysis. Regulation of these two reactions is accomplished by temperature, pH, and creatine phosphate levels. High temperature, low pH, and low creatine phosphate levels all appear to favor lactate dehydrogenase over alpha-glycerophosphate dehydrogenase; low temperature, high pH, and high creatine-phosphate levels, all expected during the quiescent state in this species, and when metabolism in aerobic, all favor alpha-glycerophosphate dehydrogenase activity.

Adaptation to temporary muscle anoxia in Anurans: Activities of glycolytic enzymes in muscles from species differing in their ability to produce lactate during exercise

1977 ◽  
Vol 25 (1) ◽  
pp. 15 ◽  
Author(s):  
J Baldwin ◽  
G Friedman ◽  
H Lillywhite
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Energy Production ◽  
Anaerobic Capacity ◽  
Glycolytic Enzymes ◽  
Lactate Dehydrogenase Activity ◽  
Anaerobic Energy ◽  
Specific Activities

Specific activities of the enzymes lactate dehydrogenase, phosphorylase, phosphofructokinase and hexokinase were determined in hind leg musculature taken from four species of anuran having different capacities for producing lactate during exercise. The specific activities of phosphorylase, phosphofructokinase, and the ratio phosphorylase: hexokinase were highest in animals having high increments of lactate following exercise, and lowest in those showing low increments. The specific activities of these glycolytic enzymes could possibly be used as an index of the reliance of different species on anaerobic energy production. Lactate dehydrogenase activity was not well correlated with anaerobic capacity.

Lactate dehydrogenase activity and its isoenzymes in concentric layers of adult bovine and calf lenses

1987 ◽  
Vol 6 (4) ◽  
pp. 555-560 ◽  
Author(s):  
David Sempol ◽  
Edurado Osinaga ◽  
Seymour Zigman ◽  
Israel Korc ◽  
Beatriz Korc ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Lactate Dehydrogenase Activity

Lactate Dehydrogenase Activity is Inhibited by Methylmalonate in vitro

2006 ◽  
Vol 31 (4) ◽  
pp. 541-548 ◽  
Author(s):  
Laura O. Saad ◽  
Sandra R. Mirandola ◽  
Evelise N. Maciel ◽  
Roger F. Castilho
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Lactate Dehydrogenase Activity
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