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coactivator-1
expression during thyroid hormone-
and contractile activity-induced mitochondrial adaptations
School of Kinesiology and Health Science, and Department of Biology, York University, Toronto, Ontario, Canada M3J 1P3
The transcriptional coactivator the
peroxisome proliferator-activated receptor 
coactivator-1
(PGC-1) has been identified as an important mediator of
mitochondrial biogenesis based on its ability to interact with
transcription factors that activate nuclear genes encoding
mitochondrial proteins. The induction of PGC-1 protein expression
under conditions that provoke mitochondrial biogenesis, such as
contractile activity or thyroid hormone (T3) treatment, is
not fully characterized. Thus we related PGC-1 protein expression to
cytochrome c oxidase (COX) activity in 1) tissues
of varying oxidative capacities, 2) tissues from animals treated with T3, and 3) skeletal muscle subject
to contractile activity both in cell culture and in vivo. Our results
demonstrate a strong positive correlation (r = 0.74;
P < 0.05) between changes in PGC-1 and COX
activity, used as an index of mitochondrial adaptations. The highest
constitutive levels of PGC-1 were found in the heart, whereas the
lowest were measured in fast-twitch white muscle and liver.
T3 increased PGC-1 content similarly in both fast- and
slow-twitch muscle, as well as in the liver, but not in heart.
T3 also induced early (6 h) increases in AMP-activated protein kinase (AMPK) activity, as well as later (5 day) increases in p38 MAP kinase activity in slow-twitch, but not in fast-twitch, muscle. Contractile activity provoked early increases in PGC-1, coincident with increases in mitochondrial transcription factor A
(Tfam), and nuclear respiratory factor-1 (NRF-1) protein expression, suggesting that PGC-1 is physiologically important in coordinating the expression of the nuclear and mitochondrial genomes.
Ca2+ ionophore treatment of muscle cells led to an
approximately threefold increase in PGC-1 protein, and contractile
activity induced rapid and marked increases in both p38 MAP kinase and
AMPK activities. 5-Aminoimidazole-4-carboxamide-1-
-D-ribofuranoside
(AICAR) treatment of muscle cells also led to parallel increases in
AMPK activity and PGC-1 protein levels. These data are consistent
with observations that indicate that increases in PGC-1 protein are
affected by Ca2+ signaling mechanisms, AMPK activity, as
well as posttranslational phosphorylation events that increase PGC-1
protein stability. Our data support a role for PGC-1 in the
physiological regulation of mitochondrial content in a variety of
tissues and suggest that increases in PGC-1 expression form part of
a unifying pathway that promotes both T3- and contractile
activity-induced mitochondrial adaptations.
peroxisome proliferator-activated receptor-; peroxisome
proliferator-activated receptor- coactivator-1; mitochondrial
biogenesis; exercise; AMP-activated protein kinase; p38 MAP kinase; cytochrome c oxidase; mitochondrial transcription factor A; nuclear
respiratory factor-1; skeletal muscle
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