Biomedical subjects

D A Hood

Publications and source records attributed to D A Hood.

At least 37 records · Page 2Linked to original sources

PubMed1995

Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle.

Molecular chaperones and cytosolic stress proteins are actively involved in the stabilization, import and refolding of precursor proteins into mitochondria. The purpose of the present study was to evaluate the relationship between mitochondrial content under steady-state conditions, and during the induction of organelle biogenesis, with the expression of stress proteins and mitochondrial chaperonins. A comparison of steady-state levels of mitochondrial enzyme activity [cytochrome c oxidase (CYTOX)] with chaperonin levels [the heat-shock protein HSP60, the glucose-regulated protein GRP75 (mtHSP70)] in striated muscles possessing a wide range of oxidative capacities revealed a proportional expression between the two. This relationship was disrupted by chronic contractile activity brought about by 10 days of 10 Hz stimulation of the tibialis anterior (TA) muscle, which induced 2.4-fold increases in CYTOX activity, but 3.2- and 9.3-fold increases in HSP60 and GRP75 respectively. The inducible stress protein HSP70i was detected at low levels in control TA muscle, and was increased 9.6-fold by chronic contractile activity, to values comparable with those found in the unstressed soleus muscle. This increase occurred in the absence of changes in type I MHC levels, indicating independent regulation of these genes. Despite the increases in HSP60 and HSP70i proteins, contractile activity did not alter their respective mRNA levels, illustrating post-transcriptional mechanisms of gene regulation during contractile activity. In contrast, the mRNA levels encoding the co-chaperonin CPN10 were increased 3.3-fold by contractile activity. Thus, the expression of individual mitochondrial chaperonins is independently regulated and uncoordinated. The extent of the induction of these stress proteins and chaperonins by contractile activity exceeded that of membrane enzymes (e.g. CYTOX). It remains to be determined whether this marked induction of proteins comprising part of the protein import machinery is beneficial for the translocation of enzyme precursors into the mitochondria during conditions of accelerated biogenesis.

Animals↗

PubMed1995

Effect of hypothyroidism on the expression of cytochrome c and cytochrome c oxidase in heart and muscle during development.

The effect of thyroid hormone on the expression of mitochondrial proteins was evaluated during development by measuring cytochrome c oxidase (CYTOX) activity and cytochrome c protein and mRNA levels in heart and skeletal muscle of control and hypothyroid rats. Animals were killed at the late fetal, early, and late postnatal stages up to 56 days of age. In heart, CYTOX activity increased 2.3-fold above the fetal level throughout development, most of which occurred prior to 2 days of age. No increase was observed in muscle. CYTOX activity was reduced in hypothyroid animals throughout development in heart compared to controls (by 50% at 56 days), but in muscle no effect of hypothyroidism was observed. In muscle and heart 4- and 1.5-fold increases in cytochrome c above the fetal level were evident by 1 day of age, with further increases to 8.5- and 2.7-fold by 56 days, respectively. The increase in cytochrome c differed from the increase in CYTOX, indicating changes in mitochondrial composition. Hypothyroidism reduced cytochrome c in muscle by 30-35% at 56 days, but had no effect in heart, indicating a muscle type-specific effect of thyroid hormone on cytochrome c protein expression. Cytochrome c mRNA increased rapidly to 4-5 fold above the fetal level in both heart and muscle by 6 h post-partum. Between 7 and 56 days of age, further increases to 6- and 25-fold were observed in muscle and heart, respectively. In muscle, the 6-fold developmental increase in mRNA paralleled that of the protein, suggesting transcriptional regulation.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1995

Mitochondrial biogenesis during pressure overload induced cardiac hypertrophy in adult rats.

Existing literature provides an equivocal picture of the behavior of mitochondrial synthesis during the time course of cardiac hypertrophy. Therefore, we examined the effect of cardiac hypertrophy on mitochondrial cytochrome c oxidase (CYTOX) activity, the content of CYTOX subunit VIc mRNA, and the expression of molecular chaperones. Adult male Sprague-Dawley rats were subjected to either abdominal aortic constriction to induce pressure overload (PO) or a sham operation (SH). Animals were studied 2, 4, 7, 14, 21, or 28 days after surgery. Aortic constriction resulted in a significant evaluation in arterial pressure by 4 days after surgery. Significant (p < 0.05) hypertrophy was attained by 4 days and was stabilized at 37% between 7 and 28 days. CYTOX activity (U/g) did not differ significantly between PO and SH animals at either early (< 7 days) or later time points, indicating that mitochondrial content increased in proportion to adaptive cellular hypertrophic growth. The concentration of the molecular chaperones HSP60 and GRP75 involved in mitochondrial protein import did not change with PO treatment. The levels of mRNAs encoding both CYTOX subunit VIc and HSP60 remained constant, in proportion to cardiac growth. This suggests that the accelerated synthesis of CYTOX and HSP60 during cardiac hypertrophy is regulated transcriptionally. The data help to resolve the controversy in the literature regarding mitochondrial biogenesis during moderate, stable cardiac hypertrophy, and they indirectly indicate that proportional mitochondrial synthesis relative to cellular hypertrophy is regulated at the transcriptional level.

Animals↗

PubMed1995

Performance and excitability of mdx mouse muscle at 2, 5, and 13 wk of age.

Dystrophin is a 427-kDa protein localized adjacent to the sarcolemma in skeletal muscle. Its physiological role remains uncertain, although its absence is known to cause muscular dystrophy. In this study, the function of dystrophin was investigated using the dystrophin-deficient mdx mouse. Control and mdx animals at 2, 5, and 13 wk of age (n = 8-11/age) were compared to evaluate in situ gastrocnemius-plantaris-soleus muscle contractile, endurance, and excitability properties at nondegenerated, degenerated, and regenerated stages, respectively. Twitch and tetanic tensions expressed per gram of muscle mass were lower in mdx muscle only at 5 wk. Fatigue produced during successive contractions at 2, 10, and 20 Hz did not differ between the two groups at 2 and 5 wk but was lower in mdx muscle at 13 wk. This was not attributed to differences in mitochondria, since cytochrome-c oxidase activity was similar in mdx and control muscle. Contractile properties of control and mdx muscle became faster with age, and at 13 wk the time to peak twitch tension was shorter in mdx muscle relative to control, whereas the half-relaxation times did not differ. Mass action potential area (M wave), an index of muscle excitability, was not significantly different between mdx and control muscle at 2 or 5 wk but was greater in mdx muscle at 13 wk. Thus, in this weight-bearing muscle group, the lack of dystrophin has only a moderate impact in modifying muscle function relative to contractile properties, fatigability, or excitability.(ABSTRACT TRUNCATED AT 250 WORDS)

Aging↗

PubMed1995

Effects of hypothyroidism and aortic construction on mitochondria during cardiac hypertrophy.

We evaluated mitochondrial adaptations in the hearts of euthyroid and hypothyroid rats subject to aortic constriction for 2, 4, 7, 14, 21, and 28 d to induce a pressure-overload (PO), compared to sham-operated (SH) controls. PO animals attained higher arterial pressures than SH animals, by 55% in the euthyroid group, but only 14% in hypothyroid rats after 28 d. The left ventricle/body weight ratio was increased 44% by PO in the euthyroid group, and 26% in the hypothyroid group. PO attenuated the decline in cardiac growth in the hypothyroid group. Thus, hypothyroidism reduces the magnitude of the PO, but not the potential for hypertrophy in response to PO. Cytochrome c oxidase activity (CYTOX) was unchanged by PO in the euthyroid animals, indicating that the synthesis of mitochondria paralleled adaptive growth. However, CYTOX activity decreased up to 20% in the hypothyroid groups (P < 0.05) and was unaltered by PO. Thus, PO prevented the decline in growth, but not the decline in mitochondrial enzymes due to hypothyroidism. The lack of effect of PO on mitochondria was partly due to pretranslational changes since CYTOX subunit VIc mRNA was reduced by PO in the hypothyroid animals, but not in the euthyroid group. Levels of the chaperones HSP60 and GRP75, as well as HSP60 mRNA were unaffected by hypothyroidism, but paralleled adaptive growth induced by PO. Hypothyroidism changes the pattern of gene expression within the heart leading to altered mitochondrial composition. This cannot be compensated for by conditions of increased physiological demand.

Animals↗

PubMed1994

Endurance training alters alanine and glutamine release from muscle during contractions.

The release of alanine and glutamine from perfused muscle of trained and control animals was investigated. Release rates did not differ between trained and control muscle at rest. During contractions in trained muscle, alanine release was higher than at rest, while glutamine release was transiently increased. Phenylalanine release did not differ between trained and control muscle, implying that protein degradation was not increased in trained muscle. The muscle cellular adaptations to training include a selective modification of amino acid output, which could potentially influence gluconeogenic flux and alter muscle ammonia levels during contractions.

Alanine↗

PubMed1994

Mitochondrial biogenesis in striated muscle.

Mitochondrial biogenesis (synthesis) has been observed to occur in skeletal muscle in response to chronic use. It also occurs in cardiac muscle during growth and hypertrophy, and it may be impaired during the aging process. This review summarizes the literature on the processes of mitochondrial biogenesis at the biochemical and molecular levels, with particular reference to striated muscles. Mitochondrial biogenesis involves the expression of nuclear and mitochondrial genes and the coordination of these two genomes, the synthesis of proteins and phospholipids and their import into the organelle, and the incorporation of these lipids and proteins into their appropriate locations within the matrix, inner or outer membranes. The emphasis is on the regulation of these events, with information derived in part from other cellular systems. Although descriptions of mitochondrial content changes in heart and skeletal muscle during altered physiological states are plentiful, much work is needed at the molecular level to investigate the regulatory processes involved. A knowledge of biochemical and molecular biology techniques is essential for continued progress in the field. This is a promising area, and potential new avenues for future research are suggested.

Animals↗

PubMed1994

Blood flow, mitochondria, and performance in skeletal muscle after denervation and reinnervation.

Tibialis anterior (TA) muscles of rats underwent bilateral peroneal nerve crush (NC) or denervation (D) and were compared with sham-operated (SO) animals to determine the effect of reinnervation on blood flow, mitochondria, metabolites, and muscle performance. After surgery, animals were left for 2, 7, 21, or 42 days (NC and SO groups) or 2, 7, or 21 days (D group; n = 7-11.day-1.group-1), after which TA muscles were stimulated in situ at 1 Hz. alpha-Motoneuron reinnervation of muscle was complete 21 days after NC. Blood flow increased 10-fold above SO values in nonstimulated TA muscle 7 days after NC and D (P < 0.05). By 21 days, blood flow to nonstimulated TA muscle in NC animals returned to SO values but remained elevated (P < 0.05) in D muscle. Thus restoration of neural control of blood flow to resting muscle likely occurred by 21 days post-NC. Blood flow to stimulated muscle was not affected by NC or D, indicating the probable importance of metabolic factors in regulating blood flow during 1-Hz contractions. Cytochrome-c oxidase activity decreased (P < 0.05) below SO values 7 days after NC and D. By 21 days, cytochrome-c oxidase activity in TA muscles of NC animals returned to SO values, while values in denervated TA muscle continued to decrease. Despite these changes, endurance performance of TA muscle was not affected by D or NC at any time. These results suggest that reinnervation processes controlling blood flow and muscle function occur along similar time courses and that muscle blood flow is more closely related to endurance performance than is muscle oxidative capacity under these contraction conditions.

Animals↗

PubMed1993

delta-Aminolaevulinate synthase expression in muscle after contractions and recovery.

The synthesis of haem has been postulated to be a key regulatory step in muscle mitochondrial biogenesis. We examined the expression of delta-aminolaevulinate synthase (ALAs), the regulatory enzyme of haem metabolism, in 10 Hz electrically stimulated and non-stimulated control rat tibialis anterior (TA) muscle. ALAs activity and mRNA levels were measured at 0, 18 and 48 h of recovery after 3 h of acute stimulation, or after 7 days of stimulation (3 h/day). ALAs activity in control muscles averaged 7.8 +/- 0.8 nmol/h per g (n = 30). After 3 h of stimulation and during recovery, no change in ALAs activity occurred. ALAs mRNA during the same time was unchanged except at 48 h of recovery, when it increased 1.3-fold above control (P < 0.05). After 7 days of stimulation, ALAs activity was unchanged at 0 h, but increased at 18 and 48 h of recovery to 2.0- and 1.8-fold above control (P < 0.05). ALAs mRNA was also increased, but to a level averaging 1.6-fold above control (P < 0.05) at all times, indicating an increased mRNA stability or synthesis. No change in the haem-containing enzyme cytochrome c oxidase (CYTOX) activity occurred after 3 h of stimulation in the red section of the TA. After 7 days of stimulation, the increase in CYTOX activity averaged 1.7-fold above control (P < 0.05) at all times. Thus the induction of ALAs during recovery after 7 days was regulated by factors which not only change ALAs mRNA content, but which also affect ALAs mRNA at translational or post-translational steps. This induction occurred despite a 1.7-fold increase in CYTOX, implying that a precursor-product relationship does not always exist.

5-Aminolevulinate Synthetase↗

PubMed1993

Properties of skeletal muscle mitochondria isolated from subsarcolemmal and intermyofibrillar regions.

Two mitochondrial fractions, termed intermyofibrillar (IMF) and subsarcolemmal (SS), were isolated from skeletal muscle, and their biochemical properties were related to differences in respiration and mitochondrial protein synthesis. State III respiration was 2.3- to 2.8-fold greater in IMF than in SS mitochondria. Site 1 inhibition of respiration with rotenone reduced this difference to 1.4-fold. When sites 1 and 2 were inhibited with antimycin, the 1.4-fold differences remained. The activities of cytochrome-c oxidase (CYTOX) and succinate dehydrogenase (SDH) could account for some of these differences, since CYTOX was 20% greater (P < 0.05) in IMF mitochondria, and SDH was 40% greater (P < 0.05) in SS mitochondria. Cytochromes a, b, c, and c1 contents were similar in the two fractions. Cardiolipin (CL) content was higher (P < 0.05) in SS mitochondria, indicating a less dense mitochondrial fraction with respect to CL. In vitro [3H]leucine incorporation was 1.8-fold higher (P < 0.05) in IMF than in SS mitochondria. Thus compositional differences between IMF and SS fractions exist, perhaps representing mitochondria at different stages of biogenesis. The biochemical and functional differences could not solely be due to differences in mitochondrial protein synthesis but could also be due to nuclear-directed protein synthesis specific to each mitochondrial fraction.

Animals↗

PubMed1993

Chronic stimulation-induced changes in mitochondria and performance in rat skeletal muscle.

Chronic low-frequency (10-Hz) electrical stimulation was used to investigate mitochondrial biogenesis in rat tibialis anterior muscle. Succinate dehydrogenase and citrate synthase were used as mitochondrial enzymes, and cardiolipin (CL) was used as a phospholipid index of the inner membrane. Stimulation was via the peroneal nerve (24 h/day) for 1, 2, 3, 5, 7, 10, 14, 21, and 28 days (n = 3-9 rats/day). After each period, endurance performance was evaluated in situ. The contralateral side (CON) served as control nonstimulated muscle. Endurance performance gradually improved after 5 days of stimulation to approximately twofold higher than CON muscle beyond 10 days. Succinate dehydrogenase activity rose to 2.4-fold above CON muscle (4.8 +/- 0.2 U/g; n = 54) by 10 days (half time = 6.1 days) and then remained constant. Citrate synthase demonstrated a similar change. The improved performance with stimulation was correlated (r = 0.61, P < 0.05) to these increases in enzyme activities. CL concentration increased from CON (0.35 +/- 0.02 mumol/g; n = 30) to 3.6- and 3.8-fold above CON at 10 and 14 days (half time = 4.2 days). This increase in CL was greater (P < 0.05) than for either enzyme during the same period. These data are consistent with a model of mitochondrial membrane biogenesis in which enzyme proteins are inserted into a presynthesized lipid bilayer.

Animals↗

PubMed1993

Portable electrical stimulator for use in small animals.

The detailed electronic configuration of a lightweight (7 g) battery-operated portable electrical stimulator unit is described. It has proven useful for the study of the effects of chronic stimulation on skeletal muscle in small animals (i.e., the rat). The unit requires wavelengths in the infrared region for activation. This allows for remote triggering of the stimulator and permits it to function reliably even when animals are housed in rooms illuminated by fluorescent lamps. Unique to the system is the inclusion of a visual indicator of unit function (light-emitting diode), thus providing a convenient means of monitoring unit activation. The stimulator unit described has proven to be highly reliable and very useful for the study of alterations in gene expression in muscle subject to chronic use (M. Takahashi and D. A. Hood, J. Appl. Physiol. 74: 934-941, 1993).

Animals↗

PubMed1992

Mitochondrial adaptations to chronic muscle use: effect of iron deficiency.

1. The effects of chronic muscle use on mitochondrial structure, enzymes and gene expression is reviewed. The role of iron deficiency in modulating this adaptation is discussed. 2. Chronic muscle use and disuse alter mitochondrial composition and affect mitochondrial subpopulations differentially. This has implications for an understanding of organelle assembly. 3. Iron deficiency decreases mitochondrial functional mass within muscle by reducing the level of heme and non-heme iron-containing components. This alters the metabolic response during exercise and results in a reduced endurance performance. 4. Both iron deficiency and chronic muscle use represent contrasting experimental models for the study of mitochondrial function and biogenesis.

Adaptation, Physiological↗

PubMed1992

Effect of thyroid status on the expression of metabolic enzymes during chronic stimulation.

The effect of thyroid status on the expression of cytochrome c oxidase (CYTOX) and the activities of citrate synthase (CS) and phosphofructokinase (PFK) were examined in chronically stimulated (10 Hz; 35 days) and contralateral, nonstimulated rat tibialis anterior muscle of hypothyroid, hyperthyroid, and euthyroid animals. Stimulation increased CYTOX activity by 2.7-, 3.2-, and 4.9-fold in hyperthyroid, euthyroid, and hypothyroid animals, respectively, to similar absolute values. CS displayed similar increases. Stimulation reduced PFK activity in hypothyroid and euthyroid animals to 45% and 60% of control values. This effect was abolished with hyperthyroidism. Thus stimulation and thyroid hormone act antagonistically on PFK activity. Stimulation increased CYTOX subunit III (mitochondrially encoded) mRNA by 2.5- and 2.9-fold in hyperthyroid and euthyroid animals. Similar increases were observed in the nuclear-encoded mRNAs of CYTOX subunit VIc in euthyroid muscle. In hyperthyroid and euthyroid conditions, the mRNA changes paralleled the increases in enzyme activity. In hypothyroid muscle, the increase in mRNA was less for subunit VIc than III, suggesting that hypothyroidism upsets the coordinate expression of nuclear and mitochondrial genes. Further, the increases in CYTOX activity exceeded that of both subunit mRNAs in hypothyroid muscle.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1991

Metabolic and contractile responses of rat fast-twitch muscle to 10-Hz stimulation.

Contractile and metabolic responses of rat fast-twitch gastrocnemius-plantaris muscles were studied. Acute in situ 10-Hz stimulation (STIM) for two 60-min periods, separated by 60 min of recovery (REC), was used. Muscles were removed at 1, 3, 15, 60, 75, 120, 123, or 180 min for metabolite measurements. Twitch and tetanic tensions were reduced to 36 and 28% of initial during the first 60 min of STIM. During REC, these tensions returned only to 56-58% of initial by 120 min. These contractile responses did not parallel changes in metabolites in mixed muscle. pH was reduced from 7.0 to 6.4 by 1 min, but by 15 min of STIM had returned to resting levels. Free ADP and AMP increased 3- and 15-fold during STIM, then decreased to resting levels by 3 min of REC. The most sensitive indicator of metabolic stress during STIM and REC was the phosphorylation potential, which varied up to 40-fold. After initial phases of depletion, ATP and phosphocreatine levels were partially restored despite ongoing STIM. Approximately 75% of the change in ATP level could be accounted for by IMP. In red gastrocnemius [fast-twitch red (FTR)] muscle, IMP was increased by 3 min of STIM but returned to control values by 60 min. Thus reamination of IMP occurred during contractions of FTR muscle. Metabolic and contractile responses during the second STIM period (120-180 min) were similar to the first. This cycle of metabolic and contractile responses occurs in fast-twitch muscle which, with chronically repeated STIM and REC periods, undergoes large phenotypic changes as a result of use.

Adenine Nucleotides↗

PubMed1991

Mitochondrial adaptations in denervated muscle: relationship to muscle performance.

We have studied mitochondrial adaptations in muscle subject to chronic denervation, and their relationship to muscle performance, using a model of unilateral sciatic nerve denervation in rats over periods of 2, 5, 8, 14, 21, 28, 35, and 42 days (n = 5-9 rats/day). Time to peak tension (TPT), one-half relaxation time (1/2RT), and endurance performance were evaluated during in situ stimulation of denervated and contralateral gastrocnemius-plantaris muscles. Denervation led to a 70% decline in muscle mass after 42 days. TPT and 1/2RT increased 17 and 30%, respectively, indicating a transformation toward slower muscle. The activities of the enzymes cytochrome-c oxidase (CYTOX), succinate dehydrogenase, and citrate synthase were decreased by 8-14 days, and by 42 days these were 34-58% of control. The mitochondrial phospholipid cardiolipin was reduced earlier, by 5 days, and gradually decreased to 37% of control. Thus phospholipid removal appears to precede the loss of enzyme activity during decreases in mitochondrial content. Endurance performance was reduced in parallel with decreases in enzyme activity and cardiolipin. Cytochrome c mRNA levels decreased to 52% of control by 5 days. Denervation resulted in coordinated changes in mRNA levels encoding the nuclear-derived CYTOX subunit VIc and the mitochondrially derived CYTOX subunit III. However, changes in CYTOX activity did not always parallel alterations in subunit mRNA levels. Thus transcriptional and translational mechanisms operate in regulating mitochondrial gene expression during denervation.

Animals↗

PubMed1991

Effect of alpha-ketoacid dehydrogenase phosphorylation on branched-chain amino acid metabolism in muscle.

The regulation of leucine and valine metabolism was evaluated in skeletal muscle of perfused rat hindlimb. Control of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) via phosphorylation was removed with 0.4 mM alpha-chloroisocaproate (CIC). CIC activated the BCKADH complex 13- to 26-fold and led to increased rates of leucine and valine uptake into muscle, transamination to the corresponding alpha-ketoacid, and leucine (3- to 4-fold) and valine (6-fold) decarboxylation but led to decreased rates of alpha-ketoacid efflux from muscle. Although the increased rates of branched-chain amino acid (BCAA) decarboxylation were extensive, they were far below the extent of BCKADH activation as measured in vitro, suggesting that factors other than BCKADH activation become dominant in controlling the flux through alpha-ketoacid decarboxylation in skeletal muscle in situ. When the BCKADH capacity of muscle was increased 70-90% by a training-induced increase in mitochondrial content, the same 13- to 26-fold activation of the complex by CIC led to a rate of BCAA decarboxylation, which was only marginally greater (10-20%; P less than 0.05) than that of normal muscle. In addition, increasing the energy demand via muscle contractions led to a significant increase in leucine decarboxylation in the presence of complete activation of BCKADH by dephosphorylation. Thus BCKADH phosphorylation-dephosphorylation plays an important though not exclusive role in modulating the rates of BCAA metabolism in skeletal muscle. Differences in valine and leucine metabolism were apparent as valine catabolism bolstered citric acid cycle contents by increasing malate in red muscle with high mitochondrial content.(ABSTRACT TRUNCATED AT 250 WORDS)

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗

PubMed1990

Co-ordinate expression of cytochrome c oxidase subunit III and VIc mRNAs in rat tissues.

Cytochrome c oxidase (EC 1.9.3.1) is an enzyme which is composed of subunits derived from both the mitochondrial and the nuclear genomes. To determine whether or not the expression of these two genomes is co-ordinated at the mRNA level, we have examined the steady-state levels of mRNAs coding for cytochrome c oxidase subunit III (mitochondrially encoded) and subunit VIc (nuclear-encoded) in rat tissues. This was compared with the tissue concentration of the holoenzyme, which was estimated by measuring cytochrome c oxidase enzyme activity. The tissues (heart, brain, liver, kidney, soleus muscle and superficial white vastus muscle) possessed a 13-fold range of enzyme activity, which was highest in heart and lowest in the superficial vastus muscle. Specific subunit mRNA levels were quantified by using slot-blot hybridization of cDNA probes to total tissue RNA. The highest values for subunit III and Vlc mRNA tissue contents were found in kidney, followed by liver and heart (40-60% of that of kidney). The white vastus muscle contained the lowest subunit mRNA level (15% of that of kidney). Although some variability was apparent within each tissue, a parallel pattern of mRNA expression of the nuclear- and mitochondrially encoded subunits was observed. Differences between muscle (heart, vastus and soleus) and non-muscle tissues were noted in the relationship between mRNA and protein levels of expression. Thus, although this suggests that tissue-specific regulatory processes operate, the steady-state expression of subunit III and subunit Vlc mRNAs appears to be co-ordinately regulated.

Animals↗