Biomedical subjects

R L Terjung

Publications and source records attributed to R L Terjung.

At least 19 recordsLinked to original sources

PubMed1992

AMP deaminase binding in contracting rat skeletal muscle.

AMP deaminase, which hydrolyses AMP to inosine 5'-monophosphate (IMP) and NH3 at high rates during excessive energy demands in skeletal muscle, is activated when bound to myosin in vitro. We evaluated AMP deaminase binding in vivo during muscle contractions to assess whether binding 1) is inherent to deamination and found only with high rates of IMP production or simply coincident with the contractile process and 2) requires cellular acidosis. AMP deaminase activity (mumol.min-1.g-1) was measured in the supernatant (free) and 10(4)-g pellet (bound) homogenate fractions of muscle of anesthetized rats after in situ contractions to determine the percent bound. In resting muscle, nearly all (approximately 90%) AMP deaminase is free (cytosolic). During contractions when energy balance was well maintained, binding did not significantly differ from resting values. However, during intense contraction conditions that lead to increased IMP concentration, binding increased to approximately 60% (P less than 0.001) in fast-twitch and approximately 50% in slow-twitch muscle. Binding increased in an apparent first-order manner and preceded initiation of IMP formation. Further, binding rapidly declined within 1 min after cessation of intense stimulation, even though the cell remained extremely acidotic. Extensive binding during contractions was also evident without cellular acidosis (iodoacetic acid-treated muscle). Thus the in vivo AMP deaminase-myosin complex association/dissociation is not coupled to changes in cellular acidosis. Interestingly, binding remained elevated after contractions, if energy recovery was limited by ischemia. Our results are consistent with myosin binding having a role in AMP deaminase activation and subsequent IMP formation in contracting muscle.

AMP Deaminase↗

PubMed1992

Altered kinetics of AMP deaminase by myosin binding.

AMP deaminase catalyzes the deamination of AMP to inosine 5'-monophosphate (IMP) and ammonia. Factors controlling the enzyme in muscle can rapidly promote high rates of IMP formation when ATP utilization exceeds supply. We evaluated whether binding of AMP deaminase to myosin, which occurs during intense contraction conditions, alters the kinetic behavior of the enzyme. Reaction kinetics of myosin-bound and free AMP deaminase were evaluated. Reaction kinetics of the free enzyme yielded a near-linear double-reciprocal plot with an expected Km of approximately 1 mM AMP concentration (AMP). In contrast, reaction kinetics of AMP deaminase became bimodal when bound to myosin. At [AMP] less than 0.15 mM, a high-affinity Km (0.05-0.10 mM) with maximal velocity approximately 20% that of free enzyme was evident. At [AMP] greater than 0.15 mM, the Km and maximal velocity values were similar to that of the free enzyme. The 10- to 20-fold higher affinity Km would allow for a higher rate of AMP deamination at the low [AMP] found physiologically. AMP deaminase binding to myosin also induced a marked resistance to orthophosphate inhibition (10 mM) in the presence of 50 microM ADP. Results were similar for purified preparations of AMP deaminase bound to myosin subfragment 2 and crude extracts obtained from contracting muscle. Our results add further support to the hypothesis that AMP deaminase binding to myosin serves an important role in control of enzyme activity in contracting muscle.

AMP Deaminase↗

PubMed1991

Adenine nucleotide synthesis in exercising and endurance-trained skeletal muscle.

Strenuous exercise leads to increased efflux of purine nucleoside and base that should necessitate recovery of adenine nucleotides by either the de novo synthesis or salvage pathway. De novo synthesis of adenine nucleotide was measured in quiescent and contracting muscle of sedentary and exercise-trained rats using an isolated perfused hindquarter preparation. Synthesis rates were assessed by measuring the incorporation of [1-14C]glycine into adenine nucleotide in muscles of both resting and stimulated hindlimbs after 1 h of either low- or high-energy demand isometric contractions. In nonstimulated sedentary and trained muscles, rates of de novo synthesis were similar. The effect of muscle contractions on de novo synthesis varied among muscle fiber types. Contracting, nonfatigued fast-twitch muscle sections showed significant declines in de novo synthesis in both sedentary and trained groups. Rates in slow-twitch red fibers and fatigued fast-twitch white fiber sections were not different from rest. Supplementing the perfusate with 5 mM ribose caused de novo synthesis to rise three- to fourfold in each of the fiber sections. However, the response in synthesis rates due to exercise was similar with or without ribose supplementation. De novo synthesis does not increase during exercise but exhibits an unchanged or reduced rate depending on the expected energy balance within the cell. This would occur if the energy state of muscle exerts significant control over de novo synthesis of adenine nucleotide.

Adenine Nucleotides↗

PubMed1991

Functional and metabolic consequences of skeletal muscle remodeling in hypothyroidism.

Functional and metabolic responses of hypothyroid skeletal muscle were evaluated during steady-state isometric contraction conditions, using an isolated perfused rat hindlimb preparation. Treating rats with propylthiouracil (PTU) for 4-5 mo resulted in a 55% decrease (P less than 0.001) in citrate synthase activity in plantaris muscle and phenotypic remodeling of the plantaris, evident by a threefold increase in type I fiber area and a 13% decrease in type II fiber area. Perfusion of PTU (n = 9) and control (n = 9) rat hindlimbs of similar size, with similar inflow (approximately 10 ml/min) and oxygen content (approximately 20 g/100 ml), resulted in similar oxygen deliveries to the contracting muscles (PTU 11.4 +/- 0.58, control 9.54 +/- 0.75 mumol.min-1.g-1; P greater than 0.05). Ten-minute tetanic contraction (100 ms at 100 Hz) periods at 4, 8, 15, 30, and 45 tetani/min were elicited in consecutive ascending order. Oxygen consumption (VO2) was lower in the PTU group at all contraction frequencies (P less than 0.005), with a decrease in peak VO2 of 44% (PTU 3.01 +/- 0.29, control 5.35 +/- 0.42 mumol.min-1.g-1; P less than 0.001). Oxygen extraction by the PTU muscle was only approximately 25% of that delivered. Developed tension was initially less (15%; P less than 0.05) in the PTU group but declined in a similar manner, as a percent of initial, to that of the control group. The slightly lower absolute tension development of the PTU muscle could not account for the large reduction in VO2.(ABSTRACT TRUNCATED AT 250 WORDS)

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)↗

PubMed1991

Muscle adaptations in trained rats with peripheral arterial insufficiency.

The influence of training adaptations, induced within the active muscles of rats with peripheral arterial insufficiency, was assessed with an isolated hindlimb preparation. Femoral artery-stenosed rats, showing symptoms of intermittent claudication, were trained for 14-20 wk by running at 20-35 m/min up a 15% grade for up to approximately 1 h/day, 5 days/wk. Similar total hindlimb blood flows (12.6 ml/min) at a similar arterial O2 content (20.7 vol/100 ml) yielded similar blood flows (95-117 ml.min-1.100 g-1) and O2 deliveries (9-11 mumol.min-1.g-1) to the contracting muscle of sedentary (n = 10) and trained (n = 10) rats. Ten-minute periods of tetanic contractions (100 ms at 100 Hz each) at 4, 8, 13, 45, 60, and 90 tetani/min were used. Muscle force development was better maintained (P less than 0.001) by the trained group. Higher peak O2 consumption (P less than 0.01) of the trained (5.69 +/- 0.53 mumol.min-1.g-1) compared with the sedentary group (3.66 +/- 0.26 mumol.min-1.g-1) involved a greater O2 extraction, since delivery of O2 was not different between groups. Thus adaptations occurred within trained muscle to enhance performance and peak O2 consumption. Muscle citrate synthase activity, an index of mitochondrial content, was greater (P less than 0.005) in the trained group, with the low-oxidative white muscle section exhibiting the greatest change (approximately threefold sedentary). Adaptations in this section were probably realized functionally, since improvements in muscle performance were evident early in the contraction sequence.(ABSTRACT TRUNCATED AT 250 WORDS)

Adaptation, Physiological↗

PubMed1991

Training-induced muscle adaptations: increased performance and oxygen consumption.

An isolated perfused rat hindlimb preparation was used to study the impact of local muscle adaptations induced by endurance exercise training on muscle performance and peak muscle oxygen consumption. Rats were trained for 12-15 wk by a running program (30 m/min up a 15% grade for 1 h/day 5 days/wk) shown previously to increase muscle mitochondrial enzyme activity. Sedentary (n = 11) and trained (n = 11) hindlimbs of similar size were perfused with a similar inflow (12.1 ml/min) at a similar oxygen content (18.1 ml O2/100 ml blood). Tetanic contractions (100 ms at 100 Hz) at 4, 8, 15, 30, 45, and 60/min were elicited in consecutive order. Initial tension was better maintained by muscles of trained animals at all frequencies above 4 tetani/min (P less than 0.05). Oxygen consumption (mumol.min-1.g-1) increased similarly in both groups at the lower contraction frequencies but was greater (P less than 0.05) in the trained [3.52 +/- 0.32 (SE)] than in the sedentary (2.44 +/- 0.31) group at 60 tetani/min. The peak oxygen consumption of the trained group (3.93 +/- 0.27) was 20% greater (P less than 0.05) than that of the sedentary group (3.28 +/- 0.28) when peak values for each animal, irrespective of the contraction condition, are compared. Blood flows to the contracting muscle (approximately 100 ml.min-1.g-1) and, therefore, oxygen deliveries (mumol.min-1.g-1) were not different between sedentary (7.99 +/- 0.56) and trained groups (8.35 +/- 0.61). Thus the 20% higher peak oxygen consumption was achieved by a greater oxygen extraction.(ABSTRACT TRUNCATED AT 250 WORDS)

Adaptation, Physiological↗

PubMed1991

Low-intensity training produces muscle adaptations in rats with femoral artery stenosis.

The effectiveness of a mild-intensity exercise program to induce adaptations within skeletal muscle of animals with peripheral arterial insufficiency was evaluated using an isolated perfused hindlimb preparation at a muscle blood flow similar to the peak found in vivo. Adult rats were subjected to bilateral femoral artery stenosis sufficient to limit peak blood flow during exercise but not alter resting blood flow. Stenosed-trained (Sten-Trained) rats walked on a treadmill at an easily achieved speed (20 m/min with a 15% grade) 5 days wk. Exercise tolerance improved from 10 min initially to 2 h/day. Non-stenosed-sedentary (Non-Sten-Sed) and stenosed-sedentary (Sten-Sed) animals were limited to cage activity. Oxygen delivery to the contracting muscles was similar among groups (7.0 +/- 0.4, 7.3 +/- 0.6, and 6.6 +/- 0.6 mumol.min-1.g-1 in Non-Sten-Sed, Sten-Sed, and Sten-Trained, respectively; n = 13 each). Force development was better maintained by Sten-Trained muscle (P less than 0.001) during a sequence of tetanic contraction conditions. Peak oxygen consumption was greater (P less than 0.05) in the Sten-Trained (5.23 +/- 0.34 mumol.min-1.g-1) than in Non-Sten-Sed (4.08 +/- 0.35) and Sten-Sed (4.34 +/- 0.37) rats. The increased peak oxygen extraction (P less than 0.05) by the muscle of the Sten-Trained rats (82.5 +/- 7.1% of oxygen inflow vs. 58.7 +/- 4.7 and 57.4 +/- 5.0%, respectively) was probably related to the increased muscle capillarity and mitochondrial enzyme activity.(ABSTRACT TRUNCATED AT 250 WORDS)

Adaptation, Physiological↗

PubMed1991

Adenine nucleotide metabolism in contracting skeletal muscle.

During steady-state muscle contractions, ATP production and utilization are well matched. When the rate of ATP hydrolysis exceeds the capacity of a given muscle fiber to phosphorylate ADP, the ADPf and AMPf concentrations rise, first leading to the deamination of adenylates and subsequently to the dephosphorylation of AMP or IMP, or both, to their respective nucleosides and bases. Several proposed roles for the purine nucleotide cycle in skeletal muscle have been reviewed and evaluated. The deaminating limb of the purine nucleotide cycle is most important; it maintains the ATP/ADP ratio and lessens adenine nucleotide degradation. Regulation of glycolytic pathway enzymes by the products of AMP deamination (IMP and NH4+) does not seem likely. During reamination there is a net production of fumarate, with the branch-chain amino acids potentially supplying a significant fraction of the amine; reamination, however, is probably not concurrent with a high rate of deamination. Evidence from some studies of AMP deaminase-deficient persons suggests that an intact purine nucleotide cycle is required for normal muscle function during intense exercise; the issue is clouded, however, by the occurrence of asymptomatic AMP deaminase deficiency. Skeletal muscle is capable of extensive adenine nucleotide degradation during severe, energy-depleting conditions. Purine nucleosides and bases not reincorporated by the salvage pathway must be synthesized de novo. The capacity for de novo synthesis differs among fiber types, being highest in muscle with the highest oxidative capacity.

Adenine Nucleotides↗

PubMed1990

The influence of pentoxifylline and torbafylline on muscle blood flow in animals with peripheral arterial insufficiency.

The potential of pentoxifylline to enhance blood flow to relatively ischemic muscle during running was evaluated in rats with peripheral arterial insufficiency. Femoral artery stenosis, sufficient to limit exercise hyperemia but not affect resting blood flow, was surgically induced in adult male rats (approximately 350 g). Day three after stenosis, rats were assigned to either a control (N = 14) or treatment (N = 14) group and exercised 5 days a week for 3 weeks. Exercise tolerance of rats fed pentoxifylline (34 +/- 1.3 mg/kg/day) or an analog (torbafylline; 34 +/- 2.3 mg/kg/day) increased more (P less than .001) than control rats in the third week of treatment. This was evidenced by a higher treadmill speed and longer duration of running. Blood flows determined with 85Sr and 141Ce labeled 15 mu spheres at low (20 m/min) and high (30-35 m/min) treadmill speeds were similar for each group and approximately 50% of that found in normal nonstenosed rats. Blood flows to the entire hindlimb, to the proximal and distal hindlimb segments, and to individual muscle fiber sections were not different between control and pentoxifylline groups. Thus, the increase in exercise tolerance could not be attributed to an increase in muscle blood flow. Rather, an enhanced oxygen extraction by the working limb muscles should lead to the increased VO2, required by the faster running speed in the pentoxifylline rats. This suggests that pentoxifylline may act to improve microvascular flow heterogeneity in working muscle. Our findings support clinical evidence that pentoxifylline is effective in managing patients with peripheral arterial insufficiency.

Animals↗

PubMed1990

Adenine nucleotide degradation in striated muscle.

Adenine nucleotides play a central role in cellular processes involving the transduction of energy. Among striated muscles, the management of adenine nucleotide catabolism differs greatly. These differences can be understood by considering the distribution, activity, and kinetic characteristics of degradative enzymes. When these factors are weighed in light of the differing energetic demands faced by heart and skeletal muscle fiber types, a coherent picture emerges. Our analysis suggests that, as the routine energy demand of a particular muscle rises in relation to the tissue's capacity for oxidative metabolism, the pattern of adenine nucleotide degradation shifts toward increased rates of AMP deamination along with lessened rates of dephosphorylation.

5'-Nucleotidase↗

PubMed1990

Adenine nucleotide degradation in slow-twitch red muscle.

The catabolism of adenine nucleotides (AdN) in rat soleus muscle (predominantly slow twitch) is very different from that in fast-twitch muscle. AMP deaminase is highly inhibited during brief (3 min) intense (120 tetani/min) in situ stimulation, resulting in little inosine 5'-monophosphate (IMP) accumulation (0.21 mumol/g). Even with ligation of the femoral artery during the same brief intense contraction conditions there is surprisingly little increase in IMP (0.37 mumol/g), although AdN depletion is evident (-1.30 mumol/g). We have tested the hypothesis that accumulation of purine nucleosides and bases accounts for the AdN depletion by measuring purine degradation products using high-performance liquid chromatography. There was no stoichiometric accumulation of purine degradation products to account for the observed AdN depletion even though metabolite recovery was essentially quantitative. We hypothesis that under these conditions AdN are converted to a form different from purine nucleoside and base degradation products. In contrast to the inhibition of AMP deamination seen during brief ischemia, slow-twitch muscle depletes a substantial fraction (28%) of muscle AdN (1.75 mumol/g) that can be accounted for stoichiometrically as purine degradation products during an extended 10-min ischemic period of mild (12 tetani/min) contraction conditions. IMP accumulation (1 mumol/g) is most prominent with inosine, accounting for 23% (0.4 mumol/g) of the depleted AdN, showing that slow-twitch red muscle is capable of both AMP deamination and the subsequent production of purine nucleosides during an extended period of ischemic contractions. The present results indicate that AdN metabolism in the soleus muscle is complex, yielding expected degradation products or a loss of total purines, depending on contraction conditions.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenine Nucleotides↗

PubMed1990

Acute inhibition of respiratory capacity of muscle reduces peak oxygen consumption.

Electron transport capacity of skeletal muscle was inhibited in situ in an acute dose-dependent manner with myxothiazol, a tight-binding inhibitor of ubiquinone-cytochrome c reductase, complex III of the respiratory chain. Peak oxygen consumption of rat hindlimb muscle was determined via consecutive 10-min isometric contraction (100 ms at 100 Hz) periods of increasing energy demands (4, 8, 15, 30, 45, and 60 tetani/min), using an isolated hindlimb preparation perfused with a high oxygen delivery (approximately 6-8 mumol.min-1.g-1). Peak oxygen consumption decreased from 4.61 +/- 0.19 mumol.min-1.g-1 (control) in a dose-dependent manner to 0.73 +/- 0.07 mumol.min-1.g-1 at 0.50 microM myxothiazol in blood. Oxygen extraction decreased from 65 to 12% of delivered oxygen. Furthermore, the reduction in peak respiratory rate became evident at lower energy demands of the contraction sequence. Myxothiazol inhibition of respiration was not dependent on the presence of muscle contractions but was evident when mitochondria were uncoupled with carbonyl cyanide m-chlorophenylhydrazone. A 50% effective dosage (ED50) of 0.21 microM myxothiazol for inhibition of peak oxygen consumption closely resembled the inhibition of NADH-cytochrome c reductase activity (ED50 of 0.27 microM) determined from homogenates of the same muscles. This suggests that the peak oxygen consumption of skeletal muscle is tightly coupled to the capacity for electron transport evaluated by flux through NADH-cytochrome c reductase. If the enzyme activity measured in vitro correctly represents available enzymatic capacity within contracting muscle, approximately 75% of electron transport capacity for handling reducing equivalents generated from NADH is utilized during peak oxygen consumption of rat hindlimb muscle contracting in situ.

Animals↗

PubMed1990

Muscle blood flow in trained rats with peripheral arterial insufficiency.

The influence of exercise training on the recovery of muscle blood flow was assessed in rats with bilateral stenosis of the femoral artery, sufficient to limit exercise hyperemia in the distal hindlimb but not alter resting blood flow. Muscle blood flow was measured with 141Ce-labeled microspheres (15 microns) during treadmill running at 20 m/min in normal (n = 10), acute stenosed (n = 9), sedentary stenosed (n = 10) and trained stenosed (n = 13) animals. Treadmill training by a progressively intense program (up to 1 h/day, 7 days/wk for 6 wk) improved exercise tolerance evident both in duration and intensity of exercise. Total hindlimb blood flow (ml.min-1.100 g-1) was not different (P greater than 0.05) between all stenosed groups but was only 46-63% that of the normal group (P less than 0.05). Acute stenosis reduced distal blood flow to only 22% of that in the proximal hindlimb tissue. A significant (P less than 0.05) but limited recovery of distal limb blood flow (to 44% of proximal) occurred in sedentary stenosed rats after 6 wk of cage activity. Training further increased (P less than 0.05) distal limb blood flow to 69% of proximal. This partial recovery of distal limb blood flow could reflect a greater collateral vessel function or an enhanced vascularity of the distal limb tissue. Our results illustrate that peripheral adaptations occur within the ischemic hindlimb of trained animals to redistribute the limited O2 delivery to the active muscles most affected by stenosis.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1990

Impact of reduced cytochrome oxidase activity on peak oxygen consumption of muscle.

The impact of reduced muscle oxidative capacity on peak oxygen consumption and isometric performance was evaluated using an isolated rat hindlimb preparation perfused with a high oxygen delivery. Capacity for electron transport was reduced with chloramphenicol (CAP), an inhibitor of mitochondrial gene-coded protein synthesis. The activity of cytochrome oxidase, a mitochondrial cristae component, was reduced approximately 45% (P less than 0.005) in the mixed-fiber-type plantaris muscle. Several facets of muscle remodeling were also evident with the 10- to 14-day CAP treatment, including decreased citrate synthase activity, increased capillarity, and increased numbers of type IIc fibers. Perfusion of CAP (n = 6) and control (n = 7) rat hindlimbs of similar size with similar total flows (10-11 ml/min) and oxygen contents (20-21 vol%) resulted in similarly high oxygen deliveries to contracting muscles of the hindlimbs (CAP, 9.66 +/- 0.83 mumols.min-1.g-1; control, 8.74 +/- 0.75). Performance of the gastrocnemius-plantaris-soleus group declined in a similar fashion for both groups during increasingly intense near-steady-state tetanic contraction (100 ms at 100 Hz) conditions of 4, 8, 15, 30, 45, and 60 per minute. Oxygen consumption was similar for both groups at rest and increased similarly at each contraction condition. Peak oxygen consumption was not different between CAP (5.34 +/- 0.55 mumols.min-1.g-1) and control (5.74 +/- 0.43) groups and required only 56-68% of the oxygen delivered. This implies that rat skeletal muscle can suffer a significant reduction in its electron transport capacity without impairing peak oxygen consumption and muscle performance.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1990

Training increases muscle blood flow in rats with peripheral arterial insufficiency.

This study investigated the effect of physical training on muscle blood flow (BF) in rats with peripheral arterial insufficiency during treadmill running. Bilateral stenosis of the femoral artery of adult rats (300-350 g) was performed to reduce exercise hyperemia in the hindlimb but not limit resting muscle BF. Rats were divided into normal sedentary, acute stenosed (stenosed 3 days before the experiment), stenosed sedentary (limited to cage activity), and stenosed trained (run on a treadmill by a progressively intense program, up to 50-60 min/day, 5 days/wk for 6-8 wk). Hindlimb BF was determined with 85Sr- and 141Ce-labeled microspheres at a low (20 m/min) and high treadmill speed (30-40 m/min depending on ability). Maximal hindlimb BF was reduced to approximately 50% normal in the acute stenosed group. Total hindlimb BF (81 +/- 5 ml.min-1.100 g-1) did not change in stenosed sedentary animals with 6-8 wk of cage activity, but a redistribution of BF occurred within the hindlimb. Two factors contributed to a higher BF to the distal limb muscle of the trained animals. A redistribution BF within the hindlimb occurred in stenosed trained animals; distal limb BF increased to approximately 80% (P less than 0.001) of the proximal tissue. In addition, an increase in total hindlimb BF with training indicates that collateral BF has been enhanced (P less than 0.025). The associated increase in oxygen delivery to the relatively ischemic muscle probably contributed to the markedly improved exercise tolerance evident in the trained animals.

Animals↗

PubMed1990

Amino acid metabolism during exercise and following endurance training.

Exercise results in marked alterations in amino acid metabolism within the body. The branched-chain amino acids, especially leucine, are particularly important since they contribute as energy substrates and as nitrogen donors in the formation of alanine, glutamine and aspartate. Leucine oxidation increases during whole-body exercise. Nonetheless, leucine's contribution as a muscle energy substrate is amll, being 3 to 4% at rest, and even lower (1%) during exercise. Traditional energy substrates (carbohydrates, lipid) remain most important. These rates of leucine oxidation can be readily attributed to skeletal muscle. Following endurance training, whole-body leucine oxidation is increased at rest and during exercise. Since its oxidation by muscle is not augmented, this whole-body increase is not due to muscle. Thus, other tissues within the body (i.e. liver) must account for this. Comparisons of leucine oxidation in rats and humans indicate that species differences exist. Much larger increases in leucine oxidation are brought about by exercise in humans. Calculations based on steady-state rates of leucine oxidation at rest and during exercise indicate that the recommended dietary intake of leucine is inadequate, since it is lower than measured whole-body rates of leucine oxidation. This inadequacy is exacerbated in individuals who are physically active.

Amino Acids↗

PubMed1988

Blood flow to different rat skeletal muscle fiber type sections during isometric contractions in situ.

In whole skeletal muscle, peak blood flow is known to correlate with the capacity for oxidative metabolism. Since most mammalian skeletal muscle is comprised of different fiber types whose oxidative potential varies widely, the possibility of heterogeneous blood flow distribution within a given muscle was investigated. An in situ preparation of the rat gastrocnemius-soleus-plantaris muscle group was used and blood flow measured by the radiolabeled microsphere technique. Blood flow at rest averaged 5-6 ml.min-1.100 g-1 in fast-twitch white (FTW) fiber sections, while flows to fast-twitch red (FTR) and slow-twitch red (STR) muscle were 10-12 ml.min-1.100 g-1. Isometric twitch contractions generated large (12-15 times above rest) increases in blood flow to all fiber type sections that tended to decrease at higher frequencies. Tetanic contractions result in greater tension development and higher blood flows in the red fiber sections. The highest blood flow to the FTR section was 300 ml.min-1.100 g-1, a value 3-4-fold greater than the maximum for the FTW fiber section. Peak blood flow to the STR (soleus) was intermediate between the two fast fiber types. Differences in blood flow response between fiber sections could not be dismissed due to measurement artifact. Thus, the capacity for blood flow is fairly proportional to the differences in oxidative capacity among fiber types. Blood flow to the skeletal muscle fiber types of the rat also differed qualitively in response to contractions.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗