Limb muscles from rats flown in space and after hindlimb unloading (HU) show an increased fatigability, and spaceflight has been shown to result in a reduced ability to oxidize fatty acids. The purpose of this investigation was to determine the effects of HU on the substrate content in fast- and slow-twitch fibers and to assess the substrate utilization patterns in single slow type I fibers isolated from control and HU animals. A second objective was to assess whether HU altered the ability of the heart or limb muscle to oxidize pyruvate or palmitate. After 2 wk of HU, single fibers were isolated from the freeze-dried soleus and gastrocnemius muscles. HU increased the glycogen content in all fiber types, and it increased lactate, ATP, and phosphocreatine in the slow type I fiber. After HU, the type I fiber substrate profile was shifted toward that observed in fast fibers. For example, fiber glycogen increased from 179 +/- 16 to 285 +/- 25 mmol/kg dry wt, which approached the 308 +/- 23 mmol/kg dry wt content observed in the post-HU type IIa fiber. With contractile activity, the type I fiber from the HU animal showed a greater utilization of glycogen and accumulation of lactate compared with the control type I fiber. HU had no effect on the ability of crude homogenate or mitochondria fractions from the soleus or gastrocnemius to oxidize pyruvate or palmitate. The increased fatigability after HU may have resulted from an elevated glycolysis producing an increased cell lactate and a decreased pH.

The purpose of this investigation was to determine how models of weightlessness, hindlimb suspension (HS), and hindlimb immobilization (HI) affect the metabolic enzyme profile in the slow oxidative (SO), fast oxidative glycolytic (FOG), and fast glycolytic (FG) fibers of rat hindlimb. After 1, 2, or 4 wk of HS or HI, single fibers were isolated from freeze-dried soleus and gastrocnemius muscles; a small section of each fiber was run on sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels to identify fiber type, and the remaining piece was assayed for either lactate dehydrogenase (LDH) and citrate synthase (CS) or phosphofructokinase (PFK) and beta-hydroxyacyl-CoA dehydrogenase (beta-OH-acyl-CoA). Two weeks of HS induced an almost twofold increase in the activity of CS (2.13 +/- 0.13 vs. 3.60 +/- 0.26 mol.kg dry wt-1.h-1) in the SO fiber of the soleus, and the activity stayed high at 4 wk. Although the FOG fiber had significantly higher CS activity (3.85 +/- 0.29) than either the SO or FG (1.59 +/- 0.16 mol.kg dry wt-1.h-1) fiber, neither fast fiber type was altered by HS. The glycolytic enzymes LDH and PFK were both elevated in the SO fiber after HS. The increase in LDH occurred by 1 wk (14.80 +/- 1.51 vs. 8.83 +/- 0.78), whereas the activity of PFK was not significantly changed until 4 wk (1.16 +/- 0.13 vs. 0.68 +/- 0.05 mol.kg dry wt-1.h-1). The control FG fiber had the highest LDH (44.30 +/- 2.29) and PFK (2.40 +/- 0.16) activities, followed by the FOG fiber (LDH, 34.10 +/- 2.83; PFK, 1.62 +/- 0.17 mol.kg dry wt-1.h-1); however, the activities of these glycolytic enzymes in the fast fiber types were unaltered by HS. The activity of beta-OH-acyl-CoA was not affected by HS in either the slow or fast fiber types. HI showed qualitatively similar changes to those observed with HS; however, the enzyme shifts developed with a slower time course. In conclusion, both HS and HI shifted the SO fiber enzyme pattern toward that of the control FOG fiber; however, a complete conversion from the SO to FOG fiber did not occur within the 4-wk treatment period.

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