SUMMARY1. The present study investigates to what extent increases in resistance to fatigue and aerobic oxidative capacity of energy metabolism are correlated in fast-twitch tibialis anterior muscles of rat and rabbit subjected to chronic low-frequency stimulation.2. Changes in the aerobic oxidative capacity of the stimulated muscles were judged from increases in citrate synthase activity, representing the constantproportion enzyme group of the citric acid cycle.3. Resistance to fatigue reached maximal values in both rat and rabbit tibialis anterior muscles after stimulation periods of 14 days, whereas citrate synthase activity continued to increase with longer stimulation periods.4. Different time courses of the changes in resistance to fatigue and citrate synthase activity were observed not only with prolonged stimulation periods but also during the first week, when pronounced increases in resistance to fatigue were accompanied by only moderate elevations in citrate synthase activity.5. The dissociation between the changes of the two parameters studied suggests that factors other than elevated aerobic oxidative capacity contribute to enhanced resistance to fatigue.

Chronic stimulation of rat fast-twitch muscle increased the content of both fatty acid-binding protein (FABP) and myoglobin. The increases in FABP, which reached values close to that of cardiac muscle, exceeded those in myoglobin and those in citrate synthase and 3-hydroxyacyl-CoA dehydrogenase activities.

Brush border (BBM) and basolateral membranes (BLM) of rat renal cortical cells separated by free flow electrophoresis revealed two distinct peaks of BBM-specific leucine aminopeptidase and Na+/K(+)-ATPase for BLM. PTH/PTH-related protein (PTHrP) receptors were identified in BBM and BLM. Specific binding of 125 pM [125I]chicken [Tyr36]-PTHrP-(1-36)amide [chPTHrP-(1-36)] to individual fractions of membranes separated by free flow electrophoresis overlapped with the leucine aminopeptidase and Na+/K(+)-ATPase profiles. Binding to pooled BBM was 53 +/- 5% (mean +/- SEM) of that to BLM (P < 0.01). In BBM and BLM, half-maximal inhibition of binding was obtained with 0.4-0.9 nM chPTHrP-(1-36) and 0.2-0.6 nM rat PTH-(1-34). Guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S; 100 microM) lowered chPTHrP-(1-36) binding to 50% of control levels, and half-maximal inhibition of binding was obtained with 480 and 8 nM GTP gamma S in BBM and BLM, respectively. Cross-linking of the PTH/PTHrP receptors with [125I]chPTHrP-(1-36) modified with N-hydroxysuccinimidyl-4-azidobenzoate revealed indistinguishable doublets of 83 and 73 kilodaltons in both BBM and BLM. Adenylyl cyclase was stimulated 6- and 10-fold by chPTHrP-(1-36) and GTP gamma S, respectively, in BLM and 1.3- and 1.9-fold in BBM. In conclusion, PTH receptors were recognized in both the basolateral and brush border membranes. Different receptor coupling to G-proteins and minimal cAMP stimulation in BBM provide evidence for PTH/PTHrP receptor isotypes and/or different postreceptor activation in BBM and BLM.

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