Biomedical subjects

P G Arabadjis

Publications and source records attributed to P G Arabadjis.

4 recordsLinked to original sources

PubMed1996

IMP reamination to AMP in rat skeletal muscle fiber types.

Inosine 5'-monophosphate (IMP) reamination in skeletal muscle fiber sections of the rat hindlimb was studied. High IMP concentrations were established during ischemic contractions in each fiber section: 3.1, 2.8, or 0.6 mumol/g in the fast-twitch white (FTW), fast-twitch red (FTR), and slow-twitch red (STR) muscle sections, respectively. Thereafter blood flow was restored and stimulation was discontinued to allow reamination of IMP. After 0, 2, 5, 10, 15, or 20 min of recovery, muscle sections were freeze-clamped and analyzed for metabolite contents. IMP was nearly fully reaminated after 10 and 20 min of recovery in STR and FTR muscles, respectively. Reamination in TW fibers was delayed and slower, with only 50% of the IMP reaminated after 20 min of recovery. Significant recovery (approximately 75%) of phosphocreatine occurs in each fiber section before the onset of reamination. Reamination was also evaluated after high-speed treadmill running with or without inhibition of reamination by hadacidin. Running resulted in large accumulations of IMP in FTW and FTR fibers (3.5 and 1.4 mumul/g, respectively); IMP in FTR fibers was higher with hadacidin treatment. Reamination after running was much greater in FTR than in FTW fibers and was associated with recovery of phosphocreatine. After running, the purine degradation products inosine and hypoxanthine were increased in FTW and FTR fibers in normal and hadacidin-treated animals. Plasma inosine, hypoxanthine, and urate increased after exercise; concentrations continued to increase if reamination was inhibited by hadacidin. These results demonstrate that when muscle IMP is increased, subsequent degradation and loss of purines occur. Rapid reamination should minimize the quantity of purine lost from muscle and limit the metabolic cost of replenishing purines by the de novo synthesis or salvage pathways.

Adenosine Monophosphate↗

PubMed1993

Purine nucleoside formation in rat skeletal muscle fiber types.

To determine the capacity for purine nucleotide degradation among skeletal muscle fiber types, we established energy-depleted conditions in muscles of the rat hindlimb by inducing muscle contraction during ischemia. After 5, 10, 15, or 20 min of ischemic contractions, representative muscle sections were freeze-clamped and analyzed for purine nucleotides, nucleosides, and bases. Fast-twitch muscle sections accumulated about fourfold more IMP than the slow-twitch red soleus muscle. Inosine begins to accumulate at < 0.5 mumol/g IMP in slow-twitch muscle and at approximately 2 mumol/g IMP in fast-twitch muscle. This suggests that inosine is formed intracellularly by 5'-nucleotidase acting on IMP and that the activity and/or substrate affinity of the 5'-nucleotidase present in slow-twitch muscle may be higher than in fast-twitch muscle. At similar concentrations of precursor IMP, slow-twitch muscle has a greater capacity for purine nucleoside formation and should be more dependent on salvage and de novo synthesis of purine for the maintenance of muscle adenine nucleotides. Fast-twitch muscles are better able to retain IMP for subsequent reamination due to their lower capacity to degrade IMP to inosine.

Adenine Nucleotides↗

PubMed1990

Morphologic and functional alterations in aging rat muscle.

To understand better the causes of reduced contractile force in aging skeletal muscle, we performed a physiologic and morphologic analysis of plantaris muscle in old rats. The peak twitch tension (Fmax) and rates of force development and relaxation were significantly lower in old (24 months old) rats than in young (six month old) rats. In teased muscle fiber preparations, there was a 5% reduction in the mean number of fibers in the aging plantaris muscle. Histologically, a net loss of fibers occurred only in the muscle belly. Histochemically, fewer Type I fibers were seen in the belly and proximal regions, whereas distally fewer Type IIa fibers were seen. The loss of Types I and IIa oxidative fibers suggested a conservation of fast-twitch Type IIb fibers in a fast-twitch muscle. The relatively small loss of muscle fibers does not explain the large decline in muscle contractile performance which, despite established doctrine, was independent of muscle mass, fiber number or size, or number of fast-twitch fibers. The reduced force production in aging rat muscle appears to be due to a defect in excitation, contraction performance or metabolic activity, rather than a purely anatomical abnormality of muscle.

Aging↗

PubMedDate not supplied

Muscle fiber composition and length-tension relationships in rats chronically exposed to alcohol.

Adult Fischer 344 rats were fed an alcohol diet (7-9 g/kg/day) for 12 weeks and were compared to pair-fed controls with regard to the contraction and fiber characteristics of the gastrocnemius and plantaris muscles of the leg. Muscles were isolated in situ with blood and nerve supplies intact. The muscles were stretched by 1 mm increments and were stimulated at each muscle length with a voltage (1 msec pulse) that had been observed to produce maximal twitch force at the initial muscle length. Maximal twitch tension was found to be only 10% less in alcohol than pair-fed rats and the increase in force resulting from stretching was approximately 15% less in alcohol than pair-fed rats. No significant changes in sciatic nerve conduction velocities were produced by alcohol exposure. Moreover, no significant differences in muscle weight or the number and size of Type I, Type IIa or Type IIb muscle fibers were observed. Although the 12 weeks of alcohol exposure affected muscle physiology and histology in the direction of increased impairment, the differences were not large enough to be statistically significant.

Alcoholism↗