Role of histidine-related compounds to intracellular buffering in fish skeletal muscle

1985 ◽  
Vol 249 (4) ◽  
pp. R449-R454 ◽  
Author(s):  
H. Abe ◽  
G. P. Dobson ◽  
U. Hoeger ◽  
W. S. Parkhouse
Keyword(s):  
Skeletal Muscle ◽  
Buffer Capacity ◽  
White Muscle ◽  
Activity Patterns ◽  
Fish Muscle ◽  
Salmo Gairdneri ◽  
Fiber Types ◽  
Ph Range ◽  
Muscle Buffering ◽  
Related Compounds

Histidine-related compounds (HRC) were analyzed in fish skeletal muscle as a means of identifying their precise role in intracellular buffering. Fish muscle was used because it contains two functionally and spatially distinct fiber types, red and white. Two fish species, rainbow trout (Salmo gairdneri) and the Pacific blue marlin (Makaira nigricans), were studied because these species demonstrate widely different activity patterns. Marlin red and white muscle buffer capacity was two times higher than trout with white muscle, buffering being two times greater than red in both species. Buffer capacity was highest in the 6.5–7.5 pH range for all tissues, which corresponded to their high anserine levels. The titrated HRC buffering was greater than the observed HRC buffering, which suggested that not all HRC were available to absorb protons. The HRC contribution to total cellular buffering varied from a high of 62% for marlin white to a low of 7% for trout red. The other principal buffers were found to be phosphate and protein with taurine contributing within red muscle in the 7.0–8.0 pH range. HRC were found to be dominant in skeletal muscle buffering by principally accounting for the buffering capacity differences found between the species and fiber types.

Influence of acclimation temperature on mitochondrial DNA, RNA, and enzymes in skeletal muscle

1998 ◽  
Vol 275 (3) ◽  
pp. R905-R912 ◽  
Author(s):  
Brendan James Battersby ◽  
Christopher D. Moyes
Keyword(s):  
Skeletal Muscle ◽  
Mitochondrial Dna ◽  
Steady State ◽  
Muscle Fiber ◽  
Copy Number ◽  
White Muscle ◽  
Fiber Types ◽  
Mitochondrial Enzymes ◽  
Dna Copy Number ◽  
Mitochondrial Content

Skeletal muscle fibers typically undergo modifications in their mitochondrial content, concomitant with alterations in oxidative metabolism that occur during the development of muscle fiber and in response to physiological stimuli. We examined how cold acclimation affects the mitochondrial properties of two fish skeletal muscle fiber types and how the regulators of mitochondrial content differed between tissues. After 2 mo of acclimation to either 4 or 18°C, mitochondrial enzyme activities in both red and white muscle were higher in cold-acclimated fish. No significant differences were detected between acclimation temperatures in the abundance of steady-state mitochondrial mRNA (cytochrome- c oxidase 1, subunit 6 of F0F1-ATPase), rRNA (16S), or DNA copy number. Steady-state mRNA for nuclear-encoded respiratory (adenine nucleotide translocase 1) and glycolytic genes showed high interindividual variability, particularly in the cold-acclimated fish. Although mitochondrial enzymes were 10-fold different between the two muscle types, mitochondrial DNA copy number differed only 4-fold. The relative abundance of mitochondrial mRNA and nuclear mRNA in red and white muscle reflected the differences in copy number of their respective genes. These data suggest that the response to physiological stimuli and determination of tissue-specific mitochondrial properties likely result from the regulation of nuclear-encoded genes.

Glycerylphosphorylcholine and Related Compounds in Rainbow Trout Muscle Stored at −4 C

1967 ◽  
Vol 24 (2) ◽  
pp. 273-280 ◽  
Author(s):  
R. E. E. Jonas ◽  
E. Bilinski
Keyword(s):  
Fatty Acids ◽  
Rainbow Trout ◽  
General Trend ◽  
Fish Muscle ◽  
Enzymic Activity ◽  
Salmo Gairdneri ◽  
Threefold Increase ◽  
Free Choline ◽  
Related Compounds ◽  
Trout Muscle

Glycerylphosphorylcholine in rainbow trout (Salmo gairdneri) muscle stored at −4 C showed an increase from 36 μmoles/100 g in fresh muscle to 46 μmoles/100 g after 2 weeks. During longer periods of storage an approximately threefold increase in concentration took place, reaching 123 and 105 μmoles/100 g muscle after 9 and 17 weeks. Liberation of free choline was found to take place after 6 weeks of storage. There was very little change in the concentration of choline after 6 weeks storage when the value was approximately 100 μmoles/100 g. The release of free fatty acid during cold storage showed a general trend, which was similar to the formation of glycerylphosphorylcholine, but quantitatively the changes were more pronounced. Free fatty acids amounted to 45 μmoles/100 g in fresh muscle and rose to a plateau of approximately 1200 μmoles/100 g after 9 weeks of storage. The results are discussed in relation to the enzymic activity present in fish muscle.

scholarly journals ULTRASTRUCTURE AND ADENOSINE TRIPHOSPHATASE ACTIVITY OF RED AND WHITE MUSCLE FIBERS OF THE CAUDAL REGION OF A FISH, SALMO GAIRDNERI

1972 ◽  
Vol 55 (1) ◽  
pp. 42-57 ◽  
Author(s):  
Asish C. Nag
Keyword(s):  
Electron Microscopy ◽  
Sarcoplasmic Reticulum ◽  
Adenosine Triphosphatase ◽  
White Muscle ◽  
Muscle Fibers ◽  
Salmo Gairdneri ◽  
Fiber Types ◽  
Surface Areas ◽  
Biochemical Studies ◽  
T System

Electron microscopy, together with quantitation using a tracing device linked to a digital computer, reveals that the red and white muscle fibers of Salmo gairdneri differ in diameter, organization of myofibrils, dimensions of myofilaments, volumes and surface areas of T system and sarcoplasmic reticulum, morphology of mitochondria, and content of mitochondria, lipid, and glycogen. Biochemical studies show that the ATPase activity of white fibers is three times that of the red fibers. Actomyosin content of red fibers is higher than that of the white fibers. The functional significance of these differences between two fiber types is discussed.

Fish muscle glycogen phosphorylase

1968 ◽  
Vol 46 (5) ◽  
pp. 423-432 ◽  
Author(s):  
M. Yamamoto
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Phosphorylase ◽  
Active Form ◽  
Maximal Activity ◽  
Fish Muscle ◽  
Salmo Gairdneri ◽  
Rabbit Muscle ◽  
Muscle Phosphorylase

Glycogen phosphorylase b was purified 70- to 90-fold from skeletal muscle of rainbow trout (Salmo gairdneri). The purified enzyme exhibited maximal activity near pH 6.8 at 37°. Of several 5′-nucleotides tested, only 5′-AMP caused stimulation of phosphorylase b. The Km value for glucose-1-phosphate was 10–15 mM, and for 5′-AMP, 0.2–0.4 mM. Glucose (25 mM) and ATP (5 mM) were both inhibitory, but glucose-6-phosphate (5 mM) had no effect. Inactive trout muscle phosphorylase was converted to the active form in vivo by subjecting a fish to physical exercise. The conversion of fish muscle phosphorylase b to a was also catalyzed in vitro with purified rabbit muscle phosphorylase b kinase in the presence of ATP and Mg++. Evidence is presented to indicate the presence of phosphorylase b kinase and phosphorylase phosphatase in trout skeletal muscle.

White muscle lactate and pyruvate concentrations in rested flounder, Platichthys flesus and plaice, Pleuronectes platessaa: a re-evaluation of handling and sampling techniques

1983 ◽  
Vol 63 (4) ◽  
pp. 897-903 ◽  
Author(s):  
P. J. Adcock ◽  
P. R. Dando
Keyword(s):  
Skeletal Muscle ◽  
White Muscle ◽  
Muscular Activity ◽  
Fish Muscle ◽  
Usual Method ◽  
Sampling Techniques ◽  
Muscle Lactate ◽  
Lactate And Pyruvate ◽  
Direct Immersion ◽  
Pyruvate Ratio

Rapid fixing of skeletal muscle by a ‘freeze-clamp’ technique results in up to a 3-fold lower lactate, a slightly higher pyruvate concentration and a 2- to 4-fold decrease in lactate/pyruvate ratio, to the lowest value yet recorded for fish muscle, when compared with the more usual method of direct immersion in liquid nitrogen. This is attributed to the faster cooling rate of freeze-clamped muscle minimizing ‘sampling anoxia’. Immobilizing fish either by anaesthetic or stunning produces no significant change in metabolite levels. It is concluded that it is relatively easy to handle quiescent flatfish, but light anaesthesia ensures no muscular activity.

Decreasing intramuscular phosphagen content simultaneously increases plasma membrane FAT/CD36 and GLUT4 transporter abundance

2008 ◽  
Vol 295 (3) ◽  
pp. R806-R813 ◽  
Author(s):  
Kristin E. Pandke ◽  
Kerry L. Mullen ◽  
Laelie A. Snook ◽  
Arend Bonen ◽  
David J. Dyck
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
White Muscle ◽  
Energy Charge ◽  
Oxidative Capacity ◽  
Fiber Types ◽  
Energy Substrates ◽  
Muscle Oxidative Capacity ◽  
Substrate Metabolism ◽  
Total Creatine

Decreasing muscle phosphagen content through dietary administration of the creatine analog β-guanidinopropionic acid (β-GPA) improves skeletal muscle oxidative capacity and resistance to fatigue during aerobic exercise in rodents, similar to that observed with endurance training. Surprisingly, the effect of β-GPA on muscle substrate metabolism has been relatively unexamined, with only a few reports of increased muscle GLUT4 content and insulin-stimulated glucose uptake/clearance in rodent muscle. The effect of chronically decreasing muscle phophagen content on muscle fatty acid (FA) metabolism (transport, oxidation, esterification) is virtually unknown. The purpose of the present study was to examine changes in muscle substrate metabolism in response to 8 wk feeding of β-GPA. Consistent with other reports, β-GPA feeding decreased muscle ATP and total creatine content by ∼50 and 90%, respectively. This decline in energy charge was associated with simultaneous increases in both glucose (GLUT4; +33 to 45%, P < 0.01) and FA (FAT/CD36; +28 to 33%, P < 0.05) transporters in the sarcolemma of red and white muscle. Accordingly, we also observed significant increases in insulin-stimulated glucose transport (+47%, P < 0.05) and AICAR-stimulated palmitate oxidation (+77%, P < 0.01) in the soleus muscle of β-GPA-fed animals. Phosphorylation of AMPK (+20%, P < 0.05), but not total protein, was significantly increased in both fiber types in response to muscle phosphagen reduction. Thus the content of sarcolemmal transporters for both of the major energy substrates for muscle increased in response to a reduced energy charge. Increased phosphorylation of AMPK may be one of the triggers for this response.

scholarly journals SCALING OF ATP-SUPPLYING ENZYMES, MYOFIBRILLAR PROTEINS AND BUFFERING CAPACITY IN FISH MUSCLE: RELATIONSHIP TO LOCOMOTORY HABIT

1990 ◽  
Vol 149 (1) ◽  
pp. 319-333 ◽  
Author(s):  
G. N. SOMERO ◽  
J. J. CHILDRESS
Keyword(s):  
Body Size ◽  
White Muscle ◽  
Citrate Synthase ◽  
Anaerobic Power ◽  
Fish Muscle ◽  
Buffering Capacity ◽  
Glycolytic Enzymes ◽  
Salmo Gairdneri ◽  
Total Body Mass ◽  
Burst Swimming

Pelagic fishes with an ability to swim in strong bursts have previously been shown to have large size-dependent increases (positive aUometric scaling exponents) in the activities of glycolytic enzymes in white skeletal muscle. This scaling of glycolytic activity has been hypothesized to provide the anaerobic power upporting the size-independence of relative burst swimming speeds (body lengths s−1) in these fishes. This paper presents tests of several predictions of this hypothesis, using different-sized individuals of two pelagic teleosts, the kelp bass (Paralabrax clathratus) and the freshwater rainbow trout (Salmo gairdneri), and a flatfish, the Dover sole (Microstomus pacificus). In the two pelagic species, an increase in body size was accompanied by an increase in activities in white muscle (i.u.g wet mass ofmuscle−1) of lactate dehydrogenase (LDH), an indicator of potential for anaerobic glycolysis, and creatine phosphokinase (CPK), an enzyme that helps maintain stable ATP concentration during muscular activity. Activities of citrate synthase (CS), an indicator of the potential for aerobic metabolism, decreased with size. In the flatfish, activities of all enzymes in white muscle decreased with body size, a trend proposed to reflect lack of adaptive value of strong burst swimming ability in this benthic fish. Activities of LDH and CS were size-independent in brain of flatfish, indicating that the scaling patterns observed in the muscle of this species were related to muscle function, not to common, organism-wide changes with size. In white muscle of P. clathratus, total protein and soluble protein concentrations and buffering capacity increased with body size in parallel, but myofibrillar protein was size-independent. These results suggest that the capacity for anaerobically powered work and the maximal potential to generate force scale only modestly in relation to total body mass and therefore do not appear to be functionally related to the pattern of glycolytic scaling. Thus, these data support the hypothesis that the functional role of the strongly positive scaling of glycolytic enzymes in the white muscle of pelagic fish is to provide increased power during burst swimming in larger-sized fishes.

GLYCOGEN PHOSPHORYLASE AND GLYCOGEN SYNTHETASE ACTIVITY IN RED AND WHITE SKELETAL MUSCLE OF THE GUINEA PIG

1965 ◽  
Vol 43 (4) ◽  
pp. 463-468 ◽  
Author(s):  
Sydney St. George Stubbs ◽  
M. C. Blanchaer
Keyword(s):  
Skeletal Muscle ◽  
Guinea Pig ◽  
Glycogen Phosphorylase ◽  
White Muscle ◽  
Synthetase Activity ◽  
Fiber Types ◽  
Phosphorylase Activity ◽  
Glycogen Synthetase ◽  
Red Muscle ◽  
Wet Weight

Glycogen phosphorylase (α-1,4-glucan:orthophosphate glucosyltransferase) and glycogen synthetase (UDPG:α-1,4-glucan α-4-glucosyltransferase) have been examined in red and white skeletal muscle of the guinea pig. Histochemically phosphorylase was found to be more active in white than in red muscle fibers but no difference in glycogen synthetase could be detected between the fiber types. However, quantitative determinations showed that total glycogen synthetase activity (I + D) was higher in red than in white muscle (1.46 ± 0.14 S.E.M. vs. 0.71 ± 0.09 μmoles/minute per g wet weight at 37°). The converse relationship held for total phosphorylase activity (a + b), which was greater in white than in red muscle (19.24 ± 2.93 vs. 10.43 ± 2.34 μmoles/minute per g wet weight at 30°). The phosphorylase a level of 3.63 ± 0.96 in red muscle at rest was similar to that of 5.44 ± 1.19 in resting white muscle. Stimulation produced a significant conversion of phosphorylase b to a only in white muscle. After 30 seconds stimulation with 1-volt impulses of 20 milliseconds duration at a rate of 20 pulses per second, the phosphorylase a activities of red and white muscle were respectively 3.72 ± 1.88 and 16.66 ± 1.79. After stimulation the glycogen synthetase values in white and red muscle were 1.02 ± 0.07 and 1.72 ± 0.11 respectively.

The KATP channel Kir6.2 subunit content is higher in glycolytic than oxidative skeletal muscle fibers

2011 ◽  
Vol 301 (4) ◽  
pp. R916-R925 ◽  
Author(s):  
Krystyna Banas ◽  
Charlene Clow ◽  
Bernard J. Jasmin ◽  
Jean-Marc Renaud
Keyword(s):  
Skeletal Muscle ◽  
Cross Sections ◽  
Fiber Type ◽  
Energy Levels ◽  
Muscle Fibers ◽  
Metabolic Stress ◽  
Oxidative Capacity ◽  
Fiber Types ◽  
Fiber Damage ◽  
The Individual

It has long been suggested that in skeletal muscle, the ATP-sensitive K+ channel (KATP) channel is important in protecting energy levels and that abolishing its activity causes fiber damage and severely impairs function. The responses to a lack of KATP channel activity vary between muscles and fibers, with the severity of the impairment being the highest in the most glycolytic muscle fibers. Furthermore, glycolytic muscle fibers are also expected to face metabolic stress more often than oxidative ones. The objective of this study was to determine whether the t-tubular KATP channel content differs between muscles and fiber types. KATP channel content was estimated using a semiquantitative immunofluorescence approach by staining cross sections from soleus, extensor digitorum longus (EDL), and flexor digitorum brevis (FDB) muscles with anti-Kir6.2 antibody. Fiber types were determined using serial cross sections stained with specific antimyosin I, IIA, IIB, and IIX antibodies. Changes in Kir6.2 content were compared with changes in CaV1.1 content, as this Ca2+ channel is responsible for triggering Ca2+ release from sarcoplasmic reticulum. The Kir6.2 content was the lowest in the oxidative soleus and the highest in the glycolytic EDL and FDB. At the individual fiber level, the Kir6.2 content within a muscle was in the order of type IIB > IIX > IIA ≥ I. Interestingly, the Kir6.2 content for a given fiber type was significantly different between soleus, EDL, and FDB, and highest in FDB. Correlations of relative fluorescence intensities from the Kir6.2 and CaV1.1 antibodies were significant for all three muscles. However, the variability in content between the three muscles or individual fibers was much greater for Kir6.2 than for CaV1.1. It is suggested that the t-tubular KATP channel content increases as the glycolytic capacity increases and as the oxidative capacity decreases and that the expression of KATP channels may be linked to how often muscles/fibers face metabolic stress.

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