scholarly journals AMP deaminase histochemical activity and immunofluorescent isozyme localization in rat skeletal muscle.

1992 ◽  
Vol 40 (7) ◽  
pp. 931-946 ◽  
Author(s):  
J L Thompson ◽  
R L Sabina ◽  
N Ogasawara ◽  
D A Riley
Keyword(s):  
Skeletal Muscle ◽  
Vascular Tissue ◽  
Immunofluorescence Microscopy ◽  
Capillary Endothelium ◽  
Kinetic Properties ◽  
Amp Deaminase ◽  
Rat Skeletal Muscle ◽  
Connective Tissues ◽  
Functional Roles ◽  
Liver And Kidney

The cellular distribution of AMP deaminase (AMPda) isozymes was documented for rat soleus and plantaris muscles, utilizing immunofluorescence microscopy and immunoprecipitation methods. AMPda is a ubiquitous enzyme existing as three distinct isozymes, A, B and C, which were initially purified from skeletal muscle, liver (and kidney), and heart, respectively. AMPda-A is primarily concentrated subsarcolemmally and intermyofibrillarly within muscle cells, while isozymes B and C are concentrated within non-myofiber elements of muscle tissue. AMPda-B is principally associated with connective tissues surrounding neural elements and the muscle spindle capsule, and AMPda-C is predominantly associated with circulatory elements, such as arterial and venous walls, capillary endothelium, and red blood cells. These specific localizations, combined with documented differences in kinetic properties, suggest multiple functional roles for the AMPda isozymes or temporal segregation of similar AMPda functions. Linkage of the AMPda substrate with adenosine production pathways at the AMP level and the localization of isozyme-C in vascular tissue suggest a regulatory role in the microcirculation.

Effect of exercise on AMP deaminase and adenylosuccinase in rat skeletal muscle

1974 ◽  
Vol 227 (6) ◽  
pp. 1411-1414 ◽  
Author(s):  
WW Winder ◽  
RL Terjung ◽  
KM Baldwin ◽  
JO Holloszy
Keyword(s):  
Skeletal Muscle ◽  
Amp Deaminase ◽  
Rat Skeletal Muscle

scholarly journals Methionine metabolism by rat muscle and other tissues. Occurrence of a new carnitine intermediate

1987 ◽  
Vol 247 (1) ◽  
pp. 35-40 ◽  
Author(s):  
P W D Scislowski ◽  
B M Hokland ◽  
W I A Davis-van Thienen ◽  
J Bremer ◽  
E J Davis
Keyword(s):  
Skeletal Muscle ◽  
Methionine Metabolism ◽  
Rat Skeletal Muscle ◽  
Citrate Cycle ◽  
Kidney Mitochondria ◽  
Rat Muscle ◽  
Mammalian Tissues ◽  
Liver And Kidney ◽  
Oxidation Of Methionine

Perfused rat hindquarter preparations were shown to incorporate radioactivity from [U-14C]methionine into citrate-cycle intermediates, lactate, alanine, glutamate, glutamine and CO2. During perfusion, large amounts of methionine were also oxidized to methionine sulphoxide. The capacity for transamination of methionine or its oxo analogue, 4-methylthio-2-oxobutyrate, by muscle extracts was demonstrated. Rat skeletal muscle, heart, liver and kidney mitochondria, when incubated with the latter plus radiolabelled carnitine, formed a newly identified carnitine derivative, 3-methylthiopropionylcarnitine. It is concluded that the capacity for oxidation of methionine by a trans-sulphuration-independent pathway occurs in several mammalian tissues. The extent of inter-organ handling of intermediates in this pathway(s) is discussed.

Disruption of microtubules in rat skeletal muscle does not inhibit insulin- or contraction-stimulated glucose transport

2003 ◽  
Vol 285 (4) ◽  
pp. E836-E844 ◽  
Author(s):  
Hua Ai ◽  
Evelyn Ralston ◽  
Hans P. M. M. Lauritzen ◽  
Henrik Galbo ◽  
Thorkil Ploug
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transport ◽  
Immunofluorescence Microscopy ◽  
Fiber Type ◽  
Force Production ◽  
Rat Skeletal Muscle ◽  
Microtubule Network ◽  
Type Composition ◽  
Flexor Digitorum Brevis ◽  
Flexor Digitorum

Insulin and muscle contractions stimulate glucose transport in skeletal muscle through a translocation of intracellular GLUT4 glucose transporters to the cell surface. Judged by immunofluorescence microscopy, part of the GLUT4 storage sites is associated with the extensive microtubule cytoskeleton found in all muscle fibers. Here, we test whether microtubules are required mediators of the effect of insulin and contractions. In three different incubated rat muscles with distinct fiber type composition, depolymerization of microtubules with colchicine for ≤8 h did not inhibit insulin- or contraction-stimulated 2-deoxyglucose transport or force production. On the contrary, colchicine at least partially prevented the ∼30% decrease in insulin-stimulated transport that specifically developed during 8 h of incubation in soleus muscle but not in flexor digitorum brevis or epitrochlearis muscles. In contrast, nocodazole, another microtubule-disrupting drug, rapidly and dose dependently blocked insulin- and contraction-stimulated glucose transport. A similar discrepancy between colchicine and nocodazole was also found in their ability to block glucose transport in muscle giant “ghost” vesicles. This suggests that the ability of insulin and contractions to stimulate glucose transport in muscle does not require an intact microtubule network and that nocodazole inhibits glucose transport independently of its microtubule-disrupting effect.

38 AMP DEAMINASE BINDING IN CONTRACTING RAT SKELETAL MUSCLE

1990 ◽  
Vol 22 (2) ◽  
pp. S7 ◽  
Author(s):  
Kenneth W. Rundell ◽  
Peter C. Tullson ◽  
R. L. Terjung
Keyword(s):  
Skeletal Muscle ◽  
Amp Deaminase ◽  
Rat Skeletal Muscle

scholarly journals Adenylate metabolism in the heart. Regulatory properties of rabbit cardiac adenylate deaminase

1979 ◽  
Vol 182 (2) ◽  
pp. 361-366 ◽  
Author(s):  
R Barsacchi ◽  
M Ranieri-Raggi ◽  
C Bergamini ◽  
A Raggi
Keyword(s):  
Skeletal Muscle ◽  
Kinetic Properties ◽  
Amp Deaminase ◽  
Alkaline Ph ◽  
Muscle Enzyme ◽  
Adenylate Deaminase ◽  
Activated State ◽  
Maximal Activation ◽  
Regulatory Properties

The kinetic properties of a 300-fold purified cardiac AMP deaminase were studied and compared with those of the corresponding enzyme from skeletal muscle. The heart enzyme is activated by ATP and less efficiently by ADP, and is inhibited by Pi, phosphocreatine and GTP. ATP, even at micromolar concentrations, is able to abolish the effects of the inhibitors. The affinity of the enzyme for AMP is low in the absence of activators (Km 3.1 mM), but, in the presence of ATP, becomes as high as that of skeletal-muscle AMP deaminase (Km 0.4 mM). The maximal activation by ATP is observed at alkaline pH (pH 7.5-8.0). Under the same conditions ATP is maximally inhibitory for skeletal-muscle enzyme. These results suggest that AMP deaminase in the heart is always in the activated state, whereas in skeletal muscle the enzyme is active only during exhaustive contractions.

AMP DEAMINASE BINDING TO MYOSIN IN RAT SKELETAL MUSCLE AFTER TREADMILL RUNNING

1992 ◽  
Vol 24 (Supplement) ◽  
pp. S60
Author(s):  
Kenneth W. Rundell ◽  
Peter C. Tullson ◽  
Ronald L. Terjung
Keyword(s):  
Skeletal Muscle ◽  
Treadmill Running ◽  
Amp Deaminase ◽  
Rat Skeletal Muscle
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