Familial AMP deaminase deficiency with skeletal muscle type I atrophy and fatal cardiomyopathy

1981 ◽  
Vol 4 (1) ◽  
pp. 169-170 ◽  
Author(s):  
H. R. Scholte ◽  
H. F. M. Busch ◽  
I. E. M. Luyt-Houwen
Keyword(s):  
Skeletal Muscle ◽  
Type I ◽  
Amp Deaminase ◽  
Muscle Type ◽  
Fatal Cardiomyopathy

Genetic and other determinants of AMP deaminase activity in healthy adult skeletal muscle

1998 ◽  
Vol 85 (4) ◽  
pp. 1273-1278 ◽  
Author(s):  
Barbara Norman ◽  
Donna K. Mahnke-Zizelman ◽  
Amy Vallis ◽  
Richard L. Sabina
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Mutant Allele ◽  
Fiber Type ◽  
Type I ◽  
Training Status ◽  
Amp Deaminase ◽  
Normal Allele ◽  
Relative Percentage ◽  
Type I Fibers

AMPD1 genotype, relative fiber type composition, training status, and gender were evaluated as contributing factors to the reported variation in AMP deaminase enzyme activity in healthy skeletal muscle. Multifactorial correlative analyses demonstrate that AMPD1 genotype has the greatest effect on enzyme activity. An AMPD1 mutant allele frequency of 13.7 and a 1.7% incidence of enzyme deficiency was found across 175 healthy subjects. Homozygotes for the AMPD1 normal allele have high enzyme activities, and heterozygotes display intermediate activities. When examined according to genotype, other factors were found to affect variability as follows: AMP deaminase activity in homozygotes for the normal allele exhibits a negative correlation with the relative percentage of type I fibers and training status. Conversely, residual AMP deaminase activity in homozygotes for the mutant allele displays a positive correlation with the relative percentage of type I fibers. Opposing correlations in different homozygous AMPD1 genotypes are likely due to relative fiber-type differences in the expression of AMPD1 and AMPD3 isoforms. Gender also contributes to variation in total skeletal muscle AMP deaminase activity, with normal homozygous and heterozygous women showing only 85–88% of the levels observed in genotype-matched men.

scholarly journals Effects of age and exercise on mouse skeletal muscle type I collagen gene promoter activity

2007 ◽  
Vol 21 (6) ◽  
Author(s):  
Ashley Ann Anderson ◽  
Shelley Lietzau‐Mourer ◽  
Adam Pearson ◽  
Brittany Bolt ◽  
Benjamin F Timson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Promoter Activity ◽  
Type I Collagen ◽  
Gene Promoter ◽  
Type I ◽  
Collagen Gene ◽  
Muscle Type ◽  
Mouse Skeletal Muscle

Thyroid hormone receptor-β-selective agonist GC-24 spares skeletal muscle type I to II fiber shift

2005 ◽  
Vol 321 (2) ◽  
pp. 233-241 ◽  
Author(s):  
Elen H. Miyabara ◽  
Marcelo S. Aoki ◽  
Antonio G. Soares ◽  
Rodrigo M. Saltao ◽  
Cassio M. Vilicev ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Type I ◽  
Muscle Type ◽  
Selective Agonist ◽  
Thyroid Hormone Receptor Β

Cloning and characterization of mouse 5′-AMP-activated protein kinase γ3 subunit

2004 ◽  
Vol 286 (2) ◽  
pp. C283-C292 ◽  
Author(s):  
Haiyan Yu ◽  
Nobuharu Fujii ◽  
Michael F. Hirshman ◽  
Jason M. Pomerleau ◽  
Laurie J. Goodyear
Keyword(s):  
Skeletal Muscle ◽  
Catalytic Activity ◽  
Protein Kinase ◽  
Muscle Glycogen ◽  
Short Form ◽  
Type I ◽  
Muscle Type ◽  
Γ Subunit ◽  
Amp Activated Protein Kinase ◽  
Fast Twitch

Naturally occurring mutations in the regulatory γ-subunit of 5′-AMP-activated protein kinase (AMPK) can result in pronounced pathological changes that may stem from increases in muscle glycogen levels, making it critical to understand the role(s) of the γ-subunit in AMPK function. In this study we cloned the mouse AMPKγ3 subunit and revealed that there are two transcription start sites, which result in a long form, γ3L (AF525500) and a short form, γ3S (AF525501). AMPKγ3L is the predominant form in mouse and is specifically expressed in mouse skeletal muscle at the protein level. In skeletal muscle, AMPKγ3 shows higher levels of expression in fast-twitch white glycolytic muscle (type IIb) compared with fast-twitch red oxidative glycolytic muscle (type IIa), whereas γ3 is undetectable in soleus muscle, a slow-twitch oxidative muscle with predominantly type I fibers. AMPKγ3 can coimmunoprecipititate with both α and β AMPK subunits. Overexpression of γ3S and γ3L in mouse tibialis anterior muscle in vivo has no effect on α1 and α2 subunit expression and does not alter AMPKα2 catalytic activity. However, γ3S and γ3L overexpression significantly increases AMPKα1 phosphorylation and activity by ∼50%. The increase in AMPKα1 activity is not associated with alterations in glycogen accumulation or glycogen synthase expression. In conclusion, the γ3 subunit of AMPK is highly expressed in fast-twitch glycolytic skeletal muscle, and wild-type γ3 functions in the regulation of α1 catalytic activity, but it is not associated with changes in muscle glycogen concentrations.

GLYCOGEN REPLETION OF HUMAN SKELETAL MUSCLE TYPE I, IIA AND IIB FIBERS FOLLOWING ENDURANCE EXERCISE

1995 ◽  
Vol 27 (Supplement) ◽  
pp. S4
Author(s):  
J.-F. Néron ◽  
J. Cléroux ◽  
A. Nadeau ◽  
Y. Lacourcière ◽  
J.-A. Simoneau
Keyword(s):  
Skeletal Muscle ◽  
Endurance Exercise ◽  
Human Skeletal Muscle ◽  
Type I ◽  
Muscle Type ◽  
Glycogen Repletion

Plasma and skeletal muscle free amino acids in type I, insulin-treated diabetic subjects

Diabetes ◽  
1985 ◽  
Vol 34 (8) ◽  
pp. 812-815 ◽  
Author(s):  
L. Borghi ◽  
R. Lugari ◽  
A. Montanari ◽  
P. Dall'Argine ◽  
G. F. Elia ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Type I

Slow skeletal muscle myosin-binding protein-C (MyBPC1) mediates recruitment of muscle-type creatine kinase (CK) to myosin

2011 ◽  
Vol 436 (2) ◽  
pp. 437-445 ◽  
Author(s):  
Zhe Chen ◽  
Tong-Jin Zhao ◽  
Jie Li ◽  
Yan-Song Gao ◽  
Fan-Guo Meng ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Muscle Contraction ◽  
Binding Protein ◽  
High Energy ◽  
Functional Coupling ◽  
Muscle Type ◽  
Myosin Binding Protein ◽  
Slow Skeletal Muscle ◽  
Myosin Binding

Muscle contraction requires high energy fluxes, which are supplied by MM-CK (muscle-type creatine kinase) which couples to the myofibril. However, little is known about the detailed molecular mechanisms of how MM-CK participates in and is regulated during muscle contraction. In the present study, MM-CK is found to physically interact with the slow skeletal muscle-type MyBPC1 (myosin-binding protein C1). The interaction between MyBPC1 and MM-CK depended on the creatine concentration in a dose-dependent manner, but not on ATP, ADP or phosphocreatine. The MyBPC1–CK interaction favoured acidic conditions, and the two molecules dissociated at above pH 7.5. Domain-mapping experiments indicated that MM-CK binds to the C-terminal domains of MyBPC1, which is also the binding site of myosin. The functional coupling of myosin, MyBPC1 and MM-CK is further corroborated using an ATPase activity assay in which ATP expenditure accelerates upon the association of the three proteins, and the apparent Km value of myosin is therefore reduced. The results of the present study suggest that MyBPC1 acts as an adaptor to connect the ATP consumer (myosin) and the regenerator (MM-CK) for efficient energy metabolism and homoeostasis.

Effect of Early Low-Intensity Exercise on Rat Hind-Limb Muscles Following Acute Ischemic Stroke

2006 ◽  
Vol 7 (3) ◽  
pp. 163-174 ◽  
Author(s):  
Myoung-Ae Choe ◽  
Gyeong Ju An ◽  
Yoon-Kyong Lee ◽  
Ji Hye Im ◽  
Smi Choi-Kwon ◽  
...  
Keyword(s):  
Hind Limb ◽  
Gastrocnemius Muscle ◽  
Exercise Group ◽  
Cross Sectional Area ◽  
Type I ◽  
Sectional Area ◽  
Muscle Type ◽  
Cross Sectional ◽  
Low Intensity ◽  
Low Intensity Exercise

This study examined the effects of daily low-intensity exercise following acute stroke on mass, Type I and II fiber cross-sectional area, and myofibrillar protein content of hind-limb muscles in a rat model. Adult male Sprague-Dawley rats were randomly assigned to 1 of 4 groups (n = 7-9 per group): stroke (occlusion of the right middle cerebral artery [RMCA]), control (sham RMCA procedure), exercise, and stroke-exercise. Beginning 48 hours post-stroke induction/sham operation, rats in the exercise group had 6 sessions of exercise in which they ran on a treadmill at grade 10 for 20 min/day at 10 m/min. At 8 days poststroke, all rats were anesthetized and soleus, plantaris, and gastrocnemius muscles were dissected from both the affected and unaffected sides. After 6 sessions of exercise following acute ischemic stroke, the stroke-exercise group showed the following significant (p < .05) increases compared to the stroke-only group: body weight and dietary intake, muscle weight of affected soleus and both affected and unaffected gastrocnemius muscle, Type I fiber cross-sectional area of affected soleus and both affected and unaffected gastrocnemius muscle, Type II fiber cross-sectional area of the unaffected soleus, both affected and unaffected plantaris and gastrocnemius muscle, Type II fiber distribution of affected gastrocnemius muscle, and myofibrillar protein content of both affected and unaffected soleus muscle. Daily low-intensity exercise following acute stroke attenuates hind-limb muscle atrophy in both affected and unaffected sides. The effects of exercise are more pronounced in the soleus and gastrocnemius as compared to the plantaris muscle.

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