scholarly journals Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification

1984 ◽  
Vol 4 (7) ◽  
pp. 573-579 ◽  
Author(s):  
Richard E. Tashian ◽  
Jack T. Johansen ◽  
Erik Christiansen ◽  
W. Richard Chegwidden
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Active Sites ◽  
Mammalian Skeletal Muscle ◽  
Carbonic Anhydrase Iii ◽  
Dehydration Reactions ◽  
Arginine Modification ◽  
Specific Activities ◽  
Arginyl Residues

Purified carbonic anhydrase isozymes I, II, and III (CA I, CA II, CA III) from various sources were treated with 2,3-butanedione and their bicarbonate dehydration reactions followed. The specific activities of human and bovine CA I and CA II and chicken CA III were not affected by the butanedione treatment, whereas the activities of human, gorilla, and bovine CA III were rapidly activated. These findings suggest that one, or both, of the two arginyl residues which appear to be unique to the active sites of the mammalian CA III isozymes are modified by butanedione.

scholarly journals Metabolic and contractile influence of carbonic anhydrase III in skeletal muscle is age dependent

1999 ◽  
Vol 276 (2) ◽  
pp. R559-R565 ◽  
Author(s):  
Claude H. Côté ◽  
Fabrisia Ambrosio ◽  
Guylaine Perreault
Keyword(s):  
Skeletal Muscle ◽  
Data Analysis ◽  
Carbonic Anhydrase ◽  
Soleus Muscle ◽  
Type I ◽  
Carbonic Anhydrase Iii ◽  
Age Dependent ◽  
Old Rats ◽  
Birth Data

Carbonic anhydrase (CA) III is very abundant in type I skeletal muscle, but its function is still debated. Our aims were to examine CA III expression during growth and determine whether the effects of CA inhibition previously observed in adult muscles could be seen in younger rats in which CA III levels are lower. CA III content and activity were measured in soleus muscles from 10- to 100-day-old rats, and the influence of CA inhibitor on fatigue and hexosemonophosphate content was quantified in vitro. CA III activity and content increased fivefold between 10 and 100 days of age. Data analysis revealed that the influence of CA inhibitor on fatigue was to some extent positively and linearly related to the level of CA III activity. Hexosemonophosphate accumulation with CA inhibition also became more significant with age. In conclusion, CA III level in soleus muscle does not stabilize before 3 mo after birth; data also confirm that the effects of CA inhibitors are due to inhibition of the CA III isoform.

scholarly journals Carbonic anhydrase III in skeletal muscle fibers: an immunocytochemical and biochemical study.

1988 ◽  
Vol 36 (7) ◽  
pp. 775-782 ◽  
Author(s):  
P Frémont ◽  
P M Charest ◽  
C Côté ◽  
P A Rogers
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Vastus Lateralis ◽  
Muscle Fibers ◽  
Water Soluble ◽  
Type I ◽  
Fiber Types ◽  
Thin Sections ◽  
Carbonic Anhydrase Iii ◽  
Skeletal Muscle Fibers

The objectives of the present study were to determine if carbonic anhydrase III (CA III) demonstrated a specific association for any particular organelle or structure of the skeletal muscle cell and to quantify the activity and content of this enzyme in different types of skeletal muscle fibers. Ultrastructural localization of CA III in the soleus (SOL), deep vastus lateralis (DVL), and superficial vastus lateralis (SVL), composed of predominantly type I, IIa, and IIb fibers, respectively, was performed using a high-resolution immunocytochemical technique and antibody specific for CA III on ultra-thin sections of skeletal muscle embedded in the water-soluble medium polyvinyl alcohol (PVA). The results indicated a uniform distribution of CA III within the sarcomere. Mitochondria, nuclei, triads, Z-, and M-bands were not specifically labeled. Immunoblotting of washed myofibril preparations did not show any detectable CA III associated with this structure. In addition to quantification of the immunogold labeling, CA III activity and content were assayed in the post-mitochondrial supernatant of the three muscles. In the SOL, these values were found to be 3.6-7.6 times higher than in the DVL. The SVL showed a labeling intensity slightly higher than background level, while the enzyme activity and content were indistinguishable from background levels. We therefore conclude that CA III is randomly distributed in the cytoplasm of the three muscle fiber types and that the relative CA III content and activity in the three muscles studied is SOL greater than DVL greater than SVL approximately equal to 0.

Characterization of human carbonic anhydrase III from skeletal muscle

1979 ◽  
Vol 17 (9-10) ◽  
pp. 837-854 ◽  
Author(s):  
Nicholas Carter ◽  
Stephen Jeffery ◽  
Alan Shiels ◽  
Yvonne Edwards ◽  
Terry Tipler ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

scholarly journals Expression of carbonic anhydrase III and skeletal muscle remodeling following selective denervation

2017 ◽  
Vol 16 (6) ◽  
pp. 8289-8294 ◽  
Author(s):  
He Huang ◽  
Yanling Zhao ◽  
Xiliang Shang ◽  
Xueyuan Liu ◽  
Huimin Ren
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Iii ◽  
Muscle Remodeling

scholarly journals Detection of CAIII mRNA in rat skeletal muscle and liver by in situ hybridization.

1991 ◽  
Vol 39 (9) ◽  
pp. 1243-1247 ◽  
Author(s):  
C D Kelly ◽  
N D Carter ◽  
P de Boer ◽  
S Jeffery ◽  
A F Moorman ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
In Situ Hybridization ◽  
Carbonic Anhydrase ◽  
Cdna Probe ◽  
Rat Skeletal Muscle ◽  
Carbonic Anhydrase Iii ◽  
In Situ Methods ◽  
Muscle Section ◽  
Biotinylated Cdna Probe

We carried out a variety of in situ methods of hybridization on rat liver and rat skeletal muscle using 35S-labeled or biotin-labeled rat carbonic anhydrase III (CAIII) cDNA clone. The methods were compared and evaluated. Use of the biotin system produced defined but nonspecific results which were shown not to be due to the biotinylated cDNA probe binding to the mRNA in the muscle sections. This artifact was shown to persist despite various attempts to eliminate it. Alternatively, using 35S-labeled cDNA gave reproducible results which were shown to be consistent with probe binding specifically to mRNA in the muscle section.

Serum carbonic anhydrase III and myoglobin concentrations in acute myocardial infarction

1990 ◽  
Vol 36 (4) ◽  
pp. 635-638 ◽  
Author(s):  
H K Väänänen ◽  
H Syrjälä ◽  
P Rahkila ◽  
J Vuori ◽  
L M Melamies ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Skeletal Muscle ◽  
Acute Myocardial Infarction ◽  
Carbonic Anhydrase ◽  
Physical Exercise ◽  
Healthy Subjects ◽  
Neuromuscular Diseases ◽  
Specific Protein ◽  
Carbonic Anhydrase Iii ◽  
Before And After

Abstract Serum concentrations of myoglobin (S-Myo) and carbonic anhydrase III (S-CA III; EC 4.2.1.1), a skeletal muscle-specific protein, were measured by RIA in 26 patients with acute myocardial infarction, 14 patients with neuromuscular diseases, and six healthy subjects before and after physical exercise. S-Myo was increased in infarct patients, whereas S-CA III was not altered. In patients with neuromuscular diseases and in healthy subjects after physical exercise, both S-Myo and S-CA III were significantly increased. S-CA III and S-Myo also showed identical peak times, 2 h postexercise. The S-Myo/S-CA III ratio was always higher in infarct patients than in the other groups. Thus, the combination of S-CA III and S-Myo determinations is useful to differentiate whether serum myoglobin is originating from myocardium or from skeletal muscle.

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