Molecular basis of the oxygen exchange from carbon dioxide catalyzed by carbonic anhydrase III from bovine skeletal muscle

Biochemistry ◽  
1986 ◽  
Vol 25 (26) ◽  
pp. 8402-8408 ◽  
Author(s):  
D. N. Silverman ◽  
C. K. Tu
Keyword(s):  
Carbon Dioxide ◽  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Molecular Basis ◽  
Oxygen Exchange ◽  
Carbonic Anhydrase Iii ◽  
Bovine Skeletal Muscle

Carbonic anhydrase III inhibition in normocapnic and hypercapnic contracting mouse soleus

1987 ◽  
Vol 65 (1) ◽  
pp. 100-104 ◽  
Author(s):  
J. K. Barclay
Keyword(s):  
Carbon Dioxide ◽  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Physiological Role ◽  
Final Concentration ◽  
Solution Ph ◽  
Hydrogen Ion Concentration ◽  
Carbonic Anhydrase Iii ◽  
Slow Twitch ◽  
Sodium Cyanate

The physiological role of carbonic anhydrase III in slow-twitch skeletal muscle was investigated using isolated mouse soleus (N = 30) contracting once every 1.7 min for 75 min in Krebs–Henseleit solution gassed with either 95% oxygen – 5% carbon dioxide (normocapnia) or 90% oxygen – 10% carbon dioxide (hypercapnia). Each contraction was 500 ms in duration at 50 Hz. When muscles contracted in normocapnic solution (pH 7.42), the developed tension decreased an average of 6.1 ± 0.8% over 25 min. For the next 50 min, 15 muscles remained normocapnic, while the remainder contracted in hypercapnic solution (pH 7.20). Tension decreased significantly more with hypercapnia. For the last 25 min, both normocapnic and hypercapnic muscles were divided into three treatment groups (N = 5). One group continued in the same environment, while acetazolamide (final concentration of 10−5 M) was added to the bath of the second and sodium cyanate (final concentration of 10−5 M) was added to the bath of the third group. Acetazolamide had no effect on tension in either carbon dioxide environment. Sodium cyanate significantly decreased tension from the hypercapnic control but had no effect in normocapnia. Thus carbonic anhydrase III inhibition with sodium cyanate increased the effect of hypercapnia implying that carbonic anhydrase III assists in the regulation of free hydrogen ion concentration in slow-twitch skeletal muscle.

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
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