Immunoelectron microscopic localization of carbonic anhydrase III in rat skeletal muscle

1986 ◽  
Vol 86 (2) ◽  
pp. 175-179 ◽  
Author(s):  
H. K. V��n�nen ◽  
T. Takala ◽  
D. C. Morris
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Rat Skeletal Muscle ◽  
Microscopic Localization ◽  
Carbonic Anhydrase Iii

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.

scholarly journals Extracellular carbonic anhydrase activity facilitates lactic acid transport in rat skeletal muscle fibres

2001 ◽  
Vol 531 (3) ◽  
pp. 743-756 ◽  
Author(s):  
Petra Wetzel ◽  
Anke Hasse ◽  
Simon Papadopoulos ◽  
Juha Voipio ◽  
Kai Kaila ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Lactic Acid ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Activity ◽  
Muscle Fibres ◽  
Acid Transport ◽  
Rat Skeletal Muscle ◽  
Skeletal Muscle Fibres

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.

Rat skeletal muscle membrane associated carbonic anhydrase is 39-kDa, glycosylated, GPI-anchored CA IV

1992 ◽  
Vol 294 (2) ◽  
pp. 550-556 ◽  
Author(s):  
Abdul Waheed ◽  
Xin Liang Zhu ◽  
William S. Sly ◽  
Petra Wetzel ◽  
Gerolf Gros
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Muscle Membrane ◽  
Rat Skeletal Muscle

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.

scholarly journals Immunocytochemical localization of carbonic anhydrase isozymes I, II, and III in rat skeletal muscle.

1986 ◽  
Vol 34 (4) ◽  
pp. 513-516 ◽  
Author(s):  
S Jeffery ◽  
N D Carter ◽  
A Smith
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Skeletal Muscle Fiber ◽  
Muscle Fiber Types ◽  
Type I ◽  
Fiber Types ◽  
Rat Skeletal Muscle ◽  
Specific Antisera ◽  
Type I Fibers ◽  
Atpase Staining

Specific antisera were raised against the three carbonic anhydrase (CA) isozymes, CAI, CAII, and CAIII, and were used to determine the fiber distribution of these isozymes in skeletal muscle. Fiber types were determined by ATPase staining, and the CA isozymes were detected using a peroxidase-anti-peroxidase (PAP) technique. All three isozymes were present in type I fibers; CAII and CAIII were exclusive to these fibers, and CAI were also present in some small type 2A fibers.

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
Sign in / Sign up

Export Citation Format

Share Document