Journal of Applied Physiology AJP: Gastrointestinal and Liver Physiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

J Appl Physiol 59: 548-558, 1985;
8750-7587/85 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Geers, C.
Right arrow Articles by Gartner, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Geers, C.
Right arrow Articles by Gartner, A.

Journal of Applied Physiology, Vol 59, Issue 2 548-558, Copyright © 1985 by American Physiological Society

ARTICLES

Extracellular carbonic anhydrase of skeletal muscle associated with the sarcolemma

C. Geers, G. Gros and A. Gartner

We report here 1) the synthesis and properties of a new macromolecular carbonic anhydrase inhibitor, Prontosil-dextran, 2) its application to determine the localization of a previously described extracellular carbonic anhydrase in skeletal muscle, and 3) the application of a recently published histochemical technique using dansylsulfonamide to the same problem. Stable macromolecular inhibitors of molecular weights of 5,000, 100,000 and 1,000,000 were produced by covalently coupling the sulfonamide Prontosil to dextrans. Their inhibition constants towards bovine carbonic anhydrase II are 1-2 X 10(-7) M. The Prontosil-dextrans, PD 5,000, PD 100,000, and PD 1,000,000, were used in studies of the washout of H14CO3-) from the perfused rabbit hindlimb. This washout is slow due to the presence of an extracellular carbonic anhydrase and can be markedly accelerated by PD 5,000 but not by PD 100,000 and PD 1,000,000. Since PD 5,000 is accessible to the entire extracellular space and PD 100,000 and PD 1,000,000 are confined to the intravascular space, we conclude that the extracellular carbonic anhydrase of skeletal muscle is located in the interstitium. The histochemical studies show a strong staining of the sarcolemma of the muscle fibers with high oxidative capacity. It appears likely, therefore, that the extracellular carbonic anhydrase of skeletal muscle is associated with muscle plasma membranes with its active site directed toward the interstitial space.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Cell Physiol.Home page
R. J. Scheibe, K. Mundhenk, T. Becker, J. Hallerdei, A. Waheed, G. N. Shah, W. S. Sly, G. Gros, and P. Wetzel
Carbonic anhydrases IV and IX: subcellular localization and functional role in mouse skeletal muscle
Am J Physiol Cell Physiol, February 1, 2008; 294(2): C402 - C412.
[Abstract] [Full Text] [PDF]

Home page
 J. Pharmacol. Exp. Ther.Home page
R. Radhakrishnan and K. A. Sluka
Acetazolamide, a Carbonic Anhydrase Inhibitor, Reverses Inflammation-Induced Thermal Hyperalgesia in Rats
J. Pharmacol. Exp. Ther., May 1, 2005; 313(2): 921 - 927.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
M. CHESLER
Regulation and Modulation of pH in the Brain
Physiol Rev, October 1, 2003; 83(4): 1183 - 1221.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
E. R. Swenson, T. W. Tewson, P. J. Wistrand, Y. Ridderstrale, and C. Tu
Biochemical, histological, and inhibitor studies of membrane carbonic anhydrase in frog gastric acid secretion
Am J Physiol Gastrointest Liver Physiol, July 1, 2001; 281(1): G61 - G68.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
P. Wetzel, A. Hasse, S. Papadopoulos, J. Voipio, K. Kaila, and G. Gros
Extracellular carbonic anhydrase activity facilitates lactic acid transport in rat skeletal muscle fibres
J. Physiol., March 15, 2001; 531(3): 743 - 756.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
G. J. Schwartz, A. M. Kittelberger, D. A. Barnhart, and S. Vijayakumar
Carbonic anhydrase IV is expressed in H+-secreting cells of rabbit kidney
Am J Physiol Renal Physiol, June 1, 2000; 278(6): F894 - F904.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
C. Geers and G. Gros
Carbon Dioxide Transport and Carbonic Anhydrase in Blood and Muscle
Physiol Rev, April 1, 2000; 80(2): 681 - 715.
[Abstract] [Full Text] [PDF]

Home page
 J. Exp. Biol.Home page
T Peters, R. Forster, and G Gros
Hagfish (Myxine glutinosa) red cell membrane exhibits no bicarbonate permeability as detected by (18)O exchange
J. Exp. Biol., January 5, 2000; 203(10): 1551 - 1560.
[Abstract] [PDF]

Home page
 Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
C. H. Cote, G. Perreault, and J. Frenette
Carbohydrate utilization in rat soleus muscle is influenced by carbonic anhydrase III activity
Am J Physiol Regulatory Integrative Comp Physiol, October 1, 1997; 273(4): R1211 - R1218.
[Abstract] [Full Text] [PDF]

Home page
 J. Pharmacol. Exp. Ther.Home page
T. H. Maren, C. W. Conroy, G. C. Wynns, and D. R. Godman
Renal and Cerebrospinal Fluid Formation Pharmacology of a High Molecular Weight Carbonic Anhydrase Inhibitor
J. Pharmacol. Exp. Ther., January 1, 1997; 280(1): 98 - 104.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online