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:

				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]

				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]

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

				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]

				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]

				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]

				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]

				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]

				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]