Variation in the pattern of carbonic anhydrase activity in the cells of the gastric glands

1974 ◽  
Vol 39 (4) ◽  
pp. 289-300 ◽  
Author(s):  
William B. Winborn ◽  
Leonard L. Seelig ◽  
Charles M. Girard
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Activity ◽  
Gastric Glands

Cellular localization of gastric intrinsic factor in the rat

1964 ◽  
Vol 206 (4) ◽  
pp. 783-786 ◽  
Author(s):  
Agna Boass ◽  
T. Hastings Wilson
Keyword(s):  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Cellular Localization ◽  
Tumor Tissue ◽  
Intrinsic Factor ◽  
Close Correlation ◽  
Carbonic Anhydrase Activity ◽  
Frozen Sections ◽  
Gastric Glands ◽  
Rat Gastric Mucosa

The distribution of carbonic anhydrase, pepsinogen, and intrinsic factor (IF) was studied in frozen sections of rat gastric mucosa using the method of Holter and Linderstrøm-Lang. Carbonic anhydrase activity was greatest in the sections nearest to the surface of the mucosa and less in the deeper regions of the glands. In contrast, the levels of both IF and pepsinogen were low at the surface and continued to increase to a maximum at the base of the gastric glands. The close correlation between the distribution of the concentrations of pepsinogen and IF suggests that the chief (zymogenic) cell may be the source of IF in the stomach of the rat. No IF was detected in human carcinoid tumor tissue. This absence of IF is consistent with the view that the argentaffine cell is not the source of IF.

1123: Renal Oxalate Transport Depends on Local Carbonic Anhydrase Activity in the Proximal Tubule

2004 ◽  
Vol 171 (4S) ◽  
pp. 296-296
Author(s):  
Michael Straub ◽  
Joséphine Befolo-Elo ◽  
Richard E Hautmann ◽  
Edgar Braendle
Keyword(s):  
Carbonic Anhydrase ◽  
Proximal Tubule ◽  
Carbonic Anhydrase Activity ◽  
Oxalate Transport

RENAL CARBONIC ANHYDRASE IN PREMATURE AND MATURE INFANTS

PEDIATRICS ◽  
1951 ◽  
Vol 7 (2) ◽  
pp. 182-185
Author(s):  
RICHARD DAY ◽  
JANE FRANKLIN
Keyword(s):  
Carbonic Anhydrase ◽  
Premature Infants ◽  
Carbonic Anhydrase Activity ◽  
Renal Carbonic Anhydrase

The carbonic anhydrase activity in the kidneys of premature infants was studied because it was thought that if the renal enzyme is as deficient as that in the blood, inefficiency in acidification of urine might result. In contrast with the blood, postmortem specimens of kidneys of premature infants were found to exhibit carbonic anhydrase activity similar to that found in the case of kidneys from older infants and adults.

The Effect of Cholera Toxin on Choroid Plexus Carbonic Anhydrase Activity In Vitro

1980 ◽  
Vol 1 (4) ◽  
pp. 333-339
Author(s):  
Arthur M. Feldman ◽  
Mel H. Epstein ◽  
Fallon Maylack ◽  
Saul W. Brusilow
Keyword(s):  
Carbonic Anhydrase ◽  
Choroid Plexus ◽  
Cholera Toxin ◽  
Carbonic Anhydrase Activity

scholarly journals The Periplasmic α-Carbonic Anhydrase Activity of Helicobacter pylori Is Essential for Acid Acclimation

2005 ◽  
Vol 187 (2) ◽  
pp. 729-738 ◽  
Author(s):  
Elizabeth A. Marcus ◽  
Amiel P. Moshfegh ◽  
George Sachs ◽  
David R. Scott
Keyword(s):  
Helicobacter Pylori ◽  
Membrane Potential ◽  
Carbonic Anhydrase ◽  
Membrane Integrity ◽  
Carbonic Anhydrase Activity ◽  
Knockout Mutant ◽  
Inner Membrane ◽  
Acid Acclimation

ABSTRACT The role of the periplasmic α-carbonic anhydrase (α-CA) (HP1186) in acid acclimation of Helicobacter pylori was investigated. Urease and urea influx through UreI have been shown to be essential for gastric colonization and for acid survival in vitro. Intrabacterial urease generation of NH3 has a major role in regulation of periplasmic pH and inner membrane potential under acidic conditions, allowing adequate bioenergetics for survival and growth. Since α-CA catalyzes the conversion of CO2 to HCO3 −, the role of CO2 in periplasmic buffering was studied using an α-CA deletion mutant and the CA inhibitor acetazolamide. Western analysis confirmed that α-CA was bound to the inner membrane. Immunoblots and PCR confirmed the absence of the enzyme and the gene in the α-CA knockout. In the mutant or in the presence of acetazolamide, there was an ∼3 log10 decrease in acid survival. In acid, absence of α-CA activity decreased membrane integrity, as observed using membrane-permeant and -impermeant fluorescent DNA dyes. The increase in membrane potential and cytoplasmic buffering following urea addition to wild-type organisms in acid was absent in the α-CA knockout mutant and in the presence of acetazolamide, although UreI and urease remained fully functional. At low pH, the elevation of cytoplasmic and periplasmic pH with urea was abolished in the absence of α-CA activity. Hence, buffering of the periplasm to a pH consistent with viability depends not only on NH3 efflux from the cytoplasm but also on the conversion of CO2, produced by urease, to HCO3 − by the periplasmic α-CA.

Sign in / Sign up

Export Citation Format

Share Document