Membrane-bound carbonic anhydrase in the heart

Bruns, W.; Gros, Gerolf

doi:10.1152/ajpheart.1992.262.2.h577

Cited by 15 publications

(27 citation statements)

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“…Soluble proteins like CAI and CAII from red cell lysate partition into the water phase in this experiment (left-hand column), whereas membrane-bound CA from heart sarcolemmal vesicles partitions into the Triton phase (right-hand column in Fig.·1; data from Bruns and Gros, 1992). Figure·1 shows the results for mucus samples from caecum and colon of guinea-pigs.…”

Section: Resultsmentioning

confidence: 84%

A distinct carbonic anhydrase in the mucus of the colon of humans and other mammals

Kleinke

Wagner

John³

et al. 2005

Journal of Experimental Biology

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SUMMARY We have collected gastrointestinal, mainly colonic, mucus from humans,guinea pigs, rats, and normal and carbonic anhydrase II (CAII)-deficient mice. In the mucus of all species, substantial CA activity was present. Using antibodies against human CA isoforms we found that the human mucus CA differs from cytosolic CAI and CAII, membrane-bound CAIV, and the secreted CAVI of saliva. The high sensitivity of mucus CA to acetazolamide rules out its identity with cytosolic CAIII. Partial sequences obtained from the purified human mucus CA show similarity, but not identity, with human CAI, and clear differences from the other known CAs. Additional evidence concerning the CA isoform present in mucus was obtained for the mucus CA of other species and was derived from: (1) the mucus of CAII-deficient mice, whose high CA activity confirms that it is not CAII that is responsible; (2) the inhibitory effect of iodide, which shows that mucus CA from mice, guinea pig and humans does not have the high anion sensitivity of CAI; (3) the inactivating effect of 0.2%SDS on guinea pig, mouse and human mucus CA, ruling out the SDS-resistant CAIV; and (4) the partitioning of guinea-pig mucus CA into the water phase in Triton X114 phase separation experiments, which also argues against its identity with membrane-bound CAs, such as CAIV. A comparison of colonic mucus CA activity in normal and germ-free rats indicates that the mucus CA is not of bacterial origin but is produced by the gastrointestinal tissues. We conclude(from its immunoreactivity, from iodide inhibition and from partial amino acid sequences) that mucus CA of human origin probably represents an isozyme, which is specific for mucus and is not identical with the known CA isozymes. The results obtained for mucus CA of other species collectively point in the same direction.

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Section: Resultsmentioning

confidence: 84%

A distinct carbonic anhydrase in the mucus of the colon of humans and other mammals

Kleinke

Wagner

John³

et al. 2005

Journal of Experimental Biology

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“…However, in cryosections of rabbit heart, Bruns and Gros (1992) did report an intracellular staining for CA with dansylsulfonamide (DNSA), a fluorescent CA inhibitor. The staining appeared to be associated with intracellular structures and was interpreted as a positive reaction of SR and T-tubules.…”

Section: Ca IV In the Sarcoplasmic Reticulummentioning

confidence: 99%

“…In contrast to mammalian skeletal muscle, no cytosolic form of CA was detectable in cardiac muscle, but high CA activity was found in the membrane fraction of heart muscle homogenates (Geers et al 1992). Bruns and Gros (1992) described CA activity in sarcolemmal and sarcoplasmic reticulum vesicles from bovine hearts and, in addition, presented histochemical evidence for an intracellular membrane-bound CA.…”

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confidence: 99%

Localization of Carbonic Anhydrase IV in Rat and Human Heart Muscle

Sender

Decker

Fenske

et al. 1998

J Histochem Cytochem.

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We investigated carbonic anhydrase IV (CA IV) in rat and human heart with immunohistochemical methods by both light and electron microscopy. In cryosections that were incubated with anti-CA IV/FITC, the capillaries showed a strong reaction for CA IV. In paraffin and semithin sections treated with anti-CA IV/ABC (avidin-biotin-peroxidase complex) blood vessels, capillaries, and sarcolemma (SL) were positively stained. By staining ultrathin sections with anti-CA IV/immunogold, CA IV could also be demonstrated at the latter two locations, including the specialized sarcolemmal structures intercalated discs, and T-tubules. In addition, by this method CA IV was seen to be associated with the sarcoplasmic reticulum (SR). The absence of immunostaining in SR and/or SL with some techniques probably indicates a problem of accessibility of the antigenic sites. In line with the immunohistochemical results, CA IV mRNA expression was visualized in both endothelial and muscle cells by in situ hybridization histochemistry.

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“…These authors hypothesized that pCO 2 was higher in the proximity of the central veins and that more active hydration of CO 2 was needed. Besides a similar role in the mouse embryonic and fetal labelled myocardium, one can speculate whether CA II in myocytes could also have the other functions mentioned for CA IV -buffering function, facilitation of CO 2 diffusion, or a role in uptake of substrates such as fatty acid or lactic acid (Bruns et Gros 1992).…”

Section: Ca II Expression In the Left Ventricular Myocardiummentioning

confidence: 97%

“…In adult heart CA IV was described for the first time in the bovine cardiac sarcolemma by Bruns and Gros (1992). Organ-RNA blots of adult rat showed abundant CA IV expression in the heart (Fleming et al 1993).…”

Section: Ca II Expression In the Left Ventricular Myocardiummentioning

confidence: 99%

Carbonic anhydrase II expression pattern in mouse embryonic and fetal heart

Vuillemin

Pexieder

1997

Anatomy and Embryology

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Carbonic anhydrase II localization was studied in mouse embryonic and fetal hearts for better understanding of the functions of this enzyme during cardiac organogenesis. Immunocytolabelling was performed on serial sections of frozen hearts after one night's fixation in 4% paraformaldehyde. In the earliest stages studied, 10, 11 and 12 ed (ed = embryonic day; vaginal plug = day 1), a sharp decrease of labelled cells was observed in the endocardium form which cushion-tissue mesenchyme is derived. During the same period, differences in the decreasing frequencies of labelled cells were also observed between three different cushion-tissue mesenchyme localizations: immunostained cells were abundant in the atrioventricular cushions, less numerous in the proximal part of the conotruncal ridges and rare in their distal part. From 13 ed their repartition was more regular along the conotruncus. From 13 to 16 ed the signal was also present in a peculiar region of the myocardium: the anterior and left walls of the left ventricle. At the 18 and 20 ed labelling was found only in some endothelial cells of coronary vessels, particularly in the interventricular septum. The pattern of expression of carbonic anhydrase II in activated endothelial cells and endothelial-derived mesenchyme cells of the cardiac cushion tissue, strongly suggests that this isoenzyme can be a useful marker for a subpopulation of endothelial cells and cells derived from this endothelium that morphologically express signs of active cell behavior (e.g., invasion, migration, proliferation).

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Membrane-bound carbonic anhydrase in the heart

Cited by 15 publications

References 0 publications

A distinct carbonic anhydrase in the mucus of the colon of humans and other mammals

A distinct carbonic anhydrase in the mucus of the colon of humans and other mammals

Localization of Carbonic Anhydrase IV in Rat and Human Heart Muscle

Carbonic anhydrase II expression pattern in mouse embryonic and fetal heart

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