Carbonic anhydrase IV expression in rat and human gastrointestinal tract regional, cellular, and subcellular localization.

Fleming, Robert E.; Parkkila, Seppo; Parkkila, Anna‐Kaisa; Rajaniemi, Hannu; Waheed, Abdül; Sly, William S.

doi:10.1172/jci118362

Cited by 95 publications

(75 citation statements)

References 32 publications

(28 reference statements)

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“…One might predict that disruption of CA XII function would result in abnormal regulation of ion and pH homeostasis, because both kidney and colon play key roles in the maintenance of body electrolyte and pH balance. However, both organs also express a number of other CA isozymes such as CA II, CA IV, and CA XIV (Zhu and Sly, 1990;Parkkila et al, 1994;Fleming et al, 1995;Parkkila et al, 2002, Kyllönen et al, 2003Parkkila et al, 2003), which may compensate for the loss of one isozyme following a gene disruption. Although this potential functional redundancy makes predicting the phenotype of the mouse with a targeted gene disruption less straightforward, establishing whether and which CA genes are upregulated would provide a clue as to the functional importance of the disrupted gene.…”

Section: Discussionmentioning

confidence: 99%

“…Some isozymes such as CA II are expressed in a number of different tissues, whereas others (e.g., CA VI, IX, and XIV) show a more limited distribution. It is notable, however, that all active isozymes are expressed in the alimentary tract, although the cellular localization is unique for each isozyme (Parkkila et al, 1994;Fleming et al, 1995;Sly and Hu, 1995;Parkkila, 1996, Pastoreková et al, 1997;Kivelä et al, 2000;Parkkila et al, 2003).…”

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Expression of hypoxia‐inducible, membrane‐bound carbonic anhydrase isozyme XII in mouse tissues

et al. 2004

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Carbonic anhydrase (CA) XII is a membrane-associated enzyme that has been demonstrated to be normally expressed in some human tissues, to be upregulated in some cancers, and to be a hypoxia-inducible gene product. In mouse, CA XII has been recently localized in the kidney. In the present study, we investigated CA XII gene and protein expression in other mouse tissues, with the kidney serving as a positive control for the reagents. The expression of CA XII mRNA was examined using polymerase chain reaction (PCR) amplification of commercial cDNAs produced from selected mouse tissues. A strong positive signal for CA XII mRNA was detected in the kidney, and weak signals were obtained in the testis and lung. Heart, spleen, liver, and skeletal muscle were negative. Immunohistochemical staining was performed using a mouse CA XII-specific antibody and biotin-streptavidin complex method. The results showed high expression of CA XII in the kidney, as expected. It was also highly expressed in the surface epithelial cells of the colon, whereas it was absent in the stomach, proximal small intestine, pancreas, liver, heart, and skeletal muscle. The maturing sperm cells showed a weak staining in a pattern that most probably indicates expression in the developing acrosomal membrane. The high expression in the kidney and colon suggests a role for CA XII in the maintenance of body ion and pH homeostasis in the mouse. However, the present findings demonstrated that CA XII has a very limited distribution in mouse tissues outside these two organs. Anat Rec Part A 277A: 171-177, 2004.

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Expression of hypoxia‐inducible, membrane‐bound carbonic anhydrase isozyme XII in mouse tissues

et al. 2004

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“…The existence of at least four CA isozymes in this region (CA I and II in the cytosol, CA IV in the apical brush border, and CA XII in the basolateral plasma membrane) makes it difficult to define the individual role of each, but their cellular distribution suggests an important role in the absorption of water, which is the major physiological function of the colon. Fleming et al 19 proposed that apical CA IV may be functionally coupled with cytosolic CA I and II in the CO 2 -stimulated uptake of Na ϩ and Cl Ϫ by catalyzing the regeneration of CO 2 from excreted H ϩ and HCO 3 Ϫ at the luminal surface. This would provide additional CO 2 to further stimulate the absorption of NaCl and water.…”

Section: Discussionmentioning

confidence: 99%

Expression of a Novel Transmembrane Carbonic Anhydrase Isozyme XII in Normal Human Gut and Colorectal Tumors

Kivelä¹,

Parkkila²,

Saarnio³

et al. 2000

The American Journal of Pathology

148

117

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“…/ 5P16$$0038 10-10-96 12:51:21 hpta WBS: Hepatology gastrointestinal tract, 40 and epididymal ducts. 23,24 The enzyme also is present on the plasma face of endothelial cells of certain capillary beds, including lung, brain, eye, heart, skeletal muscle, epididymis, stomach, and gut.…”

Section: Aid Hepa 0038mentioning

confidence: 99%

Membrane-bound carbonic anhydrase IV is expressed in the luminal plasma membrane of the human gallbladder epithelium

Parkkila¹

1996

Hepatology

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(CO 2 / H 2 O B H / / HCO 0 3 ). At present, seven isoenzymes Alkaline hepatic bile is acidified in the gallbladder to differing in their tissue distribution and enzymatic activity prevent calcium precipitation and gallstone formation.have been identified from mammals. These include cytoBecause membrane-bound carbonic anhydrase (CA) isoplasmic CAs I, II, and III 11 ; membrane-associated CA IV 12-14 ; enzyme IV participates with cytoplasmic CA II in the mitochondrial CA V 15,16 ; and a secretory isoenzyme CA VI. 17,18 acidification of urine in the kidney, we studied its ex-The most recently identified isoenzyme CA IX, originally despression in different regions of the human biliary tract ignated MN protein, has been detected in the human gastric using immunohistochemical techniques. The enzyme mucosa. 19 was expressed in the apical plasma membrane of the Cytoplasmic, high-activity CA II is present in the gallbladgallbladder epithelial cells and in the endothelium of der epithelium, where it has been linked to the concentration the subepithelial capillaries. In the liver, some epithelial and acidification of alkaline hepatic bile. 20,21 The membranecells of the large bile ducts showed positive staining. Its associated CA IV might also be involved in these processes presence in the gallbladder epithelium could be conbecause it participates in urinary acidification in the kidney firmed by Western blotting, which showed a single 35-kd and epididymal fluid acidification in the epididymal ducts. 22-24 polypeptide band, corresponding in molecular weight to Earlier histochemical studies also suggested that a memthe intact enzyme. The majority of the enzyme was brane-associated CA is expressed in the gallbladder epithephased to Triton X-114 detergent phase. A small amount lium. 25 To achieve a more comprehensive view of the bile of 35-kd polypeptide was also seen in the water phase.acidification process, we studied the expression of CA IV in Smaller proteolytic fragments of the enzyme were not the human bile tract epithelium by immunohistochemistry. 1108.)staining, the liver specimens and the gallbladder specimens from different regions were immersion-fixed in 4% neutral-buffered formaldehyde for 18 hours and washed in 20% sucrose in phosphate-A number of studies have shown that gallstone formation buffered saline (PBS) for 24 hours. They were then frozen in liquid in humans is a multifactorial phenomenon. 1-4 Calcium salts, nitrogen, stored at 080ЊC, and cut at 8 mm (Cryo-Cut Microtome; the major components of pigment gallstones, 5 are also found American Optical Corporation, Buffalo, NY). For immunoperoxidase in the central nidus region of all cholesterol stones. 5,6 The staining, the formaldehyde-fixed specimens were dehydrated, emmost abundant biliary calcium salt is calcium carbonate, 7,8 bedded in paraffin in a vacuum oven at 58ЊC, and sectioned at 5 mm. which is precipitated when the bicarbonate concentration inAntisera and Immunohistochemical Methods. Polyclonal rabbit antiserum to human recombinant CA IV was u...

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Carbonic anhydrase IV expression in rat and human gastrointestinal tract regional, cellular, and subcellular localization.

Cited by 95 publications

References 32 publications

Expression of hypoxia‐inducible, membrane‐bound carbonic anhydrase isozyme XII in mouse tissues

Expression of hypoxia‐inducible, membrane‐bound carbonic anhydrase isozyme XII in mouse tissues

Expression of a Novel Transmembrane Carbonic Anhydrase Isozyme XII in Normal Human Gut and Colorectal Tumors

Membrane-bound carbonic anhydrase IV is expressed in the luminal plasma membrane of the human gallbladder epithelium

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