Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes.

Okuyama, Torayuki; Sato, Seiji; Zhu, Xin Liang; Waheed, Abdül; Sly, William S.

doi:10.1073/pnas.89.4.1315

Cited by 77 publications

(63 citation statements)

References 42 publications

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“…The issue became confused when Wolfensberger et al (12) reported a 54-kDa protein in human retina, which they called CA IV. Because human CA IV is a 35-kDa nonglycosylated protein (25), it seems likely they misidentified CA XIV as CA IV, because the former had not yet been identified. From our own studies and those of Ochrietor et al (15), it is clear that CA XIV is the major membrane-associated CA in retina.…”

Section: Discussionmentioning

confidence: 99%

Carbonic anhydrase XIV is enriched in specific membrane domains of retinal pigment epithelium, Müller cells, and astrocytes

Nagelhus

Mathiisen

Bateman

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionmentioning

confidence: 99%

Carbonic anhydrase XIV is enriched in specific membrane domains of retinal pigment epithelium, Müller cells, and astrocytes

Nagelhus

Mathiisen

Bateman

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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“…The deduced amino acid sequence includes an 18-residue signal sequence, a 260-residue segment exhibiting 30-36% sequence identity with other human carbonic anhydrase isozymes, and an additional 27-residue segment at the C terminus containing a 21-residue hydrophobic domain. The C-terminal domain likely specifies the association of CA IV with the membrane and contains a signal for posttranslational cleavage and transfer to the GPI anchor (18). Removal of the C-terminal domain results in a fully active, soluble, secretory form of CA IV with catalytic properties identical to those of GPI-anchored CA IV (19).…”

mentioning

confidence: 99%

“…The CA IV isozyme contains two disulfide linkages which contribute to its remarkable stability upon solubilization in 5% sodium dodecyl sulfate (SDS) (12,17). The full-length cDNA for human CA IV has been isolated from a gt10 kidney cDNA library and expressed in COS cells (18). The deduced amino acid sequence includes an 18-residue signal sequence, a 260-residue segment exhibiting 30-36% sequence identity with other human carbonic anhydrase isozymes, and an additional 27-residue segment at the C terminus containing a 21-residue hydrophobic domain.…”

mentioning

confidence: 99%

Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-Å resolution

Stams

Nair

Okuyama

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

138

118

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It has recently been demonstrated that the C-terminal deletion mutant of recombinant human carbonic anhydrase IV (G267X CA IV) converts the normally glycosylphosphatidylinositol-anchored enzyme into a soluble secretory form which has the same catalytic properties as the membrane-associated enzyme purified from human tissues. We have determined the three-dimensional structure of the secretory form of human CA IV by x-ray crystallographic methods to a resolution of 2.8 Å. Although the zinc binding site and the hydrophobic substrate binding pocket of CA IV are generally similar to those of other mammalian isozymes, unique structural differences are found elsewhere in the active site. Two disufide linkages, Cys-6-Cys-11G and Cys-23-Cys-203, stabilize the conformation of the N-terminal domain. The latter disulfide additionally stabilizes an active site loop containing a cis-peptide linkage between Pro-201 and Thr-202 (this loop contains catalytic residue Thr-199). On the opposite side of the active site, the Val-131-Asp-136 segment adopts an extended loop conformation instead of an ␣-helix conformation as found in other isozymes. Finally, the C terminus is surrounded by a substantial electropositive surface potential, which is likely to stabilize the interaction of CA IV with the negatively charged phospholipid headgroups of the membrane. These structural features are unique to CA IV and provide a framework for the design of sulfonamide inhibitors selective for this particular isozyme.

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“…These results sug- gest that the CA II associated with apical plasma membranes of Capan-1 cells is bound to the inner leaflet. CA IV has been shown to be situated on the outer leaflet in many cell types, in line with the description of this enzyme as a GPI-anchored protein (Zhu and Sly 1990;Ghandour et al 1992;Okuyama et al 1992;Mairal et al 1996). On electron microscopic examination, the CA activity after the Hansson's reaction on both inner and outer leaflets of apical plasma membranes of Capan-1 cells was thought to indicate sites of activity of CA II and CA IV, respectively.…”

Section: Discussionmentioning

confidence: 73%

Carbonic Anhydrase II Associated with Plasma Membrane in a Human Pancreatic Duct Cell Line (CAPAN-1)

Alvarez

Fanjul

Carter

et al. 2001

J Histochem Cytochem.

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S U M M A R YThe subcellular distribution of carbonic anhydrase II, either throughout the cytosol or in the cytoplasm close to the apical plasma membrane or vesicular compartments, suggests that this enzyme may have different roles in the regulation of pH in intra-or extracellular compartments. To throw more light on the role of pancreatic carbonic anhydrase II, we examined its expression and subcellular distribution in Capan-1 cells. Immunocytochemical analysis by light, confocal, and electron microscopy, as well as immunoblotting of cell homogenates or purified plasma membranes, was performed. A carbonic anhydrase II of 29 kD associated by weak bonds to the inner leaflet of apical plasma membranes of polarized cells was detected. This enzyme was co-localized with markers of Golgi compartments. Moreover, the defect of its targeting to apical plasma membranes in cells treated with brefeldin A was indicative of its transport by the Golgi apparatus. We show here that a carbonic anhydrase II is associated with the inner leaflet of apical plasma membranes and with the cytosolic side of the endomembranes of human cancerous pancreatic duct cells (Capan-1). These observations point to a role for this enzyme in the regulation of intraand extracellular pH.

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Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes.

Cited by 77 publications

References 42 publications

Carbonic anhydrase XIV is enriched in specific membrane domains of retinal pigment epithelium, Müller cells, and astrocytes

Carbonic anhydrase XIV is enriched in specific membrane domains of retinal pigment epithelium, Müller cells, and astrocytes

Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-Å resolution

Carbonic Anhydrase II Associated with Plasma Membrane in a Human Pancreatic Duct Cell Line (CAPAN-1)

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