Carbonic anhydrase (CA)-related proteins (CA-RPs), and transmembrane proteins with CA or CA-RP domains

Tashian, Richard E.; Hewett‐Emmett, David; Carter, Nick; Bergenhem, Nils

doi:10.1007/978-3-0348-8446-4_6

Cited by 58 publications

(42 citation statements)

References 49 publications

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“…This suggests that the CA-RPs are conserved between protostomes and deuterostomes and that active CA amplification took place after their divergence. Although CARPs lack CA activity, they are known to be highly conserved proteins, indicating that they serve a critical cellular function (Tashian et al, 2000). Interestingly, AgCA9 and its Drosophila and Aedes counterparts were the sole insect CAs that cluster with human CAs.…”

Section: Dar Cellsmentioning

confidence: 99%

Cloning and characterization of AgCA9, a novel α-carbonic anhydrase from Anopheles gambiae Giles sensu stricto (Diptera:Culicidae) larvae

Smith

VanEkeris

Linser

2007

Journal of Experimental Biology

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SUMMARY Mosquito larvae generate a luminal pH as high as 10.5 in the anterior region of their midgut. The mechanisms responsible for the generation and maintenance of this alkaline pH are largely unknown, but there is evidence suggesting a role for the enzyme carbonic anhydrase (CA). CA has been cloned from the alimentary canal epithelium of Anopheles gambiae larvae and can generate bicarbonate, which is implicated as a buffer for the larval lumen. The question remains as to how the bicarbonate is transported from the cells into the lumen. We hypothesize the presence of a CA within the lumen itself to generate bicarbonate from CO2 produced by the metabolically active alimentary canal cells. Here, we report the cloning and characterization of a novel cytoplasmic-type α-CA from the larval An. gambiae alimentary canal. Antibody immunolocalization reveals a unique protein distribution pattern that includes the ectoperitrophic fluid,`transitional region' of the alimentary canal, Malpighian tubules and a subset of cells in the dorsal anterior region of the rectum. Localization of this CA within the lumen of the alimentary canal may be a key to larval pH regulation,while detection within the rectum reveals a novel subset of cells in An. gambiae not described to date. Phylogenetic analysis of members of theα-CA family from the Homo sapiens, Drosophila melanogaster, Aedes aegypti and An. gambiae genomes shows a clustering of the novel CA with Homo sapiens CAs but not with other insect CAs. Finally, a universal system for naming newly cloned An. gambiae CAs is suggested.

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Section: Dar Cellsmentioning

confidence: 99%

Cloning and characterization of AgCA9, a novel α-carbonic anhydrase from Anopheles gambiae Giles sensu stricto (Diptera:Culicidae) larvae

Smith

VanEkeris

Linser

2007

Journal of Experimental Biology

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“…A shorter transcript signal was seen in the placenta 23 . A number of CA10 ESTs from human placenta have been reported 13 . The expression of CA10 mRNA was also studied in the human pancreas, kidney, liver, salivary glands, brain, mammary glands, placenta, and testis by using RT-PCR.…”

Section: Expression Of Carp X Protein and Its Mrna In Tissuesmentioning

confidence: 99%

An update on carbonic anhydrase-related proteins VIII, X and XI

Aspatwar

Tolvanen

Parkkila

2013

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…Therefore, most of the analysis exhibited expression of CA isoforms almost ubiquitously in living organisms. CAs consists of five different genetic families (α, ß, γ, δ and ξ) (Tashian, 2000;Hewett-Emmett, 1996).…”

Section: Introductionmentioning

confidence: 99%

Effect of Some Drugs on Sheep Liver Carbonic Anhydrase I and Ii

Çankaya¹,

Kuzucu²

2015

FBEDERGI

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Effects of clindamycin, dexketoprofen trometamol, benzylpenicillin (penicillin G) and phenoxymethylpenicillin (penicillin V) were examined on purified sheep carbonic anhydrase I and II (SCAI, SCA-II). In our study, we were chosen sheep liver tissue; because the liver is responsible for detoxification of xenobiotics. The CA isozyme have a very important duties on organisms, the effect of xenobiotics on the CA enzyme was reported. It was observed these drugs exhibited the inhibition effects against liver carbonic anhydrase isozymes I and II in our study. SCA I and SCA II isozymes were purified with about a specific activity of 1108.51 EU/mg and 5706.67 EU/mg, 120.62 and 620.96 purification fold by using Sepharose-4B-L tyrosine-sulfanilamide affinity gel chromatography. Purity of the SCA I and SCA II isozyme was checked by SDS-PAGE technique and subunit molecular masses of the SCA I was found as 29 kDa and SCA II found as 31 kDa. The usage of clindamycin, dexketoprofen trometamol, benzylpenicillin (penicillin G) and phenoxymethylpenicillin (penicillin V) in sheep liver especially during necrotic hepatitis disease is important for scientific researches. Many antibiotic and antihistamine may have dangerous effect to sheep liver. Also, it is important to study the inhibition effects of these drugs on SCA I and II isozymes.

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Carbonic anhydrase (CA)-related proteins (CA-RPs), and transmembrane proteins with CA or CA-RP domains

Cited by 58 publications

References 49 publications

Cloning and characterization of AgCA9, a novel α-carbonic anhydrase from Anopheles gambiae Giles sensu stricto (Diptera:Culicidae) larvae

Cloning and characterization of AgCA9, a novel α-carbonic anhydrase from Anopheles gambiae Giles sensu stricto (Diptera:Culicidae) larvae

An update on carbonic anhydrase-related proteins VIII, X and XI

Effect of Some Drugs on Sheep Liver Carbonic Anhydrase I and Ii

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