Effect of Genetic Polymorphisms in CA6 Gene on the Expression and Catalytic Activity of Human Salivary Carbonic Anhydrase VI

2013 ◽  
Vol 47 (5) ◽  
pp. 414-420 ◽  
Author(s):  
M. Aidar ◽  
Rocha Marques ◽  
J. Valjakka ◽  
N. Mononen ◽  
T. Lehtimäki ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Carbonic Anhydrase ◽  
Genetic Polymorphisms ◽  
Carbonic Anhydrase Vi

scholarly journals Genetic polymorphisms in the carbonic anhydrase VI gene and dental caries susceptibility

2015 ◽  
Vol 14 (2) ◽  
pp. 5986-5993 ◽  
Author(s):  
Z.-Q. Li ◽  
X.-P. Hu ◽  
J.-Y. Zhou ◽  
X.-D. Xie ◽  
J.-M. Zhang
Keyword(s):  
Dental Caries ◽  
Carbonic Anhydrase ◽  
Genetic Polymorphisms ◽  
Dental Caries Susceptibility ◽  
Carbonic Anhydrase Vi

scholarly journals CHOP-Dependent Stress-Inducible Expression of a Novel Form of Carbonic Anhydrase VI

1999 ◽  
Vol 19 (1) ◽  
pp. 495-504 ◽  
Author(s):  
John Sok ◽  
Xiao-Zhong Wang ◽  
Nikoleta Batchvarova ◽  
Masahiko Kuroda ◽  
Heather Harding ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Target Gene ◽  
Target Genes ◽  
Direct Evidence ◽  
Nuclear Protein ◽  
Intracellular Form ◽  
Carbonic Anhydrase Vi ◽  
Responsive Element

ABSTRACT CHOP (also called GADD153) is a stress-inducible nuclear protein that dimerizes with members of the C/EBP family of transcription factors and was initially identified as an inhibitor of C/EBP binding to classic C/EBP target genes. Subsequent experiments suggested a role for CHOP-C/EBP heterodimers in positively regulating gene expression; however, direct evidence that this is the case has so far not been uncovered. Here we describe the identification of a positively regulated direct CHOP-C/EBP target gene, that encoding murine carbonic anhydrase VI (CA-VI). The stress-inducible form of the gene is expressed from an internal promoter and encodes a novel intracellular form of what is normally a secreted protein. Stress-induced expression of CA-VI is both CHOP and C/EBPβ dependent in that it does not occur in cells deficient in either gene. A CHOP-responsive element was mapped to the inducibleCA-VI promoter, and in vitro footprinting revealed binding of CHOP-C/EBP heterodimers to that site. Rescue of CA-VIexpression in c/ebpβ−/− cells by exogenous C/EBPβ and a shorter, normally inhibitory isoform of the protein known as LIP suggests that the role of the C/EBP partner is limited to targeting the CHOP-containing heterodimer to the response element and points to a preeminent role for CHOP in CA-VI induction during stress.

scholarly journals The identification of secreted carbonic anhydrase VI as a constitutive glycoprotein of human and rat milk

2001 ◽  
Vol 98 (20) ◽  
pp. 11604-11608 ◽  
Author(s):  
P. Karhumaa ◽  
J. Leinonen ◽  
S. Parkkila ◽  
K. Kaunisto ◽  
J. Tapanainen ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Vi

scholarly journals Azobenzene-based inhibitors of human carbonic anhydrase II

2015 ◽  
Vol 11 ◽  
pp. 1129-1135 ◽  
Author(s):  
Leander Simon Runtsch ◽  
David Michael Barber ◽  
Peter Mayer ◽  
Michael Groll ◽  
Dirk Trauner ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Activity ◽  
Carbonic Anhydrase ◽  
Drug Class ◽  
Carbonic Anhydrase Ii ◽  
Carbonic Anhydrases ◽  
X Ray ◽  
X Ray Crystallography ◽  
Human Carbonic Anhydrase

Aryl sulfonamides are a widely used drug class for the inhibition of carbonic anhydrases. In the context of our program of photochromic pharmacophores we were interested in the exploration of azobenzene-containing sulfonamides to block the catalytic activity of human carbonic anhydrase II (hCAII). Herein, we report the synthesis and in vitro evaluation of a small library of nine photochromic sulfonamides towards hCAII. All molecules are azobenzene-4-sulfonamides, which are substituted by different functional groups in the 4´-position and were characterized by X-ray crystallography. We aimed to investigate the influence of electron-donating or electron-withdrawing substituents on the inhibitory constant K i. With the aid of an hCAII crystal structure bound to one of the synthesized azobenzenes, we found that the electronic structure does not strongly affect inhibition. Taken together, all compounds are strong blockers of hCAII with K i = 25–65 nM that are potentially photochromic and thus combine studies from chemical synthesis, crystallography and enzyme kinetics.

scholarly journals Radioimmunoassay of carbonic anhydrase VI in saliva and sheep tissues

1991 ◽  
Vol 274 (2) ◽  
pp. 313-316 ◽  
Author(s):  
R T Fernley ◽  
R D Wright ◽  
J P Coghlan
Keyword(s):  
Carbonic Anhydrase ◽  
Parotid Gland ◽  
Saliva Sample ◽  
Secretion Rate ◽  
Parotid Saliva ◽  
Carbonic Anhydrase Vi ◽  
Conscious Sheep ◽  
Submandibular Saliva ◽  
Inter Assay Variation ◽  
Stimulation Of

A specific and sensitive radioimmunoassay has been developed for the measurement of the secreted carbonic anhydrase isoenzyme (CA VI) in sheep saliva and tissues. The assay can detect as little as 75 pg of CA VI, and the antibody used does not cross-react with CA II or CA III. The intra-assay variation, measured using a saliva sample, was 3.0%, whereas the inter-assay variation was 10.5%. The concentration of CA VI in parotid saliva from normal, resting sheep was 5.6 +/- 3.0 micrograms.ml-1 (n = 42) or 79.4 +/- 35.7 micrograms.mg of total protein-1. With feeding, the CA VI concentrations increased an average of 6-fold. The secretion rate of CA VI from the vascularly isolated neurotomized parotid gland of the anaesthetized sheep was 0.62 +/- 0.40 micrograms.min-1, compared with a rate of 11.7 +/- 7.8 micrograms.min-1 from the parotid gland of normal conscious sheep. Stimulation of the parotid-gland preparation by the muscarinic agent bethanechol increased the secretion rate to 438 +/- 172 microgram.min-1 (n = 8), and electrical stimulation of the secretomotor Moussu nerve increased CA VI secretion rate to 634 +/- 330 micrograms.min-1 (n = 4). Submandibular saliva from anaesthetized sheep contained 6.9 +/- 2.1 micrograms of CA VI.ml-1 (n = 3). The only tissues found to contain measurable amounts of CA VI were the parotid (6.4 micrograms.mg of protein-1) and submandibular (1.8 micrograms.mg of protein-1) salivary glands. The sublingual salivary gland, kidney, lung, adrenal, brain, skeletal muscle, liver, heart, pancreas, small intestine and cerebrospinal fluid did not have a measurable CA VI content.

Molecular cloning and characterization of secretory carbonic anhydrase VI in pufferfish ( Takifugu rubripes )

Gene ◽  
2018 ◽  
Vol 640 ◽  
pp. 57-65 ◽  
Author(s):  
Kanij Rukshana Sumi ◽  
Soo Cheol Kim ◽  
Sathishkumar Natarajan ◽  
Kap Seong Choi ◽  
Myeong Rak Choi ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Molecular Cloning ◽  
Takifugu Rubripes ◽  
Carbonic Anhydrase Vi

scholarly journals Structure of the carbonic anhydrase VI (CA6) gene: evidence for two distinct groups within the α-CA gene family

1999 ◽  
Vol 344 (2) ◽  
pp. 385-390 ◽  
Author(s):  
Weiping JIANG ◽  
Dwijendra GUPTA
Keyword(s):  
Carbonic Anhydrase ◽  
Untranslated Region ◽  
Sequence Similarity ◽  
Ca Ix ◽  
Its Gene ◽  
Exon 1 ◽  
Membrane Bound ◽  
Mature Enzyme ◽  
Gene Structures ◽  
Carbonic Anhydrase Vi

The secreted carbonic anhydrase (CA VI) is believed to be one of the oldest mammalian CAs in evolutionary terms. To elucidate its gene structure and compare it with other members of the α-CA family, we cloned genomic fragments encoding the bovine CA6 gene and determined its exon/intron organization. The gene spans approx. 25 kb and consists of eight exons and seven introns. Exon 1 encodes the 5′ untranslated region, the signal peptide and the N-terminus of the mature enzyme. Exon 8 encodes the 3′ untranslated region and the C-terminal extension that is unique to CA VI. Exons 2-7 encode the CA domain, which shows significant sequence similarity to other CAs. Two distinct groups exist in the α-CA family on the basis of a comparison of the known gene structures. One group consists of the cytoplasmic (CA I, II, III and VII) and mitochondrial (CA V) members. The other group consists of the membrane-bound (CA IV and IX) and secreted (CA VI) members. In particular, the seven exon/intron boundaries in the CA domain of the CA6 gene are conserved in the CA9 gene, which encodes the multidomain protein CA IX that is overexpressed in tumours and has transforming potential.

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