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Carbonic anhydrase III, muscle specific

carbonic anhydrase III, CA III, CA-3
Carbonic anhydrase III (CAIII) is a member of a multigene family (at least six separate genes are known) that encodes carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyze the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue specific and present at high levels in skeletal muscle and much lower levels in cardiac and smooth muscle. A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. The gene spans 10.3 kb and contains seven exons and six introns. [provided by RefSeq, Oct 2008] (from NCBI)
Top mentioned proteins: ACID, HAD, CAN, fibrillin-1, AGE
Papers on carbonic anhydrase III
Population Structure of Candida albicans from Three Teaching Hospitals in Ghana.
Garrill et al., Christchurch, New Zealand. In Med Mycol, Mar 2016
In this study three microsatellite loci, CAI, CAIII and CAVI, were used to investigate the population genetic structure of C. albicans from clinical isolates in Ghana.
Circulating protein synthesis rates reveal skeletal muscle proteome dynamics.
Hellerstein et al., In J Clin Invest, Feb 2016
Fractional synthesis rate (FSR) of plasma creatine kinase M-type (CK-M) and carbonic anhydrase 3 (CA-3) in the blood, more than 90% of which is derived from skeletal muscle, correlated closely with FSR of CK-M, CA-3, and other proteins of various ontologies in skeletal muscle tissue in both rodents and humans.
Ambient PM2.5, O3, and NO2 Exposures and Associations with Mortality over 16 Years of Follow-Up in the Canadian Census Health and Environment Cohort (CanCHEC).
Burnett et al., Ottawa, Canada. In Environ Health Perspect, Nov 2015
CITATION: Crouse DL, Peters PA, Hystad P, Brook JR, van Donkelaar A, Martin RV, Villeneuve PJ, Jerrett M, Goldberg MS, Pope CA III, Brauer M, Brook RD, Robichaud A, Menard R, Burnett RT. 2015.
First-principles calculations of divalent substitution of Ca(2+) in tricalcium phosphates.
Nakamura et al., Nagoya, Japan. In Acta Biomater, Sep 2015
For instance, Mg(2+) and Zn(2+) favor the substitution at the Ca-5 site of β-TCP while Sr(2+) and Ba(2+) tend to occupy Ca-3 and Ca-4 in the β-type crystal structure.
The effect of training level on opioid utilization efficiency.
Green et al., Philadelphia, United States. In J Clin Anesth, May 2015
Comparing CA-1 and CA-3 residents and CA-2 and CA-3 residents, a statistically significant difference exists between the number of vials requested and the number returned.
Liver damage and caspase-dependent apoptosis is related to protein malnutrition in mice: effect of methionine.
Giudici et al., Mar del Plata, Argentina. In Acta Histochem, 2015
The expressions of carbonic anhydrase III (CAIII), fatty acid synthase (FAS), glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and glutathione S-transferase P1 (GSTP1) were assessed by proteomics and reverse transcriptase-polymerase chain reactions.
Improved serological detection of rheumatoid arthritis: a highly antigenic mimotope of carbonic anhydrase III selected in a murine model by phage display.
Ueira-Vieira et al., Uberlândia, Brazil. In Arthritis Res Ther, 2014
The M12 peptide was identified as one that mimics a predicted antigenic site of the carbonic anhydrase III (CAIII) protein, a ubiquitous biomarker that has been identified in patients with other diseases.
Characterization of Insertion Sequence ISSau2 in the Human and Livestock-Associated Staphylococcus aureus.
Zhao et al., China. In Plos One, 2014
ISSau2 is 1660bp in length with terminal 5'-TG and CA-3' dinucleotides and has two overlapping reading frames orfA and orfB.
Simulation-based education with deliberate practice may improve intraoperative handoff skills: a pilot study.
Burden et al., Camden, United States. In J Clin Anesth, 2014
Ten residents (CA-1, CA-2, and CA-3) participated in a one-day simulation-based handoff course.
Carbonic anhydrase III: a neglected isozyme is stepping into the limelight.
Parkkila et al., Tampere, Finland. In J Enzyme Inhib Med Chem, 2013
CONTEXT: Carbonic anhydrase III (CA III) is a cytosolic enzyme which is known to be highly expressed in the skeletal muscle and has been recently linked to important roles in several physiological processes.
Analysis of Modification of Liver Proteome in Diabetic Rats by 2D Electrophoresis and MALDI-TOF-MS.
Ravikumar et al., Thanjāvūr, India. In Indian J Clin Biochem, 2012
Comparison of 2-DE protein distribution profiles among the livers from normal, alloxan-induced diabetic rats and alloxan-induced diabetic rats treated with C. dactylon leaves identified three proteins that were up-regulated in alloxan-induced diabetic rats i.e., nucleophosmin, l-xylulose reductase and carbonic anhydrase III which are known to be mainly involved in ribosome biogenesis, centrosome duplication, cell proliferation, tumor suppression, glucose metabolism, osmo-regulation, water-CO2 balance and acid-base balance.
Carbonic anhydrase III regulates peroxisome proliferator-activated receptor-γ2.
Zwerschke et al., Austria. In Exp Cell Res, 2012
We conclude that down-regulation of CAIII in preadipocytes enhances adipogenesis and that CAIII is a regulator of adipogenic differentiation which acts at the level of PPAR-gamma2 gene expression.
Biomarkers and laryngopharyngeal reflux.
Carney et al., Australia. In J Laryngol Otol, 2011
Carbonic anhydrase III levels vary in the larynx in response to laryngopharyngeal reflux, depending on location.
Sexual dimorphism in LEC rat liver: suppression of carbonic anhydrase III by copper accumulation during hepatocarcinogenesis.
Sugiyama et al., Suita, Japan. In Biomed Res, 2011
Suppression of carbonic anhydrase III (CAIII) accompanied hepatocarcinogenesis and it is a secondary consequence of the high copper levels in the liver.
Carbonic anhydrases in the mouse harderian gland.
Parkkila et al., Tampere, Finland. In J Mol Histol, 2010
Car2, Car3, Car7, and Car15 mRNAs were barely within the detection limits in the mouse harderian gland.
Ty1 integrase overexpression leads to integration of non-Ty1 DNA fragments into the genome of Saccharomyces cerevisiae.
Eckardt-Schupp et al., München, Germany. In Mol Genet Genomics, 2010
These fragments do not exhibit similarity to Ty1 cDNA except for the presence of the conserved terminal dinucleotide 5'-TG-CA-3'.
Biochemical markers of muscular damage.
Maffulli et al., Napoli, Italy. In Clin Chem Lab Med, 2010
Creatine kinase, lactate dehydrogenase, aldolase, myoglobin, troponin, aspartate aminotransferase, and carbonic anhydrase CAIII are the most useful serum markers of muscle injury, but apoptosis in muscle tissues subsequent to strenuous exercise may be also triggered by increased oxidative stress.
Protein carbonylation in skeletal muscles: impact on function.
Hussain et al., Spain. In Antioxid Redox Signal, 2010
This proposal is supported by recent studies that unveiled that several myofilament (myosin heavy chain and actin), mitochondrial (aconitase, creatine kinase), and cytosolic (enolase, aldolase and glyceraldehyde 3-phosphate dehydrogenase and carbonic anhydrase III) proteins are carbonylated inside skeletal muscle fibers in many animal models of muscle dysfunction, and in humans with impaired skeletal muscle contractility.
Enhanced sensitivity to hydrogen peroxide-induced apoptosis in Evi1 transformed Rat1 fibroblasts due to repression of carbonic anhydrase III.
Bartholomew et al., Glasgow, United Kingdom. In Febs J, 2010
Evi1 represses transcription of caIII gene expression, leading to increased sensitivity to H(2)O(2)-induced apoptosis
Carbonic anhydrase III is insufficient in muscles of myasthenia gravis patients.
Sun et al., Hangzhou, China. In Autoimmunity, 2009
The level of CAIII is specifically insufficient in the skeletal muscle of myasthenia gravis patients.
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