carbonic anhydrase III
Circulating protein synthesis rates reveal skeletal muscle proteome dynamics.
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).
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.
Analysis of Modification of Liver Proteome in Diabetic Rats by 2D Electrophoresis and MALDI-TOF-MS.
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.
Biochemical markers of muscular damage.
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.
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.