In this exploratory study, we investigated total erythrocyte carbonic anhydrase (CA) estrase activity as well as CA I isozyme concentration in patients with diabetes mellitus type II (DM) and healthy individuals of Howard University Hospital community. Total estrase activity of CA was measured spectrophotometrically using p-nitrophenol acetate before and after inhibition with acetazolamide. CA I isozyme was measured by radial immunodiffusion using monoclonal antibody (CA I) in agarose plates. The study involved 20 consented participants; 10 normal (N) and 10 (DM), 21 to 84 years of age. The study was approved by the Howard University Institution Review Board. The CA activity was measured following lysis of cells as U/min/mL and CA I concentration as mg/l. We observed CA activity as 46.3±4(N) and 25±2.1 (DM) whereas CA I concentration as 1896±125 (N) and 1104 ±63 (DM). We speculate that the change in the CA activity may of fundamental importance in the regulation of intracellular; pHi for the basic control of metabolism in diabetes mellitus. Further, we propose that CA activity is a good candidate for a biomarker of diabetes mellitus for the early detection of insulin resistance because the CA activity variation was proportional to the severity of the diabetes.
Similar content being viewed by others
References
Abel P, Wussow S, Blucher H, Gros G, Rettig R, Andig A (1997) Erythrocyte carbonic anhydrase activity in smokers and in diabetic patients. Exp Clin Endocrinol Diabetes 105(Suppl 2):17–18
Akbar Ali S, Brown RP (1996) Human erythrocytes CA I and CA II isozymes in hypoxemic and anemic fetuses. Clinica Chem Acta 29:157–163
Armstrong JM, Myers DV, Verpoorte JA, Edsall JT (1966) Purification and properties of human erythrocyte carbonic anhydrase. J Biol Chem 241(21):5137–5149
Deutsch FH (1978) Carbonic anhydrases (review). Int J Biochem Int 19(2):101–113
Gambhir KK, Archer JA, Bradley C (1978) Characteristics of human erythrocyte insulin receptors. Diabetes 27:701
Gambhir KK, Ornasir J, Headings V (2003) Carbonic anhydrase and its isozyme 1 in diabetes mellitus. Clin Chem 49:A109–A110
Kondo T, Taniguchi N, Muaro M, Takauwa E (1975) Estimations of active and inactive carbonic anhydrase isozyme B in human red blood cells. Clin Chem Acta 60:347–353
Kondo T, Murakami K, Ohtsuka Y (1987) Estimation and characterization of glycosylated carbonic anhydrase I in erythrocytes from patients with diabetes mellitus. Clinica Chem Acta 166:227–236
Mori K, Ogawa Y, Ebihara K, Tamura N, Tashiro K (1999) Characterization of CAXIV: a novel membrane bound carbonic anhydrase from mouse kidney. J Biol Chem 274:15701–15705
Parui R, Gambhir K, Mehrotra P (1991). Changes in carbonic anhydrase may be the initial step of altered metabolism in hypertension. Biochem Int 23(4):779–789
Parui R, Gambhir KK, Cruz I, Hosten OA (1992) Erythrocyte carbonic anhydrase: a major intracellular enzyme to regulate cellular sodium metabolism in chronic renal failure patients with diabetes and hypertension. Biochem Int 26(5):809–820
Roughton FJW, Booth RH (1946) The biochemical properties of carbonic anhydrase. Biochemical J 40:319
Stevens VJ, Rouzer CA, Monnier VM, Cerami A (1978) Diabetic cataract formation: potential role of glycosylation and lens crystallins. Proc Nat Acad Sci USA 75:2918–2922
Taniguchi T, Okasaki K, Okamoto M, Seko S, Ushida K, Seino Y (2001) Presence of autoantibodies to carbonic anhydrase II and lactoferrin in type I diabetes. Diabetes Care 24:1695–1696
Taniguchi T, Okasaki K, Okamoto M, Seko S, Tanaka J, Ushida K, Nagashima K, Kurose T, Yamada Y, Chiba T, Seino Y (2003) High prevalence of antoatidiabetes: concept of autoimmune exocrinopathy and endocrynopathy of the pancreas. Pancreas 27:26–30
Acknowledgments
The authors sincerely appreciate the editing and typing of the manuscript by Ms. Adriana Malheiro. The authors thank Mr. Stafford L. Battle, Digital Designer in the office of curriculum operations, for his help in formatting the figures in a publishable form. The authors also wish to acknowledge the partial funding of laboratory supplies by grant 2G12RR003048 from the RCMI Program, Division of Research Infrastructure, and the National Center for Research Resources, NIH. A part of this study was published as an abstract in Clinical Chemistry (Gambhir et al. 2003).
Author information
Authors and Affiliations
Corresponding author
Additional information
Jehan Ornasir—these studies were undertaken as a partial requirement of her M.S. Degree, Graduate School, Howard University, Washington, DC, USA
Rights and permissions
About this article
Cite this article
Gambhir, K.K., Ornasir, J., Headings, V. et al. Decreased total carbonic anhydrase esterase activity and decreased levels of carbonic anhydrase 1 isozyme in erythrocytes of type II diabetic patients. Biochem Genet 45, 431–439 (2007). https://doi.org/10.1007/s10528-007-9086-x
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10528-007-9086-x