Refine your search
Collections
Journals
Year
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z All
Mathew, Boby
- Functional Prediction from Conformational Dynamics of Glycated and Glutathionylated HbE and HbD Punjab
Abstract Views :376 |
PDF Views:77
Authors
Sreekala Narayanan
1,
Boby Mathew
1,
Bindu Y. Srinivasu
1,
Monita Muralidharan
1,
Vijay Bhat
2,
Amit Kumar Mandal
1
Affiliations
1 Clinical Proteomics Unit, Division of Molecular Medicine, St John’s Research Institute, St John’s National Academy of Health Sciences, Bengaluru 560 034, IN
2 Manipal Hospital, Old Airport Road, Bengaluru 560 017, IN
1 Clinical Proteomics Unit, Division of Molecular Medicine, St John’s Research Institute, St John’s National Academy of Health Sciences, Bengaluru 560 034, IN
2 Manipal Hospital, Old Airport Road, Bengaluru 560 017, IN
Source
Current Science, Vol 118, No 5 (2020), Pagination: 722-727Abstract
Glycation and glutathionylation are important posttranslational modifications (PTMs) of human haemoglobin that act as biomarkers of diabetes mellitus and oxidative stress. These PTMs perturb the function of normal haemoglobin. However, the structure–function correlation of these PTMs of genetically modified haemoglobin remained unexplored. Using hydrogen/ deuterium exchange mass spectrometry, we studied the conformational dynamics of glycated and glutathionylated forms of two haemoglobin variants, HbE and HbD Punjab. Like glycated and glutathionylated normal haemoglobin, these PTMs of HbE were expected to have increased oxygen affinity. However, for HbD Punjab, glycation was predicted to have decreased oxygen affinity whereas glutathionylation to have increased oxygen affinity.Keywords
Glutathionylation, HbE, HbD Punjab, Glycation, Post-Translational Modifications, Structure–Function Correlation.Full Text
References
- Saraswathy, N. and Ramalingam, P., Phosphoproteomics. Concepts Tech. Genomics Proteomics, 2011, pp. 203–211.
- Larsen, M. R., Trelle, M. B., Thingholm, T. E. and Jensen, O. N., Analysis of post-translational modifications of proteins by tandem mass spectrometry. Biotechniques, 2006, 40, 790–798.
- Bode, A. M. and Dong, Z., Post-translational modification of p53 in tumorigenesis. Nat. Rev. Cancer, 2004, 4, 793–805.
- Gong, C.-X., Liu, F., Grundke-Iqbal, I. and Iqbal, K., Posttranslational modifications of tau protein in Alzheimer’s disease. J. Neural Transm., 2005, 112, 813–838.
- Koenig, R. J., Peterson, C. M., Jones, R. L., Saudek, C., Lehrman, M. and Cerami, A., Correlation of glucose regulation and haemoglobin AIc in diabetes mellitus. New. Engl. J. Med., 1976, 295, 417–420.
- Mandal, A. K. et al., Quantitation and characterization of glutathionyl haemoglobin as an oxidative stress marker in chronic renal failure by mass spectrometry. Clin. Biochem., 2007, 40, 986–994.
- Niwa, T., Naito, C., Mawjood, A. H. and Imai, K., Increased glutathionyl haemoglobin in diabetes mellitus and hyperlipidemia demonstrated by liquid chromatography/electrospray ionizationmass spectrometry. Clin. Chem., 2000, 46, 82–88.
- Yoshida, K., Hirokawa, J., Tagami, S., Kawakami, Y., Urata, Y. and Kondo, T., Weakened cellular scavenging activity against oxidative stress in diabetes mellitus: regulation of glutathione synthesis and efflux. Diabetologia, 1995, 38, 201–210.
- Piemonte, F. et al., Glutathione in blood of patients with Friedreich’s ataxia. Eur. J. Clin. Invest., 2001, 31, 1007–1011.
- Craescu, C. T., Poyart, C., Schaeffer, C., Garel, M. C., Kister, J. and Beuzard, Y., Covalent binding of glutathione to haemoglobin. II. Functional consequences and structural changes reflected in NMR spectra. J. Biol. Chem., 1986, 261, 14710–14716.
- De Rosa, M. C. et al., Glycated human haemoglobin (HbA1c): functional characteristics and molecular modeling studies. Biophys. Chem., 1998, 72, 323–335.
- Garel, M. C., Domenget, C., Caburi-Martin, J., Prehu, C., Galacteros, F. and Beuzard, Y., Covalent binding of glutathione to haemoglobin. I. Inhibition of haemoglobin S polymerization. J. Biol. Chem., 1986, 261, 14704–14709.
- Mitra, G., Muralidharan, M., Pinto, J., Srinivasan, K. and Mandal, A. K., Structural perturbation of human haemoglobin on glutathionylation probed by hydrogen–deuterium exchange and MALDI mass spectrometry. Bioconjugate Chem., 2011, 22, 785– 793.
- Narayanan, S., Mitra, G., Muralidharan, M., Mathew, B. and Mandal, A. K., Protein structure–function correlation in living human red blood cells probed by isotope exchange-based mass spectrometry. Anal. Chem., 2015, 87, 11812–11818.
- Oski, F. A., The role of organic phosphates in erythrocytes on the oxygen dissociation of haemoglobin. Ann. Clin. Lab. Sci., 1971, 1, 162–176.
- Devlin, T. M., Textbook of Biochemistry with Clinical Correlations, Wiley-Liss, New York, 2006, 6th edn, p. 351.
- Mitra, G., Muralidharan, M., Narayanan, S., Pinto, J., Srinivasan, K. and Mandal, A. K., Glutathionylation induced structural changes in oxy human hemoglobin analyzed by backbone amide hydrogen/deuterium exchange and MALDI-mass spectrometry. Bioconjugate Chem., 2012, 23, 2344–2353.
- Bunn, H., Gabbay, K. and Gallop, P., The glycosylation of haemoglobin: relevance to diabetes mellitus. Science, 1978, 200, 21–27.
- Mcdonald, M. J., Bleichman, M., Bunn, H. F. and Noble, R. W., Functional properties of the glycosylated minor components of human adult hemoglobin. J. Biol. Chem., 1979, 254, 702–707.
- Marschner, J. P. and Rietbrock, N., Oxygen release kinetics in healthy subjects and diabetic patients. I: the role of 2,3-diphosphoglycerate. Int. J. Clin. Pharmacol. Ther., 1994, 32, 533–535.
- Signorelli, S. S. et al., Oxidative stress and endothelial damage in patients with asymptomatic carotid atherosclerosis. Clin. Exp. Med., 2001, 1, 9–12.
- Mitra, A., Muralidharan, M., Srivastava, D., Das, R., Bhat, V. and Mandal, A. K., Assessment of cysteine reactivity of human hemoglobin at its residue level: a mass spectrometry-based approach. Hemoglobin, 2017, 41, 300–305.