Literature DB >> 23105802

Analysis of protein posttranslational modifications by mass spectrometry: With special reference to haemoglobin.

Murali Woodi1, Amit Kumar Mondal, Balaram Padmanabhan, Krishnaswamy Patnam Rajagopalan.   

Abstract

Mass spectrometry provides a convenient platform for the study of different protein post translational modifications from clinical specimen. Analysis of different post translational modifications of hemoglobin like glycation and glutathionylation can provide useful information on the disease progression and the possible outcome of therapies. In the present study, we have addressed post translational modifications of hemoglobin like glutathionylation and glycation in relation to diabetes and chronic renal failure. We found that both alpha and beta chains of human hemoglobin are glycated irrespective of the extent of glycemia as evidenced by a mass increment of 162 Da. The phenomenon of glutathionylation was observed with only the beta globin chain of hemoglobin probably due to the presence of an accessible cysteine residue indicated by a mass increment of 305 Da. Also, the extent of gltuathionylation observed in the CRF patients could correlate with the severity of the oxidative stress owing to renal replacement therapies like dialysis and transplantation.

Entities:  

Keywords:  End-stage renal disease; Glutathionylation; Glycation; Oxidative stress; Renal replacement therapy

Year:  2009        PMID: 23105802      PMCID: PMC3453474          DOI: 10.1007/s12291-009-0004-3

Source DB:  PubMed          Journal:  Indian J Clin Biochem        ISSN: 0970-1915


  32 in total

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Authors:  P Stenvinkel; O Heimbürger; B Lindholm; G A Kaysen; J Bergström
Journal:  Nephrol Dial Transplant       Date:  2000-07       Impact factor: 5.992

Review 2.  Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress.

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Journal:  Eur J Biochem       Date:  2000-08

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Journal:  Transplant Proc       Date:  1996-10       Impact factor: 1.066

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Journal:  Clin Chem       Date:  2001-02       Impact factor: 8.327

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Journal:  Science       Date:  1989-10-06       Impact factor: 47.728

6.  Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons.

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Journal:  Anal Chem       Date:  1988-10-15       Impact factor: 6.986

7.  Characterization of a novel hemoglobin-glutathione adduct that is elevated in diabetic patients.

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Journal:  Mol Med       Date:  2001-09       Impact factor: 6.354

8.  Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization.

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Journal:  J Biol Chem       Date:  1986-11-05       Impact factor: 5.157

9.  Modification of human hemoglobin by glutathione. III. Perturbations of hemoglobin conformation analyzed by computer modeling.

Authors:  S J Wodak; J L De Coen; S J Edelstein; H Demarne; Y Beuzard
Journal:  J Biol Chem       Date:  1986-11-05       Impact factor: 5.157

10.  Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in NMR spectra.

Authors:  C T Craescu; C Poyart; C Schaeffer; M C Garel; J Kister; Y Beuzard
Journal:  J Biol Chem       Date:  1986-11-05       Impact factor: 5.157

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