Development of an isotope dilution mass spectrometry assay for HbA1c based on enzyme-cleaved peptide analysis

Iguchi, Ken; Nakanishi, Toyofumi; Miyazaki, Akira; Shimizu, Akira; Ota, Akira

doi:10.1016/j.jchromb.2004.01.038

Cited by 16 publications

(19 citation statements)

References 27 publications

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“…Calibrators were prepared by mixing highly purified and fully characterized HbA 0 and HbA 1c preparations in accurately measured amounts and sample analyses were performed by the standard addition procedure (Jeppson et al, 2002). An alternative procedure involved quantification of each target hexapeptide (glycated and non-glycated) by isotope dilution, employing as internal standards the analogues containing D 7 -labeled leucine at the N-terminal (Iguchi et al, 2004).…”

Section: Measurement Of Modified Oligopeptidesmentioning

confidence: 99%

Toward an “omic” physiopathology of reactive chemicals: Thirty years of mass spectrometric study of the protein adducts with endogenous and xenobiotic compounds

Rubino

Pitton

Fabio

et al. 2009

Mass Spectrometry Reviews

109

170

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Cancer and degenerative diseases are major causes of morbidity and death, derived from the permanent modification of key biopolymers such as DNA and regulatory proteins by usually smaller, reactive molecules, present in the environment or generated from endogenous and xenobiotic components by the body's own biochemical mechanisms (molecular adducts). In particular, protein adducts with organic electrophiles have been studied for more than 30 [see, e.g., Calleman et al., 1978] years essentially for three purposes: (a) as passive monitors of the mean level of individual exposure to specific chemicals, either endogenously present in the human body or to which the subject is exposed through food or environmental contamination; (b) as quantitative indicators of the mean extent of the individual metabolic processing which converts a non-reactive chemical substance into its toxic products able to damage DNA (en route to cancer induction through genotoxic mechanisms) or key proteins (as in the case of several drugs, pesticides or otherwise biologically active substances); (c) to relate the extent of protein modification to that of biological function impairment (such as enzyme inhibition) finally causing the specific health damage. This review describes the role that contemporary mass spectrometry-based approaches employed in the qualitative and quantitative study of protein-electrophile adducts play in the discovery of the (bio)chemical mechanisms of toxic substances and highlights the future directions of research in this field. A particular emphasis is given to the measurement of often high levels of the protein adducts of several industrial and environmental pollutants in unexposed human populations, a phenomenon which highlights the possibility that a number of small organic molecules are generated in the human organism through minor metabolic processes, the imbalance of which may be the cause of "spontaneous" cases of cancer and of other degenerative diseases of still uncharacterized etiology. With all this in mind, it is foreseen that a holistic description of cellular functions will take advantage of new analytical methods based on time-integrated metabolomic measurements of a new biological compartment, the "adductome," aimed at better understanding integrated organism response to environmental and endogenous stressors.

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Section: Measurement Of Modified Oligopeptidesmentioning

confidence: 99%

Toward an “omic” physiopathology of reactive chemicals: Thirty years of mass spectrometric study of the protein adducts with endogenous and xenobiotic compounds

Rubino

Pitton

Fabio

et al. 2009

Mass Spectrometry Reviews

109

170

View full text Add to dashboard Cite

show abstract

“…However, the ICP-MS allows a very sensitive and isotope-specific analysis of Fe-proteins, without the use of radioactive tracers. It is known that accuracy and precision for the determination of the four isotopes of iron ( 54 Fe 5.8%, 56 Fe 91.7%, 57 Fe 2.14%, 58 Fe 0.31%) by ICP-MS with a conventional quadrupole analyzer is limited by polyatomic interferences (coming from the argon, the atmospheric gases and the biological material [52]). However, the use of double focusing sector field, ICP-(SF)-MS, multicollector, MC-ICP-MS, or collision/reaction cell, ICP-(ORS)-MS, instruments facilitates the elimination of such interferences and provides robust, high sensitivity and specific iron detection.…”

Section: The Role Of Mass Spectrometric Techniques In the Analysis Ofmentioning

confidence: 99%

“…However, the intensity ratio of the glycated and non-glycated hexapeptides (relative to each other) is used to calculate the relative concentration of HbA 1c and both methods calibration is carried out using mixtures of highly purified HbA 1c and HbA. In order to improve the reproducibility and reliability of such HbA 1c measurement, the LC-ESI-MS reference method [56] was slightly modified using deuterium-labelled synthetic peptides as internal standards in a posterior publication [58].…”

Section: Glycated Haemoglobinmentioning

confidence: 99%

The potential of mass spectrometry to study iron-containing proteins used in clinical diagnosis

Busto

Montes-Bayón

Sanz‐Medel

2009

Analytica Chimica Acta

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“…In recent years, it has been successfully expanded for absolute protein quantitation, and several proteins have been quantified by the IDMS method [9][10][11][12][13][14][15][16][17][18]. It has also proved successful for HbA 1c quantitation by both high-performance LC (HPLC)-IDMS [19,20] and HPLC-ICP-IDMS [21,22]. It has also been shown that the calibration systems for HbA 1c quantitation by LC-IDMS agreed well with IFCC reference measurement procedure [20].…”

Section: Introductionmentioning

confidence: 99%

“…Because IDMS is a method of the highest metrological order, the LC-IDMS procedure for HbA 1c analysis allows the current IFCC reference measurement procedure to be raised to a higher order of accuracy [20]. Compared with previously published work [19,20], in the work reported here, leucine and valine CRMs with independent assigned certified values were used to set up the traceability to SI units and to ensure the accuracy of the certified value of HbA 1c CRM. The possible VHLTPE residue in the 1-deoxyfructosyl-VHLTPE (G-VHLTPE) standard was also determined with LC-IDMS for correction to ensure the accurate certified value of the CRM.…”

Section: Introductionmentioning

confidence: 99%

Development of hemoglobin A1c certified reference material by liquid chromatography isotope dilution mass spectrometry

Yang

et al. 2012

Anal Bioanal Chem

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We report the development of a National Institute of Metrology (NIM) hemoglobin A(1c) (HbA(1c)) certified reference material (CRM). Each CRM unit contains about 10 μL of hemoglobin. Both hemoglobin and glycated hemoglobin were quantitatively determined by high-performance liquid chromatography (HPLC)-isotope dilution mass spectrometry (IDMS) with synthesized VHLTPE and glycated VHLTPE as standards. The mass fraction of synthesized VHLTPE or glycated VHLTPE was also quantitatively determined by HPLC-IDMS with NIM amino acid CRMs as standards. The homogeneity and stability of the CRMs were examined with a commercial HbA(1c) analyzer based on the HPLC principle. Fifteen units were randomly selected for homogeneity examination, and statistical analysis showed there was no inhomogeneity. Examination of the stability showed that the CRM was stable for at least 6 months at -80 °C. Uncertainty components of the balance, amino acid purity, hydrolysis and proteolysis efficiency, method reproducibility, homogeneity, and stability were taken into consideration for uncertainty evaluation. The certified value of NIM HbA(1c) CRM was expressed as the ratio of HbA(1c) to total hemoglobin in moles, and was (9.6 ± 1.9)%. The CRM can be used as a calibration or validation standard for clinical diagnostics. It is expected to improve the comparability for HbA(1c) measurement in China.

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Development of an isotope dilution mass spectrometry assay for HbA1c based on enzyme-cleaved peptide analysis

Cited by 16 publications

References 27 publications

Toward an “omic” physiopathology of reactive chemicals: Thirty years of mass spectrometric study of the protein adducts with endogenous and xenobiotic compounds

Toward an “omic” physiopathology of reactive chemicals: Thirty years of mass spectrometric study of the protein adducts with endogenous and xenobiotic compounds

The potential of mass spectrometry to study iron-containing proteins used in clinical diagnosis

Development of hemoglobin A1c certified reference material by liquid chromatography isotope dilution mass spectrometry

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