Protein glutathiolation in human blood

Wayne A. Kleinman; Despina Komninou; Yvonne Leutzinger; Stephen Colosimo; Julie Cox; Calvin A. Lang; John P. Richie

doi:10.1016/S0006-2952(02)01560-5

Protein glutathiolation in human blood

Wayne A. Kleinman, Despina Komninou, Yvonne Leutzinger, Stephen Colosimo, Julie Cox, Calvin A. Lang, John P. Richie

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Abstract

Glutathione (GSH) exists in both free and protein-bound (glutathiolated) forms (GSSP). Protein glutathiolation may represent an important post-translational regulatory mechanism for proteins. However, there are little data regarding the regulation of glutathiolation in blood. Our objectives were to examine GSSP levels of human blood by determining the distribution and variability of blood GSSP, as well as its relationship to free GSH and hemoglobin in healthy adults. To this end, we used a newly modified method allowing for rapid analysis of both GSH and GSSP in blood. GSSP was found in red cells with levels ranging from 4 to 27% of total (free+bound) GSH (mean±SD: 12.1±4.5%) with a concentration of 0.13±0.05μEq GSH/mL (mean±SD). No correlations were observed between GSSP and either GSH (r=-0.085) or hemoglobin (r=0.086). Together these results suggest that the extent of protein glutathiolation in blood is substantial (∼0.1mmol/L). While the interindividual variation in GSSP is large (34%), its levels are apparently not regulated by GSH content.

Original language	English (US)
Pages (from-to)	741-746
Number of pages	6
Journal	Biochemical Pharmacology
Volume	65
Issue number	5
DOIs	https://doi.org/10.1016/S0006-2952(02)01560-5
State	Published - Mar 1 2003

All Science Journal Classification (ASJC) codes

Biochemistry
Pharmacology

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10.1016/S0006-2952(02)01560-5

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title = "Protein glutathiolation in human blood",

abstract = "Glutathione (GSH) exists in both free and protein-bound (glutathiolated) forms (GSSP). Protein glutathiolation may represent an important post-translational regulatory mechanism for proteins. However, there are little data regarding the regulation of glutathiolation in blood. Our objectives were to examine GSSP levels of human blood by determining the distribution and variability of blood GSSP, as well as its relationship to free GSH and hemoglobin in healthy adults. To this end, we used a newly modified method allowing for rapid analysis of both GSH and GSSP in blood. GSSP was found in red cells with levels ranging from 4 to 27% of total (free+bound) GSH (mean±SD: 12.1±4.5%) with a concentration of 0.13±0.05μEq GSH/mL (mean±SD). No correlations were observed between GSSP and either GSH (r=-0.085) or hemoglobin (r=0.086). Together these results suggest that the extent of protein glutathiolation in blood is substantial (∼0.1mmol/L). While the interindividual variation in GSSP is large (34%), its levels are apparently not regulated by GSH content.",

author = "Kleinman, {Wayne A.} and Despina Komninou and Yvonne Leutzinger and Stephen Colosimo and Julie Cox and Lang, {Calvin A.} and Richie, {John P.}",

note = "Funding Information: We thank Shelley Isaacs for her technical assistance, and Marie-Ange Brunnemann for her editorial assistance. This study was supported, in part, by NIH Grants CA17613 and CA68384. ",

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T1 - Protein glutathiolation in human blood

AU - Kleinman, Wayne A.

AU - Komninou, Despina

AU - Leutzinger, Yvonne

AU - Colosimo, Stephen

AU - Cox, Julie

AU - Lang, Calvin A.

AU - Richie, John P.

N1 - Funding Information: We thank Shelley Isaacs for her technical assistance, and Marie-Ange Brunnemann for her editorial assistance. This study was supported, in part, by NIH Grants CA17613 and CA68384.

PY - 2003/3/1

Y1 - 2003/3/1

N2 - Glutathione (GSH) exists in both free and protein-bound (glutathiolated) forms (GSSP). Protein glutathiolation may represent an important post-translational regulatory mechanism for proteins. However, there are little data regarding the regulation of glutathiolation in blood. Our objectives were to examine GSSP levels of human blood by determining the distribution and variability of blood GSSP, as well as its relationship to free GSH and hemoglobin in healthy adults. To this end, we used a newly modified method allowing for rapid analysis of both GSH and GSSP in blood. GSSP was found in red cells with levels ranging from 4 to 27% of total (free+bound) GSH (mean±SD: 12.1±4.5%) with a concentration of 0.13±0.05μEq GSH/mL (mean±SD). No correlations were observed between GSSP and either GSH (r=-0.085) or hemoglobin (r=0.086). Together these results suggest that the extent of protein glutathiolation in blood is substantial (∼0.1mmol/L). While the interindividual variation in GSSP is large (34%), its levels are apparently not regulated by GSH content.

AB - Glutathione (GSH) exists in both free and protein-bound (glutathiolated) forms (GSSP). Protein glutathiolation may represent an important post-translational regulatory mechanism for proteins. However, there are little data regarding the regulation of glutathiolation in blood. Our objectives were to examine GSSP levels of human blood by determining the distribution and variability of blood GSSP, as well as its relationship to free GSH and hemoglobin in healthy adults. To this end, we used a newly modified method allowing for rapid analysis of both GSH and GSSP in blood. GSSP was found in red cells with levels ranging from 4 to 27% of total (free+bound) GSH (mean±SD: 12.1±4.5%) with a concentration of 0.13±0.05μEq GSH/mL (mean±SD). No correlations were observed between GSSP and either GSH (r=-0.085) or hemoglobin (r=0.086). Together these results suggest that the extent of protein glutathiolation in blood is substantial (∼0.1mmol/L). While the interindividual variation in GSSP is large (34%), its levels are apparently not regulated by GSH content.

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Protein glutathiolation in human blood

Abstract

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