Stimulation of a human erythrocyte membrane ATPase by glutathione conjugates

Rajendra Sharma, Sanjiv Gupta, Hassan Ahmad, Ghulam Ansari, Yogesh C. Awasthi

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

An ATP-dependent transport process for S-(2,4-dinitrophenyl) glutathione (Dnp-SG) mediated by a novel ATPase designated as Dnp-SG ATPase has been demonstrated in human erythrocytes (LaBelle et al., FEBS Lett. 228, 51-53, 1988). In order to investigate whether the Dnp-SG ATPase system represents a generalized mechanism for the transport of xenobiotic conjugates of glutathione (GSH), stimulation of this ATPase by different GSH conjugates was studied in membrane vesicles prepared from human erythrocytes. Kinetic parameters for several GSH conjugates including S-(methyl)glutathione, S-(n-propyl)glutathione, S-(n-pentyl)glutathione, S-(n-decyl)glutathione, S-(p-chlorophenacyl)glutathione, S-(p-nitrobenzyl)glutathione, and the GSH conjugate of 9,10-epoxystearic acid were determined in order to evaluate their affinity for Dnp-SG ATPase. These studies reveal that all these conjugates stimulated Dnp-SG ATPase of human erythrocyte membrane. The apparent Km values of Dnp-SG ATPase for different conjugates were found to be in the range of 0.26-0.66 mm with Vmax values ranging from 0.55 to 4.44 nmol/min/mg protein. The results of these studies indicate that erythrocyte membrane Dnp-SG ATPase represents a generalized mechanism for the transport of GSH conjugates formed with xenobiotics as well as with the endogenously generated electrophilic compounds such as epoxystearic acid. It is suggested that Dnp-SG ATPase in conjunction with GSH and GSH S-transferase may play an important role in the protection of erythrocytes from exogenous as well as endogenous electrophilic toxicants.

Original languageEnglish (US)
Pages (from-to)421-428
Number of pages8
JournalToxicology and Applied Pharmacology
Volume104
Issue number3
DOIs
StatePublished - 1990

Fingerprint

Erythrocyte Membrane
Glutathione
Adenosine Triphosphatases
Membranes
Erythrocytes
Xenobiotics
Transferases
S-(dinitrophenyl)glutathione ATPase
Kinetic parameters
Adenosine Triphosphate
Acids
Proteins

ASJC Scopus subject areas

  • Pharmacology
  • Toxicology

Cite this

Stimulation of a human erythrocyte membrane ATPase by glutathione conjugates. / Sharma, Rajendra; Gupta, Sanjiv; Ahmad, Hassan; Ansari, Ghulam; Awasthi, Yogesh C.

In: Toxicology and Applied Pharmacology, Vol. 104, No. 3, 1990, p. 421-428.

Research output: Contribution to journalArticle

Sharma, Rajendra ; Gupta, Sanjiv ; Ahmad, Hassan ; Ansari, Ghulam ; Awasthi, Yogesh C. / Stimulation of a human erythrocyte membrane ATPase by glutathione conjugates. In: Toxicology and Applied Pharmacology. 1990 ; Vol. 104, No. 3. pp. 421-428.
@article{8dcc5ac2ee3a4ea4bea21fd54c7d8246,
title = "Stimulation of a human erythrocyte membrane ATPase by glutathione conjugates",
abstract = "An ATP-dependent transport process for S-(2,4-dinitrophenyl) glutathione (Dnp-SG) mediated by a novel ATPase designated as Dnp-SG ATPase has been demonstrated in human erythrocytes (LaBelle et al., FEBS Lett. 228, 51-53, 1988). In order to investigate whether the Dnp-SG ATPase system represents a generalized mechanism for the transport of xenobiotic conjugates of glutathione (GSH), stimulation of this ATPase by different GSH conjugates was studied in membrane vesicles prepared from human erythrocytes. Kinetic parameters for several GSH conjugates including S-(methyl)glutathione, S-(n-propyl)glutathione, S-(n-pentyl)glutathione, S-(n-decyl)glutathione, S-(p-chlorophenacyl)glutathione, S-(p-nitrobenzyl)glutathione, and the GSH conjugate of 9,10-epoxystearic acid were determined in order to evaluate their affinity for Dnp-SG ATPase. These studies reveal that all these conjugates stimulated Dnp-SG ATPase of human erythrocyte membrane. The apparent Km values of Dnp-SG ATPase for different conjugates were found to be in the range of 0.26-0.66 mm with Vmax values ranging from 0.55 to 4.44 nmol/min/mg protein. The results of these studies indicate that erythrocyte membrane Dnp-SG ATPase represents a generalized mechanism for the transport of GSH conjugates formed with xenobiotics as well as with the endogenously generated electrophilic compounds such as epoxystearic acid. It is suggested that Dnp-SG ATPase in conjunction with GSH and GSH S-transferase may play an important role in the protection of erythrocytes from exogenous as well as endogenous electrophilic toxicants.",
author = "Rajendra Sharma and Sanjiv Gupta and Hassan Ahmad and Ghulam Ansari and Awasthi, {Yogesh C.}",
year = "1990",
doi = "10.1016/0041-008X(90)90164-P",
language = "English (US)",
volume = "104",
pages = "421--428",
journal = "Toxicology and Applied Pharmacology",
issn = "0041-008X",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Stimulation of a human erythrocyte membrane ATPase by glutathione conjugates

AU - Sharma, Rajendra

AU - Gupta, Sanjiv

AU - Ahmad, Hassan

AU - Ansari, Ghulam

AU - Awasthi, Yogesh C.

PY - 1990

Y1 - 1990

N2 - An ATP-dependent transport process for S-(2,4-dinitrophenyl) glutathione (Dnp-SG) mediated by a novel ATPase designated as Dnp-SG ATPase has been demonstrated in human erythrocytes (LaBelle et al., FEBS Lett. 228, 51-53, 1988). In order to investigate whether the Dnp-SG ATPase system represents a generalized mechanism for the transport of xenobiotic conjugates of glutathione (GSH), stimulation of this ATPase by different GSH conjugates was studied in membrane vesicles prepared from human erythrocytes. Kinetic parameters for several GSH conjugates including S-(methyl)glutathione, S-(n-propyl)glutathione, S-(n-pentyl)glutathione, S-(n-decyl)glutathione, S-(p-chlorophenacyl)glutathione, S-(p-nitrobenzyl)glutathione, and the GSH conjugate of 9,10-epoxystearic acid were determined in order to evaluate their affinity for Dnp-SG ATPase. These studies reveal that all these conjugates stimulated Dnp-SG ATPase of human erythrocyte membrane. The apparent Km values of Dnp-SG ATPase for different conjugates were found to be in the range of 0.26-0.66 mm with Vmax values ranging from 0.55 to 4.44 nmol/min/mg protein. The results of these studies indicate that erythrocyte membrane Dnp-SG ATPase represents a generalized mechanism for the transport of GSH conjugates formed with xenobiotics as well as with the endogenously generated electrophilic compounds such as epoxystearic acid. It is suggested that Dnp-SG ATPase in conjunction with GSH and GSH S-transferase may play an important role in the protection of erythrocytes from exogenous as well as endogenous electrophilic toxicants.

AB - An ATP-dependent transport process for S-(2,4-dinitrophenyl) glutathione (Dnp-SG) mediated by a novel ATPase designated as Dnp-SG ATPase has been demonstrated in human erythrocytes (LaBelle et al., FEBS Lett. 228, 51-53, 1988). In order to investigate whether the Dnp-SG ATPase system represents a generalized mechanism for the transport of xenobiotic conjugates of glutathione (GSH), stimulation of this ATPase by different GSH conjugates was studied in membrane vesicles prepared from human erythrocytes. Kinetic parameters for several GSH conjugates including S-(methyl)glutathione, S-(n-propyl)glutathione, S-(n-pentyl)glutathione, S-(n-decyl)glutathione, S-(p-chlorophenacyl)glutathione, S-(p-nitrobenzyl)glutathione, and the GSH conjugate of 9,10-epoxystearic acid were determined in order to evaluate their affinity for Dnp-SG ATPase. These studies reveal that all these conjugates stimulated Dnp-SG ATPase of human erythrocyte membrane. The apparent Km values of Dnp-SG ATPase for different conjugates were found to be in the range of 0.26-0.66 mm with Vmax values ranging from 0.55 to 4.44 nmol/min/mg protein. The results of these studies indicate that erythrocyte membrane Dnp-SG ATPase represents a generalized mechanism for the transport of GSH conjugates formed with xenobiotics as well as with the endogenously generated electrophilic compounds such as epoxystearic acid. It is suggested that Dnp-SG ATPase in conjunction with GSH and GSH S-transferase may play an important role in the protection of erythrocytes from exogenous as well as endogenous electrophilic toxicants.

UR - http://www.scopus.com/inward/record.url?scp=0025172649&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025172649&partnerID=8YFLogxK

U2 - 10.1016/0041-008X(90)90164-P

DO - 10.1016/0041-008X(90)90164-P

M3 - Article

C2 - 2143605

AN - SCOPUS:0025172649

VL - 104

SP - 421

EP - 428

JO - Toxicology and Applied Pharmacology

JF - Toxicology and Applied Pharmacology

SN - 0041-008X

IS - 3

ER -