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Cited by 272

The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.

Extracellular glutathione is a source of cysteine for cells that express .gamma.-glutamyl transpeptidase

Hanigan, Marie H., Ricketts, William A.·1993·Biochemistry
DOI 10.1021/bi00075a026
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Abstract

We show that gamma-glutamyl transpeptidase (GGT) is a glutathionase that enables cells to use extracellular glutathione as a source of cysteine. We transfected NIH/3T3 mouse fibroblasts with a plasmid containing cDNA for human GGT, and obtained stably transformed cell lines that expressed GGT in its proper orientation on the outer surface of the cell. NIH/3T3 fibroblasts require cysteine for growth and are unable to use extracellular glutathione as a source of cysteine. We demonstrate GGT-positive fibroblasts are able to grow in cysteine-free medium supplemented with glutathione. Cysteine derived from the cleavage of extracellular glutathione can be used to maintain intracellular levels of glutathione. GGT-positive NIH/3T3 cells were able to replenish intracellular glutathione when incubated in cysteine-free medium containing glutathione. GGT-negative cells could not. Therefore, GGT is a glutathionase that provides the cell with access to a secondary source of cysteine.

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Metadata

Authors
Hanigan, M. H., & Ricketts, W. A.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1993-06-22
Volume
32
Issue
24
Pages
6302-6306
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi00075a026
OpenAlex
W2076837930
Cited by
272
References
22
FWCI
4.20
Type
journal article
Language
en
Open access
closed

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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