The Chemistry of Glutathione: the Work of Alton Meister
Year: 2007
Type: article
Abstract: Structural and Functional Significance of Cysteine Residues of Glutathione-independent Prostaglandin D Synthase: IDENTIFICATION OF CYS65 AS AN ESSENTIAL THIOL Journal of Biological ChemistryVol. 270Issue 3PreviewGlutathione-independent prostaglandin D synthase in rat brain is composed of 189 amino acid residues and catalyzes the isomerization of prostaglandin H2 to prostaglandin D2, an endogenous sleep-promoting substance. This enzyme is the only enzyme among members of the lipocalin superfamily composed of various secretory lipophilic ligand-carrier proteins and is recently identified to be a β-trace protein, a major constituent of human cerebrospinal fluid. We expressed the active enzyme in Escherichia coli and then systematically substituted all cysteine residues of the Δ1-29 enzyme at positions of 65, 89, and 186 with alanine or serine. Full-Text PDF Open Access Regulation of Gamma-glutamyl-cysteine Synthetase by Nonallosteric Feedback Inhibition by Glutathione (Richman, P. G., and Meister, A. (1975) J. Biol. Chem. 250, 1422–1426) Alton Meister (1922–1995) was born in New York City. He earned his B.S. from Harvard University in 1942 and his M.D. from Cornell University Medical College in New York in 1945. He then went to the National Cancer Institute at the National Institutes of Health and remained there until 1955 when he became chairman of the biochemistry department at the Tufts University School of Medicine. In 1967 Meister returned to the Cornell University Medical College and served as chairman of the college's biochemistry department until 1995. He was also biochemist-in-chief at New York Hospital from 1971 to 1995. Meister spent much of his career studying the chemistry of glutathione, a ubiquitous compound that protects cells from oxidation by absorbing oxygen. He had a suspicion that the compound might play an important role in the body's immune system. This suspicion was confirmed when Meister observed that people infected with the AIDS virus had exceptionally low levels of glutathione. Later, he found that glutathione can dramatically block the spread of the AIDS virus in vitro and that the more glutathione that was used, the greater the effect. As a result, Meister helped transform glutathione into a drug that has shown some initial promise in reducing the growth of the AIDS virus. The Journal of Biological Chemistry (JBC) Classic reprinted here reports Meister's discovery that glutathione regulates its own synthesis. Glutathione is synthesized from l-glutamate and l-cysteine via a γ-glutamyl-cysteine intermediate. By examining the effect of glutathione and several related compounds on the activity of kidney γ-glutamyl-cysteine synthetase, Meister was able to conclude that, “γ-glutamyl-cysteine synthetase is inhibited by glutathione under conditions similar to those which prevail in vivo, thus strongly suggesting a physiologically significant feedback mechanism.” 1More information about glutathione metabolism can be found in Meister's JBC Minireview (1Meister A. Glutathione metabolism and its selective modification.J. Biol. Chem. 1988; 263: 17205-17208Abstract Full Text PDF PubMed Google Scholar).1More information about glutathione metabolism can be found in Meister's JBC Minireview (1Meister A. Glutathione metabolism and its selective modification.J. Biol. Chem. 1988; 263: 17205-17208Abstract Full Text PDF PubMed Google Scholar). In addition to his work on glutathione, Meister authored the 2-volume Biochemistry of Amino Acids and was Editor of Advances in Enzymology and Associate Editor of the Journal of Biological Chemistry and the Annual Review of Biochemistry. He served on several Editorial Boards including those of the Journal of Biological Chemistry, Biochemistry, Methods in Biochemical Analysis, Biochimica et Biophysica Acta, and the Annual Review of Biochemistry. He was President of the American Society of Biological Chemists in 1977. Meister was a member of the National Academy of Sciences, the American Academy of Arts and Sciences, and the New York Academy of Sciences. He received many honors including the American Chemical Society's Paul-Lewis Award in enzyme chemistry (1954), the American Society of Biological Chemists' William C. Rose Award in biochemistry (1984), and the Chemical Industry Institute of Toxicology Founders' Award (1985).
Source: Journal of Biological Chemistry
Language: English
Topic: Sulfur Compounds in Biology
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1510347845