Skip to main content
NCBI home page
Annals of the Rheumatic Diseases logoLink to Annals of the Rheumatic Diseases
. 1992 Aug;51(8):969–971. doi: 10.1136/ard.51.8.969

Action of sodium aurothiomalate on erythrocyte membrane.

J M Campbell 1, J Reglinski 1, W E Smith 1, D Porter 1, R D Sturrock 1
PMCID: PMC1004806  PMID: 1417122

Abstract

The number of sulphydryl groups on the erythrocyte membrane has been assessed as a function of nutritional status for two groups of patients, one receiving non-steroidal anti-inflammatory drugs (NSAIDs) and the other receiving sodium aurothiomalate (Myocrisin). The patients receiving NSAIDs had a significantly higher number of sulphydryl groups in both the glucose depleted and glucose activated states than the patients receiving sodium aurothiomalate. The study focuses on the hexose transport protein where there is a specific binding site for gold using the two sulphydryl residues on helices 11 and 12 of the protein. The data suggest that the strong binding of gold to the erythrocyte membrane occurs via thiol pairs rather than by isolated sulphydryl groups and that there are possibly two further binding sites for gold on the membrane, the identities of which are still unclear.

Full text

PDF
969

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arnett F. C., Edworthy S. M., Bloch D. A., McShane D. J., Fries J. F., Cooper N. S., Healey L. A., Kaplan S. R., Liang M. H., Luthra H. S. The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis. Arthritis Rheum. 1988 Mar;31(3):315–324. doi: 10.1002/art.1780310302. [DOI] [PubMed] [Google Scholar]
  2. Chilles C., Mulheron M., McCrae F. M., Reglinksi J., Smith W. E., Brzeski M., Sturrock R. D. Concentration and reactivity of the sulphydryl group population on the membrane of intact erythrocytes in patients with rheumatoid arthritis. Ann Rheum Dis. 1990 Sep;49(9):668–671. doi: 10.1136/ard.49.9.668. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Holman G. D., Parkar B. A., Midgley P. J. Exofacial photoaffinity labelling of the human erythrocyte sugar transporter. Biochim Biophys Acta. 1986 Feb 13;855(1):115–126. doi: 10.1016/0005-2736(86)90195-1. [DOI] [PubMed] [Google Scholar]
  4. Holman G. D., Rees W. D. Photolabelling of the hexose transporter at external and internal sites: fragmentation patterns and evidence for a conformational change. Biochim Biophys Acta. 1987 Mar 12;897(3):395–405. doi: 10.1016/0005-2736(87)90437-8. [DOI] [PubMed] [Google Scholar]
  5. Lin S., Spudich J. A. Biochemical studies on the mode of action of cytochalasin B. Cytochalasin B binding to red cell membrane in relation to glucose transport. J Biol Chem. 1974 Sep 25;249(18):5778–5783. [PubMed] [Google Scholar]
  6. McCrae F., Reglinski J., Smith W. E., Brzeski M., Sturrock R. D. The action of myocrisin on membrane bound sulphhydryl groups. Clin Chim Acta. 1990 Dec 31;195(1-2):41–45. doi: 10.1016/0009-8981(90)90192-u. [DOI] [PubMed] [Google Scholar]
  7. Rae K. J., Mackay C. N., McNeil C. J., Brown D. H., Smith W. E., Lewis D., Capell H. A. Early and late changes in sulphydryl group and copper protein concentrations and activities during drug treatment with aurothiomalate and auranofin. Ann Rheum Dis. 1986 Oct;45(10):839–846. doi: 10.1136/ard.45.10.839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Reglinski J., Hoey S., Smith W. E., Sturrock R. D. Cellular response to oxidative stress at sulfhydryl group receptor sites on the erythrocyte membrane. J Biol Chem. 1988 Sep 5;263(25):12360–12366. [PubMed] [Google Scholar]

Articles from Annals of the Rheumatic Diseases are provided here courtesy of BMJ Publishing Group

RESOURCES