Skip to main content
NCBI home page
The British Journal of Cancer. Supplement logoLink to The British Journal of Cancer. Supplement
. 1987 Jun;8:60–65.

Protein fluorescence and its relationship to free radical activity.

A F Jones 1, J Lunec 1
PMCID: PMC2149460  PMID: 3307875

Abstract

Evidence for free radical involvement in pathological processes is often indirect and frequently depends upon the detection of characteristic changes in tissue constituents, particularly polyunsaturated lipids. Free radical attack on protein leads to specific oxidative changes in their constituent amino acids, principally cysteine, tryptophan and tyrosine. This is associated with the induction of characteristic fluorescence (excitation 360 nm, emission 454 nm) and protein aggregation. This observation leads to a suitable assay for studying protein oxidation, and such fluorescent proteins may be relevant in the pathogenesis of diabetic microangiopathy and rheumatoid arthritis.

Full text

PDF
60

Selected References

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

  1. Ansari N. H., Awasthi Y. C., Srivastava S. K. Role of glycosylation in protein disulfide formation and cataractogenesis. Exp Eye Res. 1980 Jul;31(1):9–19. doi: 10.1016/0014-4835(80)90086-x. [DOI] [PubMed] [Google Scholar]
  2. Babior B. M. Oxygen-dependent microbial killing by phagocytes (first of two parts). N Engl J Med. 1978 Mar 23;298(12):659–668. doi: 10.1056/NEJM197803232981205. [DOI] [PubMed] [Google Scholar]
  3. Chio K. S., Tappel A. L. Inactivation of ribonuclease and other enzymes by peroxidizing lipids and by malonaldehyde. Biochemistry. 1969 Jul;8(7):2827–2832. doi: 10.1021/bi00835a020. [DOI] [PubMed] [Google Scholar]
  4. Iversen S. A., Cawood P., Madigan M. J., Lawson A. M., Dormandy T. L. Identification of a diene conjugated component of human lipid as octadeca-9,11-dienoic acid. FEBS Lett. 1984 Jun 11;171(2):320–324. doi: 10.1016/0014-5793(84)80512-8. [DOI] [PubMed] [Google Scholar]
  5. Kennedy L., Baynes J. W. Non-enzymatic glycosylation and the chronic complications of diabetes: an overview. Diabetologia. 1984 Feb;26(2):93–98. doi: 10.1007/BF00281113. [DOI] [PubMed] [Google Scholar]
  6. Lunec J., Blake D. R., McCleary S. J., Brailsford S., Bacon P. A. Self-perpetuating mechanisms of immunoglobulin G aggregation in rheumatoid inflammation. J Clin Invest. 1985 Dec;76(6):2084–2090. doi: 10.1172/JCI112212. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lunec J., Dormandy T. L. Fluorescent lipid-peroxidation products in synovial fluid. Clin Sci (Lond) 1979 Jan;56(1):53–59. doi: 10.1042/cs0560053. [DOI] [PubMed] [Google Scholar]
  8. Lunec J., Halloran S. P., White A. G., Dormandy T. L. Free-radical oxidation (peroxidation) products in serum and synovial fluid in rheumatoid arthritis. J Rheumatol. 1981 Mar-Apr;8(2):233–245. [PubMed] [Google Scholar]
  9. Monnier V. M., Cerami A. Non-enzymatic glycosylation and browning of proteins in diabetes. Clin Endocrinol Metab. 1982 Jul;11(2):431–452. doi: 10.1016/s0300-595x(82)80023-6. [DOI] [PubMed] [Google Scholar]
  10. Monnier V. M., Vishwanath V., Frank K. E., Elmets C. A., Dauchot P., Kohn R. R. Relation between complications of type I diabetes mellitus and collagen-linked fluorescence. N Engl J Med. 1986 Feb 13;314(7):403–408. doi: 10.1056/NEJM198602133140702. [DOI] [PubMed] [Google Scholar]
  11. Nishigaki I., Hagihara M., Tsunekawa H., Maseki M., Yagi K. Lipid peroxide levels of serum lipoprotein fractions of diabetic patients. Biochem Med. 1981 Jun;25(3):373–378. doi: 10.1016/0006-2944(81)90096-x. [DOI] [PubMed] [Google Scholar]
  12. Satoh K. Serum lipid peroxide in cerebrovascular disorders determined by a new colorimetric method. Clin Chim Acta. 1978 Nov 15;90(1):37–43. doi: 10.1016/0009-8981(78)90081-5. [DOI] [PubMed] [Google Scholar]
  13. Schnider S. L., Kohn R. R. Effects of age and diabetes mellitus on the solubility and nonenzymatic glucosylation of human skin collagen. J Clin Invest. 1981 Jun;67(6):1630–1635. doi: 10.1172/JCI110198. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Schnider S. L., Kohn R. R. Glucosylation of human collagen in aging and diabetes mellitus. J Clin Invest. 1980 Nov;66(5):1179–1181. doi: 10.1172/JCI109950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Stevens V. J., Rouzer C. A., Monnier V. M., Cerami A. Diabetic cataract formation: potential role of glycosylation of lens crystallins. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2918–2922. doi: 10.1073/pnas.75.6.2918. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Tchobroutsky G. Relation of diabetic control to development of microvascular complications. Diabetologia. 1978 Sep;15(3):143–152. doi: 10.1007/BF00421230. [DOI] [PubMed] [Google Scholar]
  17. Thornalley P. J. Monosaccharide autoxidation in health and disease. Environ Health Perspect. 1985 Dec;64:297–307. doi: 10.1289/ehp.8564297. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Wickens D. G., Norden A. G., Lunec J., Dormandy T. L. Fluorescence changes in human gamma-globulin induced by free-radical activity. Biochim Biophys Acta. 1983 Feb 15;742(3):607–616. doi: 10.1016/0167-4838(83)90279-0. [DOI] [PubMed] [Google Scholar]

Articles from The British Journal of Cancer. Supplement are provided here courtesy of Cancer Research UK

RESOURCES