Antibacterial activity of lysozyme and lactoferrin is inhibited by binding of advanced glycation–modified proteins to a conserved motif

Nature Medicine

Volumn 1, Issue 10, 1995, Pages 1057-1061

  Li, Yong Ming ^a   Tan, Annie X ^a   Vlassara, Helen ^a  

^a PICOWER INST FOR MEDICAL RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LACTOFERRIN; LYSOZYME;

ANTIBACTERIAL ACTIVITY; ARTICLE; BACTERIAL INFECTION; DIABETES MELLITUS; GLUCOSE METABOLISM; GLYCATION; HUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMAL; ANTI-INFECTIVE AGENTS; BINDING SITES; CONSERVED SEQUENCE; DIABETES MELLITUS; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMAN; LACTOFERRIN; MOLECULAR SEQUENCE DATA; MURAMIDASE; PROTEIN BINDING;

EID: 0028875176     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm1095-1057     Document Type: Article

References (27)

1. Monnier, V.M. & Cerami, A. Nonenzymatic browning in vivo: Possible process for aging of long-lived proteins. Science 211, 491-454 (1981).
2. Bucala, R., Vlassara, H. & Cerami, A. in Post-Transìationaì Modifications of Proteins (eds Harding, J.J. Crabbe, & MJ.C.) Ch 2, 53-79 (CRC Press, Boca Raton, Florida, 1992).
3. Vlassara, H., Bucala, R. & Striker, L. Pathogenic effects of advanced glycosyla-tion: Biochemical, biological, and clinical implications for diabetes and aging. J. lab. Invest. 70, 138-151 (1994).
4. Moutshen, M.P., Scheen, A.J. & Lefebvre P.J. Impaired immune responses in diabetes mellitus: Analysis of the factors and mechanisms involved. Relevance to the increased susceptibility of diabetic patients to specific infections. Diabetes Metab. (Paris) 18, 187-207 (1992).
5. Philips, D. The three-dimensional structure of an enzyme molecule. Sci. Am. 215, 78-90 (1966).
6. Anderson, B., Baker, H.M., Norris, G.E., Rumball, S.V. & Baker, E.N. Apo-lacto-ferrin structure demonstrates ligand-induced conformational change in transferrins. Nature 344, 784-787 (1992).
7. Reiter, B. & Oram, J.D. Bacterial inhibitors in milk and other biological fluids. Nature 216, 643-658 (1969).
8. Tenovuo, J., Lumikari, M. & Soukka, T. Salivary lysozyme, lactoferrin and peroxidases: Antibacterial effects on cariogenic bacteria and clinical applications in preventive dentistry. Proc. Finn, Dent. Soc. 87, 197-208 (1991).
9. Velikov, V.K. et al. Humoral factors of general and local immunity in diabetes mellitus. Ter. Arkh. 57, 20-22 (1985).
10. Muratsu, K. & Morioka, T. Levels of salivary lysosyme, lactoperoxidase and lactoferrin in diabetic hamsters. Infect. Immun. 48, 389-394 (1985).
11. Tenovuo, J. et al. Immunoglobulins and innate antimicrobial factors in whole saliva of patients with insulin-dependent diabetes mellitus. J. dent. Res. 65, 62-66 (1986).
12. Oberg, G. et al. Bactericidal proteins and neutral proteases in diabetes neutrophils. Diabetologia 29, 426-429 (1986).
13. Lechowski, R. et al. Serum lysosyme activity and nitroblue tetrazolium reduction test in dogs with diabetes mellitus. Zentralbl. Veterìnaermed. 38, 530-503 (1991).
14. Ben-Aryeh, H. et al. Oral health and salivary composition in diabetic patients. J. diabetes Complications 7, 57-62 (1993).
15. Makita, Z., Vlassara, H., Cerami, A. & Bucala, R. Immunochemical detection of advanced glycosylation end products. J. biol. Chem. 267, 5133-5138 (1992).
16. Soukka, T., Tenovuo, J. & Rundegren, J. Agglutination of Streptococcus mutans serotype C cells but inhibition of Porphyromonas gingivalis autoaggregation by human lactoferrin. Arch. Oral Biol. 38, 227-232 (1993).
17. Perillie, P.E. & Finch, S.C. in Lysosyme (eds Osserman, E.F., Canfield, R.E. & Beychok, S.) Ch. 31, 359-372 (Academic, New York and London, 1974).
18. Schmidt, A.M. et al. Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface. J. biol. Chem. 267, 14987-14997 (1992).
19. Vlassara, H., Brownlee, M. & Cerami, A. Novel macrophage receptor for glucose-modified proteins is distinct from previously described scavenger receptors. J. exp. Med. 164, 1301-1309 (1986).
20. Casey, J.I. in Diabetes Mellitus Theory and Practice (eds Rifkin, H. & Porte, D. Jr) Ch, 37, 617-625 (Elsevier, New York, Amsterdam, London, 1991).
21. Takada, K., Ohno, N. & Yadomae, T. Binding of lysozyme to lipopolysaccharide suppresses tumor necrosis factor production in vivo. Infect Immun. 62, 1171-1175 (1994).
22. Bellamy, W. et al. Identification of the bactericidal domain of LF. Biochim. biophys. Acta 1121, 130-136 (1992).
23. Gabay, J.E & Almeida, R.P. Antibiotic peptides and serine protease homologs in human polymorphonuclear leukocytes: Defensins and azurocidin. Curr. Opin. Immun. 5, 97-102 (1993).
24. Lehrer, R.I. Defensins: Antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11, 105-128 (1993).
25. Johnstone, A.P., Thunberg, A.L. & Kindt, T.J. Homogeneous rabbit immunoglobulin lacking group a allotypes: Amino acid sequence analysis of the heavy chain. Biochemistry 17, 1337-1343 (1978).
26. Mahoney, W.C. & Hermodson, M.A. High-yield cleavage of tryptophophnyl peptide bonds by o-iodosobenzoic acid. Biochemistry 18, 3810-4814 (1979).
27. Hopp-Woods method. Analyzed with MacVector 4.0 software, New Haven, Connecticut, and Lasergene, DNASTAR, Madison, Wisconsin.