Identification of chicken lysozyme g2 and its expression in the intestine

Cellular and Molecular Life Sciences

Volumn 61, Issue 21, 2004, Pages 2760-2766

  Nile, C J ^a   Townes, C L ^a   Michailidis, G ^a   Hirst, B H ^a   Hall, J ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

Antimicrobial; Chicken; Innate immunity; Lysozyme; Paneth cell

Indexed keywords

CYSTEINE; MESSENGER RNA; PEPTIDE;

ARTICLE; CHICKEN; EPITHELIUM CELL; FISH; GENE IDENTIFICATION; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; IMMUNOLOCALIZATION; INTESTINE CELL; INTESTINE CRYPT; LYSOSOME; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PANETH CELL; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION; SMALL INTESTINE; STAINING;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CHICKENS; GENE EXPRESSION PROFILING; IMMUNOHISTOCHEMISTRY; INTESTINES; MICE; MOLECULAR SEQUENCE DATA; MURAMIDASE; RNA, MESSENGER; SEQUENCE ALIGNMENT;

AVES; GALLUS; GALLUS GALLUS; MAMMALIA;

EID: 11144295219     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-004-4345-z     Document Type: Article

References (24)

1. Ouellette A. J. (1997) Paneth cells and innate immunity in the crypt microenvironment. Gastroenterology 113: 1779-1784
2. Ganz T. (2004) Antimicrobial polypeptides. J. Leukoc. Biol. 75: 28-34
3. Hancock R. E. and Scott M. G. (2000) The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. USA 97: 8856-8861
4. Short M. L., Nickel J., Schmitz A. and Renkawitz R. (1996) Lysozyme gene expression and regulation. Exs 75: 243-257
5. Ibrahim H. R., Thomas U. and Pellegrini A. (2001) A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. J. Biol. Chem. 276: 43767-43774
6. Ghoos Y. and Vantrappen G. (1971) The cytochemical localization of lysozyme in Paneth cell granules. Histochem. J. 3: 175-178
7. Peeters T. and Vantrappen G. (1975) The Paneth cell: a source of intestinal lysozyme. Gut 16: 553-558
8. Porter E. M., Bevins C. L., Ghosh D. and Ganz T. (2002) The multifaceted Paneth cell. Cell. Mol. Life Sci. 59: 156-170
9. Hammer M. F., Schilling J. W., Prager E. M. and Wilson A. C. (1987) Recruitment of lysozyme as a major enzyme in the mouse gul: duplication, divergence, and regulatory evolution. J. Mol. Evol. 24: 272-279
10. Ganz T., Gabayan V., Liao H. I., Liu L., Oren A., Graf T. et al. (2003) Increased inflammation in lysozyme M-deficient mice in response to Micrococcus luteus and its peptidoglycan. Blood 101: 2388-2392
11. Hindenburg A., Spitznagel J. and Arnheim N. (1974) Isozymes of lysozyme in leukocytes and egg white: evidence for the species-specific control of egg-white lysozyme synthesis. Proc. Natl. Acad. Sci. USA 71: 1653-1657
12. Humphrey C. D. and Turk D. E. (1974) The ultrastructure of normal chick intestinal epithelium. Poultry Sci. 53: 990-1000
13. Jolles P., Schoentgen F., Jolles J., Dobson D. E., Prager E. M. and Wilson A. C. (1984) Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2 and immunological comparisons with other lysozymes. J. Biol. Chem. 259: 11617-11625
14. Yu M. and Irwin D. M. (1996) Evolution of stomach lysozyme: the pig lysozyme gene. Mol. Phylogenet. Evol. 5: 298-308
15. Nakano T. and Graf T. ( 1991 ) Goose-type lysozyme gene of the chicken: sequence, genomic organization and expression reveals major differences to chicken-type lysozyme gene. Biochim. Biophys. Acta 1090: 273-276
16. Irwin D. M. and Gong Z. (2003) Molecular evolution of vertebrate goose-type lysozyme genes. J. Mol. Evol. 56: 234-242
17. Rubio C. A. and Nesi G. (2003) A simple method to demonstrate normal and metaplastic Paneth cells in tissue sections. In Vivo 17: 67-71
18. Boardman P. E., Sanz-Ezquerro J., Overton I. M., Burt D. W., Bosch E., Fong W. T. et al. (2002) A comprehensive collection of chicken cDNAs. Curr. Biol. 12: 1965-1969
19. Hikima J., Minagawa S., Hirono I. and Aoki T. (2001) Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein. Biochim. Biophys. Acta 1520: 35-44
20. Yin Z. X., He J. G., Deng W. X. and Chan S. M. (2003) Molecular cloning, expression of orange-spotted grouper goose-type lysozyme cDNA, and lytic activity of its recombinant protein. Dis. Aquat. Organ. 55: 117-123
21. Savan R., Aman A. and Sakai M. (2003) Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.). Fish Shellfish Immunol. 15: 263-268
22. Dobson D. E., Prager E. M. and Wilson A. C. (1984) Stomach lysozymes of ruminants. I. Distribution and catalytic properties. J. Biol. Chem. 259: 11607-11616
23. Hemmen F., Mahana W., Jolles P. and Paraf A. (1992) Common antigenic properties of a g-type (goose) and a c-type (duck) egg white lysozyme: antibody responses in rabbits and mice. Experientia 48: 79-84
24. Wein S., Fauroux M., Laffitte J., De Nadai P., Guaini C., Pons F. et al. (2004) Mediation of annexin 1 secretion by a probenecid-sensitive ABC-transporter in rat inflamed mucosa. Biochem. Pharmacol. 67: 1195-1202