Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1996 Apr 16;93(8):3205–3208. doi: 10.1073/pnas.93.8.3205

Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues.

J Moskovitz 1, N A Jenkins 1, D J Gilbert 1, N G Copeland 1, F Jursky 1, H Weissbach 1, N Brot 1
PMCID: PMC39583  PMID: 8622914

Abstract

Peptide methionine sulfoxide reductase (MsrA; EC 1.8.4.6) is a ubiquitous protein that can reduce methionine sulfoxide residues in proteins as well as in a large number of methyl sulfoxide compounds. The expression of MsrA in various rat tissues was determined by using immunocytochemical staining. Although the protein was found in all tissues examined, it was specifically localized to renal medulla and retinal pigmented epithelial cells, and it was prominent in neurons and throughout the nervous system. In addition, blood and alveolar macrophages showed high expression of the enzyme. The msrA gene was mapped to the central region of mouse chromosome 14, in a region of homology with human chromosomes 13 and 8p21.

Full text

PDF
3205

Images in this article

3206Fig. 2
on p.3206
3207Fig. 3
on p.3207
3207Fig. 4
on p.3207
3207Fig. 5
on p.3207

Selected References

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

  1. Abrams W. R., Weinbaum G., Weissbach L., Weissbach H., Brot N. Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7483–7486. doi: 10.1073/pnas.78.12.7483. [DOI] [PMC free article] [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. Blanton S. H., Heckenlively J. R., Cottingham A. W., Friedman J., Sadler L. A., Wagner M., Friedman L. H., Daiger S. P. Linkage mapping of autosomal dominant retinitis pigmentosa (RP1) to the pericentric region of human chromosome 8. Genomics. 1991 Dec;11(4):857–869. doi: 10.1016/0888-7543(91)90008-3. [DOI] [PubMed] [Google Scholar]
  4. Brot N., Fliss H., Coleman T., Weissbach H. Enzymatic reduction of methionine sulfoxide residues in proteins and peptides. Methods Enzymol. 1984;107:352–360. doi: 10.1016/0076-6879(84)07023-3. [DOI] [PubMed] [Google Scholar]
  5. Brot N., Weissbach H. Biochemistry of methionine sulfoxide residues in proteins. Biofactors. 1991 Jun;3(2):91–96. [PubMed] [Google Scholar]
  6. Brot N., Weissbach L., Werth J., Weissbach H. Enzymatic reduction of protein-bound methionine sulfoxide. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2155–2158. doi: 10.1073/pnas.78.4.2155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Copeland N. G., Jenkins N. A. Development and applications of a molecular genetic linkage map of the mouse genome. Trends Genet. 1991 Apr;7(4):113–118. doi: 10.1016/0168-9525(91)90455-y. [DOI] [PubMed] [Google Scholar]
  8. Copeland N. G., Jenkins N. A., Harvey R. P. The murine homeobox genes Nkx2.3 and Nkx2.6 are located on chromosomes 19 and 14, respectively. Genomics. 1994 Aug;22(3):655–656. doi: 10.1006/geno.1994.1444. [DOI] [PubMed] [Google Scholar]
  9. Coyle J. T., Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science. 1993 Oct 29;262(5134):689–695. doi: 10.1126/science.7901908. [DOI] [PubMed] [Google Scholar]
  10. Dryja T. P., Li T. Molecular genetics of retinitis pigmentosa. Hum Mol Genet. 1995;4(Spec No):1739–1743. doi: 10.1093/hmg/4.suppl_1.1739. [DOI] [PubMed] [Google Scholar]
  11. Duescher R. J., Lawton M. P., Philpot R. M., Elfarra A. A. Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes. J Biol Chem. 1994 Jul 1;269(26):17525–17530. [PubMed] [Google Scholar]
  12. Fliss H., Vasanthakumar G., Schiffmann E., Weissbach H., Brot N. Enzymatic reduction of oxidized chemotactic peptide N-formyl-L-methionyl-sulfoxide-L-leucyl-L-phenylalanine. Biochem Biophys Res Commun. 1982 Nov 16;109(1):194–201. doi: 10.1016/0006-291x(82)91584-4. [DOI] [PubMed] [Google Scholar]
  13. Haefliger J. A., Bruzzone R., Jenkins N. A., Gilbert D. J., Copeland N. G., Paul D. L. Four novel members of the connexin family of gap junction proteins. Molecular cloning, expression, and chromosome mapping. J Biol Chem. 1992 Jan 25;267(3):2057–2064. [PubMed] [Google Scholar]
  14. Jenkins N. A., Copeland N. G., Taylor B. A., Lee B. K. Organization, distribution, and stability of endogenous ecotropic murine leukemia virus DNA sequences in chromosomes of Mus musculus. J Virol. 1982 Jul;43(1):26–36. doi: 10.1128/jvi.43.1.26-36.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Katz M. L., Stone W. L., Dratz E. A. Fluorescent pigment accumulation in retinal pigment epithelium of antioxidant-deficient rats. Invest Ophthalmol Vis Sci. 1978 Nov;17(11):1049–1058. [PubMed] [Google Scholar]
  16. Liles M. R., Newsome D. A., Oliver P. D. Antioxidant enzymes in the aging human retinal pigment epithelium. Arch Ophthalmol. 1991 Sep;109(9):1285–1288. doi: 10.1001/archopht.1991.01080090111033. [DOI] [PubMed] [Google Scholar]
  17. Miceli M. V., Liles M. R., Newsome D. A. Evaluation of oxidative processes in human pigment epithelial cells associated with retinal outer segment phagocytosis. Exp Cell Res. 1994 Sep;214(1):242–249. doi: 10.1006/excr.1994.1254. [DOI] [PubMed] [Google Scholar]
  18. Moore K. J., D'Amore-Bruno M. A., Korfhagen T. R., Glasser S. W., Whitsett J. A., Jenkins N. A., Copeland N. G. Chromosomal localization of three pulmonary surfactant protein genes in the mouse. Genomics. 1992 Feb;12(2):388–393. doi: 10.1016/0888-7543(92)90389-a. [DOI] [PubMed] [Google Scholar]
  19. Moskovitz J., Rahman M. A., Strassman J., Yancey S. O., Kushner S. R., Brot N., Weissbach H. Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J Bacteriol. 1995 Feb;177(3):502–507. doi: 10.1128/jb.177.3.502-507.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Moskovitz J., Weissbach H., Brot N. Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2095–2099. doi: 10.1073/pnas.93.5.2095. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Noell W. K. Effects of environmental lighting and dietary vitamin A on the vulnerability of the retina to light damage. Photochem Photobiol. 1979 Apr;29(4):717–723. doi: 10.1111/j.1751-1097.1979.tb07756.x. [DOI] [PubMed] [Google Scholar]
  22. Rahman M. A., Nelson H., Weissbach H., Brot N. Cloning, sequencing, and expression of the Escherichia coli peptide methionine sulfoxide reductase gene. J Biol Chem. 1992 Aug 5;267(22):15549–15551. [PubMed] [Google Scholar]
  23. Young R. W., Bok D. Participation of the retinal pigment epithelium in the rod outer segment renewal process. J Cell Biol. 1969 Aug;42(2):392–403. doi: 10.1083/jcb.42.2.392. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES