D-aspartate content of erythrocyte membrane proteins is decreased in uremia: Implications for the repair of damaged proteins

Journal of the American Society of Nephrology

Volumn 8, Issue 1, 1997, Pages 95-104

  Perna, Alessandra F ^a   D'Aniello, Antimo ^b   Lowenson, Jonathan D ^c   Clarke, Steven ^c   De Santo, Natale G ^a   Ingrosso, Diego ^a,d  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

^b STAZIONE ZOOLOGICA ANTON DOHRN   (Italy)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d Ist di Biochim delle Macromolecole   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; MEMBRANE PROTEIN;

ADULT; AGED; ARTICLE; CHRONIC KIDNEY FAILURE; CLINICAL ARTICLE; CONTROLLED STUDY; ERYTHROCYTE MEMBRANE; FEMALE; HEMODIALYSIS; HUMAN; MALE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MODIFICATION; PROTEIN STRUCTURE; SIMULATION; UREMIA;

EID: 0030712472     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (48)

1. Galletti P, Ingrosso D, Manna C, Clemente G, Zappia V: Protein damage and methylation mediated repair in the erythrocyte. Biochem J 306: 313-325, 1995
2. Ota IM, Clarke S: The function and enzymology of protein D-aspartyl/L-isoaspartyl methyltrasferases in eukaryotic and prokaryotic cells. In:. Protein Methylation, edited by Paik WK, Kim S, Boca Raton, FL, CRC Press, 1990, pp 179-194
3. Brunauer LS, Clarke S: Age-dependent accumulation of protein residues that can be hydrolyzed to D-aspartic acid in human erythrocytes. J Biol Chem 261: 12538-12543, 1986
4. Stephenson RC, Clarke S: Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J Biol Chem 264: 6164-6170, 1989
5. Clarke S: Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins. Int J Peptide Protein Res 30: 808-821, 1987
6. Geiger T, Clarke S: Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides: Succinimide-linked reactions that contribute to protein degradation. J Biol Chem 262: 785-794, 1987
7. McFadden PN, Clarke S: Chemical conversion of aspartyl peptides to isoaspartyl peptides: A method for generating new methyl-accepting substrates for the erythrocyte D-aspartyl/L-isoaspartyl protein methyltransferase. J Biol Chem 261: 11503-11511, 1986
8. Roher AE, Lowenson JD, Clarke S, Wolkow C, Wang R, Cotter RJ, Reardon IM, Zürcher-Neely HA, Heinrikson RL, Ball MJ, Greenberg BD: Structural alterations in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem 268: 3072-3083, 1993
9. Fabian H, Szendrei GI, Mantsch HH, Greenberg BD, Ötvös L: Synthetic post-translationally modified human Aβ peptide exhibits a markedly increased tendency to form β-pleated sheets in vitro. Eur J Biochem 221: 959-964, 1994
10. Roher AE, Lowenson JD, Clarke S, Woods AS, Cotter RJ, Cowing E, Ball MJ: β-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease. Proc Natl Acad Sci USA 90: 10836-10840, 1993
11. 23 residue affects the aggregation properties of Alzheimer amyloid β protein analogues. J Biol Chem 269: 10205-10208, 1994
12. Hefman PM, Bada JL: Aspartic acid racemization in dentine as a measure of aging. Nature (Lond) 262: 279-281, 1976
13. Masters PM, Bada JL, Zigler JS: Aspartic acid racemization in heavy molecular weight crystallins and water-insoluble protein from normal human lenses and cataracts. Proc Natl Acad Sci USA 75: 1204-1208, 1978
14. Cohen CM: New trends in understanding the regulation of red cell membrane skeleton organization. Adv Cell Biol 2: 1-24, 1988
15. Johnson BA, Murray ED, Clarke S, Glass DB, Aswad DA: Protein carboxyl methyltransferase facilitates the conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides. J Biol Chem 262: 5622-5629, 1987
16. Galletti P, Ciardiello A, Ingrosso D, Di Donato A, D'Alessio G: Repair of isopeptide bonds by protein carboxyl O-methyltransferase: Seminal ribonuclease as a model system. Biochemistry 27: 1752-1757, 1988
17. McFadden PN, Clarke S: Conversion of isoaspartyl peptides to normal peptides: Implications for the cellular repair of damaged proteins. Proc Natl Acad Sci USA 84: 2595-2599, 1987
18. Inauen W, Stäubli M, Descoeudres C, Galeazzi RL, Straub PW: Erythrocyte deformability in dialysed and nondialysed uraemic patients. Eur J Clin Invest 12: 173-176, 1982
19. - anion exchanger in erythrocytes of uraemic patients. Nephrol Dial Transplant 5: 1018-1022, 1990
20. Perna AF, Ingrosso D, Galletti P, Zappia V, De Santo NG: Enzymatic methyl esterification of erythrocyte membrane proteins is impaired in chronic renal failure: Evidence for high levels of the natural inhibitor S-adenosylhomocysteine. J Clin Invest 91: 2497-2503, 1993
21. D'Aniello A, Giuditta A: Identification of D-aspartic acid in the brain of Octopus vulgaris Lam. J Neurochem 29: 1053-1057, 1977
22. D'Aniello A, D'Onofrio G, Pischetola M, D'Aniello G, Vetere A, Petrucelli L, Fisher GH: Biological role of D-amino acid oxidase and D-aspartate oxidase. Effects of D-amino acids. J Biol Chem 268: 26941-26949, 1993
23. D'Aniello A, Strazzullo L: Peptidyl-D-amino acid hydrolase from Loligo vulgaris Lam: Purification and characterization. J Biol Chem 259: 4237-4243, 1984
24. Lowenson JD, Clarke S: Recognition of D-aspartyl residues in polypeptides by the erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis. J Biol Chem 267: 5985-5995, 1992
25. Bradford MM: A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254, 1976
26. D'Aniello A, Petrucelli L, Gardner C, Fisher G: Improved method for hydrolyzing proteins and peptides without inducing racemization and for determining their true D-amino acid content. Anal Biochem 213: 290-295, 1993
27. Doi E, Shibata D, Matoba T: Modified colorimetric ninhydrin methods for peptidase assay. Anal Biochem 118: 173-184, 1981
28. Godel H, Graser T, Földi P, Pfaender P, Fürst P: Measurement of free amino acids in human biological fluids by high-performance liquid chromatography. J Chromatogr 297: 49-61, 1984
29. D'Aniello A, Vetere A, Petrucelli L: Further study on the specificity of D-amino acid oxidase and of D-aspartate oxidase and time course for complete oxidation of D-amino acids. Comp Biochem Physiol 105B: 731-734, 1993
30. Aswad DW: Determination of D- and L-aspartate in amino acid mixtures by high performance liquid chromatography after derivatization with a chiral adduct of o-phthaldialdehyde. Anal Biochem 137: 405-407, 1984
31. Kaplan NO, Colowick SP, Barnes CC: Effect of alkali on diphosphopyridine nucleotide. J Biol Chem 191: 461-471, 1951
32. Akmal M, Telfer N, Ansari AN, Massry SG: Erythrocyte survival in chronic renal failure. Role of secondary hyperparathyroidism. J Clin Invest 76: 1695-1698, 1985
33. Haram S, Carriero D, Seaman C, Piomelli S: The mechanism of decline of age-dependent enzymes in the red blood cell. Enzyme 45: 47-53, 1991
34. Zappia V, Zydek-Cwick CR, Schlenk F: The specificity of s-adenosylmethionine derivatives in methyl transfer reactions. J Biol Chem 244: 4499-4505, 1969
35. Cantoni GL, Chiang PK: The role of S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase in the control of biologic methylations. In: Natural Sulfur Compounds: Novel Biochemical and Structural Aspects, edited by Cavallini D, Gaull GE, Zappia V, New York, Plenum Press, 1980, pp 67-89
36. Johnson BA, Aswad DW: Kinetic properties of bovine brain protein L-isoaspartyl methyltransferase determined using a synthetic isoaspartyl peptide substrate. Neurochem Res 18: 87-94, 1993
37. Lowenson JD, Clarke S: Spontaneous degradation and enzymatic repair of aspartyl and asparaginyl residues in aging red cell proteins analyzed by computer simulation. Gerontology 37: 128-151, 1991
38. Murray ED, Clarke S: Synthetic peptide substrates for the erythrocyte protein carboxyl methyltransferase. J Biol Chem 259: 10722-10732, 1984
39. Brennan TV, Anderson JW, Jia Z, Waygood EB, Clarke S: Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L-isoaspartate-(D-Aspartate)-O-methyltransferase. J Biol Chem 269: 24586-24595, 1994
40. Fujii N, Satoh K, Harada K, Ishibashi Y: Simultaneous stereoinversion and isomerization at specific aspartic acid residues in alpha A-crystallin from human lens. J Biochem 116: 663-669, 1994
41. Perna AF, Ingrosso D, De Santo N G, Galletti P, Zappia V: Mechanism of erythrocyte accumulation of methylation inhibitor S-adenosylhomocystcine in uremia. Kidney Int 47: 247-253, 1995
42. Lubec G, Weniger M, Anderson SR: Racemization and oxidation studies of hair protein in the Homo tirolensis. FASEB J 8: 1166-1169, 1994
43. Ingrosso D, D'Angelo S, Perna AF, Miraglia del Giudice E, Iolascon A, Perrotta S, Zappia V, Galletti P: Increased membrane protein methylation in hereditary spherocytosis: A marker of cytoskeletal disarray. Eur J Biochem 228: 894-898, 1995
44. Ingrosso D, D'Angelo S, Perrotta S, D'Urzo G, Iolascon A, Perna AF, Galletti P, Zappia V, Miraglia del Giudice E: Cytoskeletal behaviour in spectrin and in band 3 deficient spherocytic red cells: Evidence for a differentiated splenic conditioning role. Br J Haematol 93: 38-41, 1996
45. + pump in chronic renal failure. Am J Physiol 252: F785-F793, 1987
46. Kelly RA, Canessa ML, Steinman TI, Mitch WE: Hemodialysis and red cell cation transport in uremia: Role of membrane free fatty acids. Kidney Int 35: 595-603, 1989
47. Corry DB, Lee DBM, Tuek ML: A kinetic study of cation transport in erythrocytes from uremic patients. Kidney Int 32: 256-260, 1987
48. McGrath LT, Douglas AF, McClean E, Brown JH, Doherty CC, Johnston GD, Pooler G, Archbold R: Oxidative stress and erythrocyte membrane fluidity in patients undergoing regular dialysis. Clin Chim Acta 235: 179-188, 1995