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Volumn 7, Issue 5, 1989, Pages 521-536

Macroxyproteinase (M.O.P.): A 670 kDa Proteinase complex that degrades oxidatively denatured proteins in red blood cells

Author keywords

Antioxidants; Free radicals; Macropin; Oxidative stress; Prosome; Proteasome; Protein degradation; Protein oxidation; Proteolysis

Indexed keywords

FREE RADICAL; PROTEASOME; PROTEINASE;

EID: 0024843661     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/0891-5849(89)90028-2     Document Type: Article
Times cited : (151)

References (54)
  • 2
  • 4
    • 0023655258 scopus 로고
    • Oxygen radicals stimulate proteolysis and lipid peroxidation by independent mechanisms in erythrocytes
    • (1987) J. Biol. Chem. , vol.262 , pp. 8220-8226
    • Davies1    Goldberg2
  • 9
    • 0023698151 scopus 로고
    • Oxidatively denatured proteins are degraded by an ATP-independent pathway in Escherichia coli
    • (1988) Free Radical Biol. Med. , vol.5 , pp. 225-236
    • Davies1    Lin2
  • 10
    • 0023655050 scopus 로고
    • Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells
    • (1987) J. Biol. Chem. , vol.262 , pp. 8227-8234
    • Davies1    Goldberg2
  • 11
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals: I. general aspects
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies1
  • 13
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals: III. modification of secondary and tertiary structure
    • (1987) J. Biol. Chem. , vol.262 , pp. 9908-9913
    • Davies1    Delsignore2
  • 14
    • 0023655449 scopus 로고
    • Protein damage and degradation by oxygen radicals: IV. degradation of denatured protein
    • (1987) J. Biol. Chem. , vol.262 , pp. 9914-9920
    • Davies1    Lin2    Pacific3
  • 15
  • 16
    • 9344223520 scopus 로고
    • A 700-kDa red cell proteinase which selectively degrades oxidatively denatured hemoglobin
    • abstr.
    • (1988) FASEB J. , vol.2 , pp. A1007
    • Pacifici1    Davies2
  • 18
    • 0024274376 scopus 로고
    • Superoxide dismutase is preferentially degraded by a proteolytic system from red blood cells following oxidative modification by hydrogen peroxide
    • (1988) Free Radical Biol. Med. , vol.5 , pp. 335-339
    • Salo1    Lin2    Pacific3    Davies4
  • 19
    • 0022644072 scopus 로고
    • Free radicals, lipids, and protein degradation
    • (1986) TIBS , vol.11 , pp. 27-31
    • Wolff1    Garner2    Dean3
  • 21
    • 0022996157 scopus 로고
    • Free-radical-mediated fragmentation of monoamine oxidase in the mitochondrial membrane
    • (1986) Biochem. J. , vol.240 , pp. 489-494
    • Dean1    Thomas2    Garner3
  • 22
    • 0022451471 scopus 로고
    • Fragmentation of proteins by free radicals and its effect on their susceptivility to enzymatic hydrolysis
    • (1986) Biochem. J. , vol.234 , pp. 399-403
    • Wolff1    Dean2
  • 25
    • 0021100174 scopus 로고
    • Oxidative inactivation of glutamine synthetase: I. inactivation is due to loss of one histidine residue
    • (1986) J. Biol. Chem. , vol.258 , pp. 11823-11827
    • Levine1
  • 26
    • 0021100140 scopus 로고
    • Oxidative modification of glutamine synthetase: II. characterization of the ascorbate model systems
    • (1983) J. Biol. Chem. , vol.258 , pp. 11828-11833
    • Levine1
  • 28
    • 0021848073 scopus 로고
    • Inactivation of Escherichi coli glutamine by xanthine oxidase, nicotine hydroxylase, horseradish peroxidase, or glucose oxidase: Effects of ferredoxin, putidaredoxin, and menadione
    • (1985) Arch. Biochem. Biophys. , vol.239 , pp. 379-387
    • Stadtman1    Wittenberger2
  • 29
    • 0023654044 scopus 로고
    • Purification of a protease from Escherichia coli with specificity for oxidase glutamine synthetase
    • (1987) J. Biol. Chem. , vol.262 , pp. 2101-2110
    • Roseman1    Levine2
  • 30
    • 0023766518 scopus 로고
    • Modulation of the hydrophobicity of glutamine synthetase by mixed-function oxidation
    • (1988) FASEB J. , vol.2 , pp. 2591-2595
    • Cervera1    Levine2
  • 31
    • 0021928777 scopus 로고
    • Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases
    • (1985) J. Biol. Chem. , vol.260 , pp. 300-305
    • Rivett1
  • 32
    • 0022374263 scopus 로고
    • Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase: Characterization as a high molecular weight cysteine proteinase
    • (1985) J. Biol. Chem. , vol.260 , pp. 12600-12606
    • Rivett1
  • 33
    • 0023664012 scopus 로고
    • Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes one of which degrades ubiquitin conjugates
    • (1987) J Biol Chem , vol.262 , pp. 2451-2457
    • Waxman1    Fagan2    Goldberg3
  • 36
    • 0018800923 scopus 로고
    • Identification and partial purification of an ATP-stimulated alkaline protease in rat liver
    • (1979) J. Biol. Chem. , vol.254 , pp. 3712-3715
    • DeMartino1    Goldberg2
  • 37
    • 0019195859 scopus 로고
    • Cation-sensitive neutral endopeptidase: Isolation and specificity of the bovine pituitary enzyme
    • (1980) J. Neurochem. , vol.35 , pp. 1172-1182
    • Wilk1    Orlowski2
  • 38
    • 0020674228 scopus 로고
    • Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex
    • (1983) J. Neurochem. , vol.40 , pp. 842-849
    • Wilk1    Orlowski2
  • 39
    • 0021110108 scopus 로고
    • Identification of three high molecular mass cysteine proteinases from rat skeletal muscle
    • (1983) FEBS Lett. , vol.160 , pp. 243-247
    • Dahlmann1    Kuehn2    Reinauer3
  • 41
    • 0347796615 scopus 로고
    • Purification of neutral lens endopeptidase: Close similarity to a neutral proteinase in pituitary
    • (1985) Proc. Nat. Acad. Sci. USA , vol.82 , pp. 7545-7549
    • Ray1    Harris2
  • 42
    • 0021925338 scopus 로고
    • Isolation of two forms of the high-molecular-mass serine protease, ingensin, from porcine skeletal muscle
    • (1985) FEBS Lett. , vol.189 , pp. 119-123
    • Ishiura1    Sano2    Kamakura3    Sagita4
  • 45
    • 0024285837 scopus 로고
    • Identity of the 19S ‘prosome’ particle with the large multifunctional protease complex of mammalian cells (the proteasome)
    • (1988) Nature , vol.331 , pp. 192-194
    • Arrigo1    Tanaka2    Goldberg3    Welch4
  • 46
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quatitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • (1976) Annal. Biochem. , vol.72 , pp. 248-254
    • Bradford1
  • 48
    • 0018786839 scopus 로고
    • Labeling of proteins by reductive methylation using sodium cyanoborohydride
    • (1979) J. Biol. Chem. , vol.245 , pp. 4359-4365
    • Jentoft1    Dearborn2
  • 51
    • 77957004737 scopus 로고
    • Protein fractionation on the basis of solubility in aqueous solutions of salts and organic solvents
    • (1955) Methods Enzymol. , vol.1 , pp. 67-90
    • Green1    Hughes2
  • 53
    • 0019784838 scopus 로고
    • ATP-dependent proteolysis of reticulocyte mitochondria is preceded by the attack of lipoxygenase
    • (1981) Biochem. I. , vol.3 , pp. 165-171
    • Dubiel1    Müller2    Rapoport3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.