메뉴 건너뛰기




Volumn 2006, Issue , 2006, Pages

Heme deficiency in Alzheimer's disease: A possible connection to porphyria

Author keywords

[No Author keywords available]

Indexed keywords

HEME;

EID: 33746824988     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/JBB/2006/24038     Document Type: Review
Times cited : (11)

References (48)
  • 2
    • 0345276568 scopus 로고    scopus 로고
    • Synaptic pathology in Alzheimer's disease: A review of ultrastructural studies
    • sscheff@email.uky.edu
    • S W Scheff sscheff@email.uky.edu D A Price Synaptic pathology in Alzheimer's disease: a review of ultrastructural studies. Neurobiology of Aging 24 8 2003 1029 1046
    • (2003) Neurobiology of Aging , vol.24 , Issue.8 , pp. 1029-1046
    • Scheff, S.W.1    Price, D.A.2
  • 3
    • 0346250794 scopus 로고    scopus 로고
    • Psychosis of Alzheimer's disease: Clinical characteristics and history
    • lschneid@usc.edu
    • L S Schneider lschneid@usc.edu K S Dagerman Psychosis of Alzheimer's disease: clinical characteristics and history. Journal of Psychiatric Research 38 1 2004 105 111
    • (2004) Journal of Psychiatric Research , vol.38 , Issue.1 , pp. 105-111
    • Schneider, L.S.1    Dagerman, K.S.2
  • 11
    • 4644269324 scopus 로고    scopus 로고
    • Porphyric neuropathy
    • jwalbers@umich.edu
    • J W Albers jwalbers@umich.edu J K Fink Porphyric neuropathy. Muscle and Nerve 30 4 2004 410 422
    • (2004) Muscle and Nerve , vol.30 , Issue.4 , pp. 410-422
    • Albers, J.W.1    Fink, J.K.2
  • 12
    • 14844362079 scopus 로고    scopus 로고
    • Recommendations for the diagnosis and treatment of the acute porphyrias
    • K E Anderson J R Bloomer H L Bonkovsky Recommendations for the diagnosis and treatment of the acute porphyrias. Annals of Internal Medicine 142 6 2005 439 450
    • (2005) Annals of Internal Medicine , vol.142 , Issue.6 , pp. 439-450
    • Anderson, K.E.1    Bloomer, J.R.2    Bonkovsky, H.L.3
  • 13
    • 19444372706 scopus 로고    scopus 로고
    • Molecular mechanisms of dominant expression in porphyria
    • badmintonmn@Cardiff.ac.uk
    • M N Badminton badmintonmn@Cardiff.ac.uk G H Elder Molecular mechanisms of dominant expression in porphyria. Journal of Inherited Metabolic Disease 28 3 2005 277 286
    • (2005) Journal of Inherited Metabolic Disease , vol.28 , Issue.3 , pp. 277-286
    • Badminton, M.N.1    Elder, G.H.2
  • 14
    • 23944476164 scopus 로고    scopus 로고
    • Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1α
    • C Handschin J Lin J Rhee Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1α Cell 122 4 2005 505 515
    • (2005) Cell , vol.122 , Issue.4 , pp. 505-515
    • Handschin, C.1    Lin, J.2    Rhee, J.3
  • 15
    • 23944503364 scopus 로고    scopus 로고
    • PGC-1α: Looking behind the sweet treat for porphyria
    • D Li PGC-1α: looking behind the sweet treat for porphyria. Cell 122 4 2005 487 489
    • (2005) Cell , vol.122 , Issue.4 , pp. 487-489
    • Li, D.1
  • 16
    • 0033560646 scopus 로고    scopus 로고
    • Motor neuropathy in porphobilinogen deaminase-deficient mice imitates the peripheral neuropathy of human acute porphyria
    • R LP Lindberg R Martini M Baumgartner Motor neuropathy in porphobilinogen deaminase-deficient mice imitates the peripheral neuropathy of human acute porphyria. Journal of Clinical Investigation 103 8 1999 1127 1134
    • (1999) Journal of Clinical Investigation , vol.103 , Issue.8 , pp. 1127-1134
    • Lindberg, R.L.P.1    Martini, R.2    Baumgartner, M.3
  • 17
    • 0030069657 scopus 로고    scopus 로고
    • Porphobilinogen deaminase deficiency in mice causes a neuropathy resembling that of human hepatic porphyria
    • R LP Lindberg C Porcher B Grandchamp Porphobilinogen deaminase deficiency in mice causes a neuropathy resembling that of human hepatic porphyria. Nature Genetics 12 2 1996 195 199
    • (1996) Nature Genetics , vol.12 , Issue.2 , pp. 195-199
    • Lindberg, R.L.P.1    Porcher, C.2    Grandchamp, B.3
  • 18
    • 3042698908 scopus 로고    scopus 로고
    • Biochemical characterization of porphobilinogen deaminase-deficient mice during phenobarbital induction of heme synthesis and the effect of enzyme replacement
    • Annika.Johansson@labmed.ki.se
    • A Johansson Annika.Johansson@labmed.ki.se C Möller J Fogh P Harper Biochemical characterization of porphobilinogen deaminase-deficient mice during phenobarbital induction of heme synthesis and the effect of enzyme replacement. Molecular Medicine 9 9-12 2003 193 199
    • (2003) Molecular Medicine , vol.9 , Issue.9-12 , pp. 193-199
    • Johansson, A.1    Möller, C.2    Fogh, J.3    Harper, P.4
  • 19
    • 0027486719 scopus 로고
    • Tissue distribution of succinylacetone in the rat in vivo: A possible basis for neurotoxicity in hereditary infantile tyrosinemia
    • P A Wyss S Boynton J Chu K S Roth Tissue distribution of succinylacetone in the rat in vivo: a possible basis for neurotoxicity in hereditary infantile tyrosinemia. Biochimica et Biophysica Acta 1182 3 1993 323 328
    • (1993) Biochimica et Biophysica Acta , vol.1182 , Issue.3 , pp. 323-328
    • Wyss, P.A.1    Boynton, S.2    Chu, J.3    Roth, K.S.4
  • 20
    • 1542271496 scopus 로고    scopus 로고
    • Liver transplantation as a cure for acute intermittent porphyria
    • Z F Soonawalla T Orug M N Badminton Liver transplantation as a cure for acute intermittent porphyria. The Lancet 363 9410 2004 705 706
    • (2004) The Lancet , vol.363 , Issue.9410 , pp. 705-706
    • Soonawalla, Z.F.1    Orug, T.2    Badminton, M.N.3
  • 21
    • 7744243502 scopus 로고    scopus 로고
    • Acute intermittent porphyria: Studies of the severe homozygous dominant disease provides insights into the neurologic attacks in acute porphyrias
    • C Solis A Martinez-Bermejo T P Naidich Acute intermittent porphyria: studies of the severe homozygous dominant disease provides insights into the neurologic attacks in acute porphyrias. Archives of Neurology 61 11 2004 1764 1770
    • (2004) Archives of Neurology , vol.61 , Issue.11 , pp. 1764-1770
    • Solis, C.1    Martinez-Bermejo, A.2    Naidich, T.P.3
  • 25
    • 0018160696 scopus 로고
    • δ-Aminolevulinic acid synthetase: Regulation of activity in various tissues of the aging rat
    • J R Jr Paterniti C IP Lin D S Beattie δ-Aminolevulinic acid synthetase: regulation of activity in various tissues of the aging rat. Archives of Biochemistry and Biophysics 191 2 1978 792 797
    • (1978) Archives of Biochemistry and Biophysics , vol.191 , Issue.2 , pp. 792-797
    • Paterniti Jr., J.R.1    Lin, C.I.P.2    Beattie, D.S.3
  • 26
    • 0035879693 scopus 로고    scopus 로고
    • Active glycation in neurofibrillary pathology of Alzheimer disease: Nε-(carboxymethyl) lysine and hexitol-lysine
    • R J Castellani P LR Harris L M Sayre Active glycation in neurofibrillary pathology of Alzheimer disease: N ε-(carboxymethyl) lysine and hexitol-lysine. Free Radical Biology and Medicine 31 2 2001 175 180
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.2 , pp. 175-180
    • Castellani, R.J.1    Harris, P.L.R.2    Sayre, L.M.3
  • 27
    • 0034213854 scopus 로고    scopus 로고
    • Preventive aspirin treatment of streptozotocin induced diabetes: Blockage of oxidative status and revertion of heme enzymes inhibition
    • batlle@mail.retina.ar
    • F Caballero E Gerez A Batlle batlle@mail.retina.ar E Vazquez Preventive aspirin treatment of streptozotocin induced diabetes: blockage of oxidative status and revertion of heme enzymes inhibition. Chemico-Biological Interactions 126 3 2000 215 225
    • (2000) Chemico-Biological Interactions , vol.126 , Issue.3 , pp. 215-225
    • Caballero, F.1    Gerez, E.2    Batlle, A.3    Vazquez, E.4
  • 30
    • 0035930604 scopus 로고    scopus 로고
    • Heme deficiency selectively interrupts assembly of mitochondrial complex IV in human fibroblasts: Relevance to aging
    • bnames@uclink4.berkeley.edu
    • H Atamna J Liu B N Ames bnames@uclink4.berkeley.edu Heme deficiency selectively interrupts assembly of mitochondrial complex IV in human fibroblasts: relevance to aging. Journal of Biological Chemistry 276 51 2001 48410 48416
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.51 , pp. 48410-48416
    • Atamna, H.1    Liu, J.2    Ames, B.N.3
  • 31
    • 0141671890 scopus 로고    scopus 로고
    • Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation
    • rkhalifah@biostratum.com
    • B L Cussimanio A A Booth P Todd B G Hudson R G Khalifah rkhalifah@biostratum.com Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophysical Chemistry 105 2-3 2003 743 755
    • (2003) Biophysical Chemistry , vol.105 , Issue.2-3 , pp. 743-755
    • Cussimanio, B.L.1    Booth, A.A.2    Todd, P.3    Hudson, B.G.4    Khalifah, R.G.5
  • 32
    • 0028304705 scopus 로고
    • Heme oxygenase-1 is associated with the neurofibrillary pathology of Alzheimer's disease
    • M A Smith R K Kutty P L Richey Heme oxygenase-1 is associated with the neurofibrillary pathology of Alzheimer's disease. American Journal of Pathology 145 1 1994 42 47
    • (1994) American Journal of Pathology , vol.145 , Issue.1 , pp. 42-47
    • Smith, M.A.1    Kutty, R.K.2    Richey, P.L.3
  • 33
    • 0029032632 scopus 로고
    • Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain
    • H M Schipper S Cisse E G Stopa Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain. Annals of Neurology 37 6 1995 758 768
    • (1995) Annals of Neurology , vol.37 , Issue.6 , pp. 758-768
    • Schipper, H.M.1    Cisse, S.2    Stopa, E.G.3
  • 34
    • 0030778396 scopus 로고    scopus 로고
    • Hemin and related porphyrins inhibit β-amyloid aggregation
    • Patrick_Camilleri@sbphrd.com
    • D Howlett P Cutler S Heales P Camilleri Patrick_Camilleri@sbphrd.com Hemin and related porphyrins inhibit β-amyloid aggregation. FEBS Letters 417 2 1997 249 251
    • (1997) FEBS Letters , vol.417 , Issue.2 , pp. 249-251
    • Howlett, D.1    Cutler, P.2    Heales, S.3    Camilleri, P.4
  • 35
    • 0034633298 scopus 로고    scopus 로고
    • Detection of β-amyloid peptide aggregation using DNA electrophoresis
    • B W Ahn D U Song Y D Jung Detection of β-amyloid peptide aggregation using DNA electrophoresis. Analytical Biochemistry 284 2 2000 401 405
    • (2000) Analytical Biochemistry , vol.284 , Issue.2 , pp. 401-405
    • Ahn, B.W.1    Song, D.U.2    Jung, Y.D.3
  • 36
    • 33644836605 scopus 로고    scopus 로고
    • Heme deficiency is associated with senescence and causes suppression of N-methyl-D-aspartate receptor subunits expression in primary cortical neurons
    • tc28@le.ac.uk
    • T Chernova tc28@le.ac.uk P Nicotera A G Smith Heme deficiency is associated with senescence and causes suppression of N-methyl-D-aspartate receptor subunits expression in primary cortical neurons. Molecular Pharmacology 69 3 2006 697 705
    • (2006) Molecular Pharmacology , vol.69 , Issue.3 , pp. 697-705
    • Chernova, T.1    Nicotera, P.2    Smith, A.G.3
  • 37
    • 20444427541 scopus 로고    scopus 로고
    • Heme deficiency suppresses the expression of key neuronal genes and causes neuronal cell death
    • lz2115@columbia.edu
    • A Sengupta T Hon L Zhang lz2115@columbia.edu Heme deficiency suppresses the expression of key neuronal genes and causes neuronal cell death. Molecular Brain Research 137 1-2 2005 23 30
    • (2005) Molecular Brain Research , vol.137 , Issue.1-2 , pp. 23-30
    • Sengupta, A.1    Hon, T.2    Zhang, L.3
  • 39
    • 0022547219 scopus 로고
    • Generation of active oxygen species during coupled auto oxidation of oxyhemoglobin and δ-aminolevulinic acid
    • 3081047
    • H P Monteiro D SP Abdalla A Faljoni-Alario E JH Bechara Generation of active oxygen species during coupled auto oxidation of oxyhemoglobin and δ-aminolevulinic acid. Biochimica et Biophysica Acta 1986 881 1 100 106 3081047
    • (1986) Biochimica et Biophysica Acta , vol.881 , Issue.1 , pp. 100-106
    • Monteiro, H.P.1    Abdalla, D.S.P.2    Faljoni-Alario, A.3    Bechara, E.J.H.4
  • 40
  • 41
    • 0034650877 scopus 로고    scopus 로고
    • DNA damage by 5-aminolevulinic and 4,5-dioxovaleric acids in the presence of ferritin
    • pdmascio@iq.usp.br
    • P Di Mascio pdmascio@iq.usp.br P C Teixeira J Onuki DNA damage by 5-aminolevulinic and 4,5-dioxovaleric acids in the presence of ferritin. Archives of Biochemistry and Biophysics 373 2 2000 368 374
    • (2000) Archives of Biochemistry and Biophysics , vol.373 , Issue.2 , pp. 368-374
    • Di Mascio, P.1    Teixeira, P.C.2    Onuki, J.3
  • 42
  • 44
    • 0034672594 scopus 로고    scopus 로고
    • Roles of phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid
    • M EM Rocha A MDC Ferreira E JH Bechara Roles of phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid. Free Radical Biology and Medicine 29 12 2000 1272 1279
    • (2000) Free Radical Biology and Medicine , vol.29 , Issue.12 , pp. 1272-1279
    • Rocha, M.E.M.1    Mdc, F.A.2    Bechara, E.J.H.3
  • 47
    • 0030799468 scopus 로고    scopus 로고
    • Acute intermittent porphyria: Prevalence of mutations in the porphobilinogen deaminase gene in blood donors in France
    • Y Nordmann H Puy V Da Silva Acute intermittent porphyria: prevalence of mutations in the porphobilinogen deaminase gene in blood donors in France. Journal of Internal Medicine 242 3 1997 213 217
    • (1997) Journal of Internal Medicine , vol.242 , Issue.3 , pp. 213-217
    • Nordmann, Y.1    Puy, H.2    Da Silva, V.3
  • 48
    • 4444302117 scopus 로고    scopus 로고
    • Molecular genetics of late-onset Alzheimer's disease
    • ikamboh@hgen.pitt.edu
    • M I Kamboh ikamboh@hgen.pitt.edu Molecular genetics of late-onset Alzheimer's disease. Annals of Human Genetics 68 4 2004 381 404
    • (2004) Annals of Human Genetics , vol.68 , Issue.4 , pp. 381-404
    • Kamboh, M.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.