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Volumn 10, Issue 2, 1999, Pages 123-131

Molecular genetics of the Smith-Lemli-Opitz syndrome and postsqualene sterol metabolism

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL;

EID: 0032892291     PISSN: 09579672     EISSN: None     Source Type: Journal    
DOI: 10.1097/00041433-199904000-00006     Document Type: Review
Times cited : (31)

References (69)
  • 1
    • 0031592431 scopus 로고    scopus 로고
    • A new face for an old syndrome
    • Kelley RI. A new face for an old syndrome. Am J Med Genet 1997, 68:251-256
    • (1997) Am J Med Genet , vol.68 , pp. 251-256
    • Kelley, R.I.1
  • 2
    • 0344301951 scopus 로고    scopus 로고
    • Cholesterol metabolism and morphogenesis
    • Farese RV, Herz J Cholesterol metabolism and morphogenesis. Trends Genet 1998; 14:115-120.
    • (1998) Trends Genet , vol.14 , pp. 115-120
    • Farese, R.V.1    Herz, J.2
  • 3
    • 0032493196 scopus 로고    scopus 로고
    • Mutations in the Δ7-sterol reductase gene in patients with the Smith-Lemli-Opitz syndrome
    • Fitzky BU, Witsch-Baumgartner M, Erdel M, Lee JN, Paik Y-K, Glossmann H, et al. Mutations in the Δ7-sterol reductase gene in patients with the Smith-Lemli-Opitz syndrome. Proc Natl Acad Sci USA 1998; 95 8181-8186. This compelling study describes the structure and localization of the human and murine DHCR7 genes on chromosomal regions 11q13 and 7F5, respectively. It is the first study that identifies mutations therein at the genomic level in 13 patients demonstrating that the V326L and the IVS8-1G>C mutations are recurrent A total of 13 mutations is identified. The heredity of mutations in SLOS families is shown and the functional consequences of five missense mutations are investigated which intriguingly all reduce protein expression.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8181-8186
    • Fitzky, B.U.1    Witsch-Baumgartner, M.2    Erdel, M.3    Lee, J.N.4    Paik, Y.-K.5    Glossmann, H.6
  • 4
    • 0000139419 scopus 로고
    • A newly recognized syndrome of multiple congenital anomalies
    • Smith DW, Lemli L, Opitz JM. A newly recognized syndrome of multiple congenital anomalies. J Pediatr 1964; 64:210-217.
    • (1964) J Pediatr , vol.64 , pp. 210-217
    • Smith, D.W.1    Lemli, L.2    Opitz, J.M.3
  • 5
    • 0023253263 scopus 로고
    • Smith-Lemli-Opitz sydrome-type II. multiple congenital anomalies with male pseudohermaphroditism and frequent early lethality
    • Curry CJR, Carey JC, Holland JS, Chopra D, Finemn R, Golabi M, et al. Smith-Lemli-Opitz sydrome-type II. multiple congenital anomalies with male pseudohermaphroditism and frequent early lethality. Am J Med Genet 1987; 26:45-57.
    • (1987) Am J Med Genet , vol.26 , pp. 45-57
    • Curry, C.J.R.1    Carey, J.C.2    Holland, J.S.3    Chopra, D.4    Finemn, R.5    Golabi, M.6
  • 6
    • 0018963505 scopus 로고
    • Borderline normal intelligence in the Smith-Lemli-Opitz (RSH) syndrome
    • Lowry RB, Yong SL. Borderline normal intelligence in the Smith-Lemli-Opitz (RSH) syndrome Am J Med Genet 1980, 5:137-143.
    • (1980) Am J Med Genet , vol.5 , pp. 137-143
    • Lowry, R.B.1    Yong, S.L.2
  • 7
    • 0031812755 scopus 로고    scopus 로고
    • Smith-Lemli-Opitz syndrome: A variable clinical and biochemical phenotype
    • Ryan AK, Bartlett K, Clayton P, Eaton S, Mills K, Donnai D, et al Smith-Lemli-Opitz syndrome: a variable clinical and biochemical phenotype. Am J Med Genet 1998; 35:558-565. An interesting overview on the clinical phenotype of a large number of English patients and an attempt to estimate the incidence of the SLOS (>1 in 60 000 newborns).
    • (1998) Am J Med Genet , vol.35 , pp. 558-565
    • Ryan, A.K.1    Bartlett, K.2    Clayton, P.3    Eaton, S.4    Mills, K.5    Donnai, D.6
  • 10
    • 0028884255 scopus 로고
    • Markedly inhibited 7-dehydrocholesterol-Δ7-reductase activity in liver microsomes from Smith-Lemli-Opitz homozygotes
    • Shefer S, Salen G, Batta AK, Honda A, Tint GS, Irons M, et al. Markedly inhibited 7-dehydrocholesterol-Δ7-reductase activity in liver microsomes from Smith-Lemli-Opitz homozygotes. J Clin Invest 1995; 96.1779-1785.
    • (1995) J Clin Invest , vol.96 , pp. 1779-1785
    • Shefer, S.1    Salen, G.2    Batta, A.K.3    Honda, A.4    Tint, G.S.5    Irons, M.6
  • 11
    • 12644267305 scopus 로고    scopus 로고
    • Rapid identification of Smith-Lemli-Opitz homozygotes and heterozygotes (carriers) by measurement of deficient 7-dehydrocholesterol-Δ7-reductase activity in fibroblasts
    • Shefer S, Salen G, Honda A, Batta A, Hauser S, Tint GS, et al. Rapid identification of Smith-Lemli-Opitz homozygotes and heterozygotes (carriers) by measurement of deficient 7-dehydrocholesterol-Δ7-reductase activity in fibroblasts. Metabolism 1997; 46:844-850.
    • (1997) Metabolism , vol.46 , pp. 844-850
    • Shefer, S.1    Salen, G.2    Honda, A.3    Batta, A.4    Hauser, S.5    Tint, G.S.6
  • 12
    • 0032539605 scopus 로고    scopus 로고
    • Molecular cloning and expression of the human Δ7-sterol reductase
    • Moebius FF, Fitzky BU, Lee JN, Paik Y-K, Glossmann H. Molecular cloning and expression of the human Δ7-sterol reductase. Proc Natl Acad Sci USA 1998, 95:1899-1902. First report of the cloning and functional expression of the human DHCR7 cDNA and tentative chromosomal assignment to 11q13. The mRNA for the 55kDa protein is ubiquitously expressed and abundant in the adult brain.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1899-1902
    • Moebius, F.F.1    Fitzky, B.U.2    Lee, J.N.3    Paik, Y.-K.4    Glossmann, H.5
  • 13
    • 0032231459 scopus 로고    scopus 로고
    • Mutations in the human sterol Δ7-reductase gene at 11q12-13 cause Smith-Lemli-Opitz syndrome
    • Wassif CA, Maslen C, Kachilele-Linjewile S, Lin D, Linck, Connor WE, et al. Mutations in the human sterol Δ7-reductase gene at 11q12-13 cause Smith-Lemli-Opitz syndrome. Am J Hum Genet 1998; 63:55-62 This study reports complementation of the DHCR7 deficiency by a partial cDNA clone, identification of mutations in cDNA from three patients and the chromosomal assignment to 11q13. The designation of mutant nucleotides and amino acid residues needs revision because of the partial cDNA sequence (5′ coding and non-coding sequence missing).
    • (1998) Am J Hum Genet , vol.63 , pp. 55-62
    • Wassif, C.A.1    Maslen, C.2    Kachilele-Linjewile, S.3    Lin, D.4    Linck5    Connor, W.E.6
  • 14
    • 0032231706 scopus 로고    scopus 로고
    • Smith-Lemli-Opitz syndrome is caused by mutations in the 7-dehydrocholesterol reductase gene
    • Waterham HR, Wijburg FA, Hennekam RC, Vreken P, Poll-The BT, Dorland L, et al. Smith-Lemli-Opitz syndrome is caused by mutations in the 7-dehydrocholesterol reductase gene. Am J Hum Genet 1998; 63:329-338. This flawless investigation reports the cloning and functional expression in yeast of a human DHCR7 cDNA, mutations therein in three patients and their parents and chromosomal assignment to 11q13.
    • (1998) Am J Hum Genet , vol.63 , pp. 329-338
    • Waterham, H.R.1    Wijburg, F.A.2    Hennekam, R.C.3    Vreken, P.4    Poll-The, B.T.5    Dorland, L.6
  • 15
    • 0023681436 scopus 로고
    • Biosynthesis of cholesterol in the yeast mutant erg6
    • Xu SH, Nes WD. Biosynthesis of cholesterol in the yeast mutant erg6. Biochem Biophys Res Communication 1988, 155.509-517.
    • (1988) Biochem Biophys Res Communication , vol.155 , pp. 509-517
    • Xu, S.H.1    Nes, W.D.2
  • 18
    • 0028920880 scopus 로고
    • Cholesterol biosynthesis from lanosterol: Regulation and purification of rat hepatic sterol 8-isomerase
    • Kang MK, Kim CK, Johng TN, Paik YK. Cholesterol biosynthesis from lanosterol: regulation and purification of rat hepatic sterol 8-isomerase. J Biochem 1995; 117:819-823.
    • (1995) J Biochem , vol.117 , pp. 819-823
    • Kang, M.K.1    Kim, C.K.2    Johng, T.N.3    Paik, Y.K.4
  • 21
    • 9544223310 scopus 로고    scopus 로고
    • Emopamil-binding protein, a mammalian protein that binds a series of structurally diverse neuroprofective agents, exhibits δ8-δ7 isomerase activity in yeast
    • Silve S, Dupuy PH, Labit-Lebouteiller C, Kaghad M, Chalon P, Rahier A, et al Emopamil-binding protein, a mammalian protein that binds a series of structurally diverse neuroprofective agents, exhibits δ8-δ7 isomerase activity in yeast J Biol Chem 1996; 271:22434-22440.
    • (1996) J Biol Chem , vol.271 , pp. 22434-22440
    • Silve, S.1    Dupuy, P.H.2    Labit-Lebouteiller, C.3    Kaghad, M.4    Chalon, P.5    Rahier, A.6
  • 22
    • 0014771854 scopus 로고
    • The stereochemistry of hydrogen elimination from C-7 in cholesterol and ergosterol biosynthesis
    • Akhtar M, Rahimtula AD, Wilton DC The stereochemistry of hydrogen elimination from C-7 in cholesterol and ergosterol biosynthesis. Biochem J 1970, 117:539-542.
    • (1970) Biochem J , vol.117 , pp. 539-542
    • Akhtar, M.1    Rahimtula, A.D.2    Wilton, D.C.3
  • 23
    • 0028906887 scopus 로고
    • Cloning of the late genes in the ergosterol biosynthetic pathway of saccharomyces cerevisiae-a review
    • Lees ND, Skaggs B, Kirsch DR, Bard M. Cloning of the late genes in the ergosterol biosynthetic pathway of saccharomyces cerevisiae-a review. Lipids 1995, 30:221-226
    • (1995) Lipids , vol.30 , pp. 221-226
    • Lees, N.D.1    Skaggs, B.2    Kirsch, D.R.3    Bard, M.4
  • 24
    • 0030033387 scopus 로고    scopus 로고
    • Cloning and characterization of ERG25, the Saccharomyces cerevisiae gene encoding C-4 sterol methyl oxidase
    • Bard M, Bruner DA, Pierson CA, Lees ND, Biermann B, Frye L, et al. Cloning and characterization of ERG25, the Saccharomyces cerevisiae gene encoding C-4 sterol methyl oxidase Proc Natl Acad Sci USA 1996; 93:186-190
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 186-190
    • Bard, M.1    Bruner, D.A.2    Pierson, C.A.3    Lees, N.D.4    Biermann, B.5    Frye, L.6
  • 25
    • 0029967548 scopus 로고    scopus 로고
    • Cloning and characterization of the Saccharomyces cerevisiae C-22 sterol desaturase gene, encoding a second cytochrome P-450 involved in ergosterol biosynthesis
    • Skaggs BA, Alexander JF, Pierson CA, Schweitzer KS, Chun KT, Koegel C, et al. Cloning and characterization of the Saccharomyces cerevisiae C-22 sterol desaturase gene, encoding a second cytochrome P-450 involved in ergosterol biosynthesis. Gene 1996, 169:105-109.
    • (1996) Gene , vol.169 , pp. 105-109
    • Skaggs, B.A.1    Alexander, J.F.2    Pierson, C.A.3    Schweitzer, K.S.4    Chun, K.T.5    Koegel, C.6
  • 26
    • 0030014654 scopus 로고    scopus 로고
    • Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue
    • Li L, Kaplan J. Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue. J Biol Chem 1996; 271:16927-16933.
    • (1996) J Biol Chem , vol.271 , pp. 16927-16933
    • Li, L.1    Kaplan, J.2
  • 27
    • 0029851321 scopus 로고    scopus 로고
    • Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase
    • Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y. Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet 1996; 74.252-254.
    • (1996) Cytogenet Cell Genet , vol.74 , pp. 252-254
    • Matsushima, M.1    Inazawa, J.2    Takahashi, E.3    Suzumori, K.4    Nakamura, Y.5
  • 29
    • 0023655537 scopus 로고
    • Subcellular localization of the enzymes of cholesterol biosynthesis and metabolism in rat liver
    • Reinhart MP, Billheimer JT, Faust JR, Gaylor JL Subcellular localization of the enzymes of cholesterol biosynthesis and metabolism in rat liver. J Biol Chem 1987; 262:9649-9655.
    • (1987) J Biol Chem , vol.262 , pp. 9649-9655
    • Reinhart, M.P.1    Billheimer, J.T.2    Faust, J.R.3    Gaylor, J.L.4
  • 30
    • 0031931498 scopus 로고    scopus 로고
    • Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles
    • Leber R, Landl K, Zinser E, Ahorn H, Spok A, Kohlwein SD, et al. Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles Mol Biol Cell 1998; 9.375-386.
    • (1998) Mol Biol Cell , vol.9 , pp. 375-386
    • Leber, R.1    Landl, K.2    Zinser, E.3    Ahorn, H.4    Spok, A.5    Kohlwein, S.D.6
  • 31
    • 0031876967 scopus 로고    scopus 로고
    • Variant RSH/Smith-Lemli-Opitz syndrome with atypical sterol metabolism
    • Anderson AJ, Stephan MJ, Walker WO, Kelley RI. Variant RSH/Smith-Lemli-Opitz syndrome with atypical sterol metabolism. Am J Med Genet 1998; 78:413-418.
    • (1998) Am J Med Genet , vol.78 , pp. 413-418
    • Anderson, A.J.1    Stephan, M.J.2    Walker, W.O.3    Kelley, R.I.4
  • 33
    • 0014249673 scopus 로고
    • The biological conversion of 7-dehydrocholesterol into cholesterol and comments on the reduction of double bonds
    • Wilton DC, Munday KA, Skinner SH, Akhtar M. The biological conversion of 7-dehydrocholesterol into cholesterol and comments on the reduction of double bonds. Biochem J 1968; 106.803-810.
    • (1968) Biochem J , vol.106 , pp. 803-810
    • Wilton, D.C.1    Munday, K.A.2    Skinner, S.H.3    Akhtar, M.4
  • 34
    • 17544366424 scopus 로고    scopus 로고
    • Cloning by metabolic interference in yeast and enzymatic characterization of Arabidopsis thaliana sterol A7-reductase
    • Lecain E, Chenivesse X, Spagnoli R, Pompon D. Cloning by metabolic interference in yeast and enzymatic characterization of Arabidopsis thaliana sterol A7-reductase. J Biol Chem 1996; 271.10866-10873.
    • (1996) J Biol Chem , vol.271 , pp. 10866-10873
    • Lecain, E.1    Chenivesse, X.2    Spagnoli, R.3    Pompon, D.4
  • 36
    • 0030949390 scopus 로고    scopus 로고
    • The mysteries of σ-receptors: New family members reveal a role in cholesterol synthesis
    • Moebius FF, Striessnig J, Glossmann H The mysteries of σ-receptors: new family members reveal a role in cholesterol synthesis. Trends Pharmacol Sci 1997; 18:67-70
    • (1997) Trends Pharmacol Sci , vol.18 , pp. 67-70
    • Moebius, F.F.1    Striessnig, J.2    Glossmann, H.3
  • 37
    • 0028363978 scopus 로고
    • Primary structure analysis and lamin B and DNA binding of human LBR, an integral membrane protein of the nuclear envelope inner membrane
    • Ye Q, Worman HJ. Primary structure analysis and lamin B and DNA binding of human LBR, an integral membrane protein of the nuclear envelope inner membrane. J Biol Chem 1994; 269:11306-11311.
    • (1994) J Biol Chem , vol.269 , pp. 11306-11311
    • Ye, Q.1    Worman, H.J.2
  • 38
    • 0027500249 scopus 로고
    • The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • Soullam B, Worman HJ. The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal. J Cell Biol 1993; 120:1093-1100.
    • (1993) J Cell Biol , vol.120 , pp. 1093-1100
    • Soullam, B.1    Worman, H.J.2
  • 39
    • 0030942845 scopus 로고    scopus 로고
    • Mitotic phosphorylation of the lamin B receptor by a serine/arginine kinase and p34 (cdc2)
    • Nikolakaki E, Meier J, Simos G, Georgatos SD, Giannakouros T. Mitotic phosphorylation of the lamin B receptor by a serine/arginine kinase and p34 (cdc2). J Biol Chem 1997; 272.6208-6213.
    • (1997) J Biol Chem , vol.272 , pp. 6208-6213
    • Nikolakaki, E.1    Meier, J.2    Simos, G.3    Georgatos, S.D.4    Giannakouros, T.5
  • 40
    • 0031798822 scopus 로고    scopus 로고
    • LBR, a chromatin and lamin binding protein from the inner nuclear membrane, is proteolyzed at late stages of apoptosis
    • Duband-Goulet I, Courvalin JC, Buendia B, LBR, a chromatin and lamin binding protein from the inner nuclear membrane, is proteolyzed at late stages of apoptosis J Cell Sci 1998; 111:1441-1451.
    • (1998) J Cell Sci , vol.111 , pp. 1441-1451
    • Duband-Goulet, I.1    Courvalin, J.C.2    Buendia, B.3
  • 41
    • 0028237891 scopus 로고
    • Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane
    • Schuler E, Lin F, Worman HJ. Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane. J Biol Chem 1994; 269:11312-11317.
    • (1994) J Biol Chem , vol.269 , pp. 11312-11317
    • Schuler, E.1    Lin, F.2    Worman, H.J.3
  • 42
    • 0031834439 scopus 로고    scopus 로고
    • Identification and molecular characterization of TM7SF2 in the FAUNA gene cluster on human chromosome 11q13
    • Lemmens IH, Kas K, Merregaert J, Van de Ven WJ. Identification and molecular characterization of TM7SF2 in the FAUNA gene cluster on human chromosome 11q13. Genomics 1998; 49:437-442.
    • (1998) Genomics , vol.49 , pp. 437-442
    • Lemmens, I.H.1    Kas, K.2    Merregaert, J.3    Van De Ven, W.J.4
  • 43
    • 0032535470 scopus 로고    scopus 로고
    • The human lamin B receptor/sterol reductase multigene family
    • Holmer L, Pezhman A, Worman HJ. The human lamin B receptor/sterol reductase multigene family Genomics 1998; 54:469-476.
    • (1998) Genomics , vol.54 , pp. 469-476
    • Holmer, L.1    Pezhman, A.2    Worman, H.J.3
  • 44
    • 0031838013 scopus 로고    scopus 로고
    • 14-reductase activity in Saccharomyces cerevisiae
    • 14-reductase activity in Saccharomyces cerevisiae. Biochim Biophys Acta 1998; 1392:233-244. An important finding is the demonstration of Δ14-sterol reductase activity of the lamin B receptor in yeast by complementation of an erg24 (Δ14-sterol reductase) mutant strain.
    • (1998) Biochim Biophys Acta , vol.1392 , pp. 233-244
    • Silve, S.1    Dupuy, P.H.2    Ferrara, P.3    Loison, G.4
  • 45
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphass and mitosis
    • Ellenberg J, Siggia ED, Moreira JE, Smith CL, Presley JF, Worman HJ, Lippincott-Schwartz J. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphass and mitosis J Cell Biol 1998; 138:1193-1206.
    • (1998) J Cell Biol , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippincott-Schwartz, J.7
  • 47
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway regulation of cholesterol metabolism by proteolysis of a membrane bound transcription factor
    • Brown MS, Goldstein JL. The SREBP pathway regulation of cholesterol metabolism by proteolysis of a membrane bound transcription factor. Cell 1997; 89:331-340.
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 48
    • 0032572729 scopus 로고    scopus 로고
    • Cholesterol homeostasis: A role for oxysterols
    • Accad M, Farese RV Jr. Cholesterol homeostasis: a role for oxysterols. Curr Biol 1998; 8.R601-R604
    • (1998) Curr Biol , vol.8
    • Accad, M.1    Farese Jr., R.V.2
  • 49
    • 0031919848 scopus 로고    scopus 로고
    • 7-Dehydrocholesterol down-regulates cholesterol biosynthesis in cultured Smith-Lemli-Opitz syndrome skin fibroblasts
    • Honda M, Tint GS, Honda A, Nguyen LB, Chen TS, Shefer S. 7-Dehydrocholesterol down-regulates cholesterol biosynthesis in cultured Smith-Lemli-Opitz syndrome skin fibroblasts. J Lipid Res 1998; 39:647-657.
    • (1998) J Lipid Res , vol.39 , pp. 647-657
    • Honda, M.1    Tint, G.S.2    Honda, A.3    Nguyen, L.B.4    Chen, T.S.5    Shefer, S.6
  • 50
    • 0020824881 scopus 로고
    • Structural and physiological features of sterols necessary to satisfy bulk membrane and sparking requirements in yeast sterol auxotrophs
    • Rodriguez RJ, Parks LW. Structural and physiological features of sterols necessary to satisfy bulk membrane and sparking requirements in yeast sterol auxotrophs Arch Biochem Biophys 1983; 225:861-871
    • (1983) Arch Biochem Biophys , vol.225 , pp. 861-871
    • Rodriguez, R.J.1    Parks, L.W.2
  • 51
    • 0030770249 scopus 로고    scopus 로고
    • Assessment of the essentiality of ERG genes late in ergosterol biosynthesis in Saccharomyces cerevisiae
    • Palermo LM, Leak FW, Tove S, Parks LW. Assessment of the essentiality of ERG genes late in ergosterol biosynthesis in Saccharomyces cerevisiae. Curr Genet 1997; 32:93-99.
    • (1997) Curr Genet , vol.32 , pp. 93-99
    • Palermo, L.M.1    Leak, F.W.2    Tove, S.3    Parks, L.W.4
  • 52
    • 0031899024 scopus 로고    scopus 로고
    • Related membrane domains in proteins of sterol sensing and cell signaling provide a glimpse of treasures still buried within the dynamic realm of intracellular metabolic regulation
    • Osborne TF, Rosenfeld JM. Related membrane domains in proteins of sterol sensing and cell signaling provide a glimpse of treasures still buried within the dynamic realm of intracellular metabolic regulation. Curr Opin Lipidol 1998; 9:137-140.
    • (1998) Curr Opin Lipidol , vol.9 , pp. 137-140
    • Osborne, T.F.1    Rosenfeld, J.M.2
  • 53
    • 0030458446 scopus 로고    scopus 로고
    • Holoprosencephaly in RSH/Smith-Lemli-Opitz syndrome, does abnormal cholesterol metabolism affect the function of sonic hedgehog
    • Kelley RI, Roessler E, Hennekam RCM, Feldman GL, Kosaki K, Jones MC, et al. Holoprosencephaly in RSH/Smith-Lemli-Opitz syndrome, does abnormal cholesterol metabolism affect the function of sonic hedgehog. Am J Med Genet 1996, 66:478-484.
    • (1996) Am J Med Genet , vol.66 , pp. 478-484
    • Kelley, R.I.1    Roessler, E.2    Hennekam, R.C.M.3    Feldman, G.L.4    Kosaki, K.5    Jones, M.C.6
  • 55
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of hedgehog signaling proteins in animal development
    • Porter JA, Young KE, Beachy PA Cholesterol modification of hedgehog signaling proteins in animal development. Science 1996; 274:255-259.
    • (1996) Science , vol.274 , pp. 255-259
    • Porter, J.A.1    Young, K.E.2    Beachy, P.A.3
  • 56
    • 0032486433 scopus 로고    scopus 로고
    • Teratogen-mediated inhibition of target tissue response to Shh signaling
    • Cooper MK, Porter JA, Young KE, Beachy PA. Teratogen-mediated inhibition of target tissue response to Shh signaling. Science 1998; 280.1603-1607. Evidence is presented that autocatalytic modification of SHH with sterols does not depend critically on sterol structure. Signalling activity of recombinant SHH in chicken embryos is inhibited by jervine and other teratogenes. Evidence that demonstrates that jervine has no effect on sterol metabolism is missing but could have established that jervine acts on intracellular sterol transport or SHH signalling.
    • (1998) Science , vol.280 , pp. 1603-1607
    • Cooper, M.K.1    Porter, J.A.2    Young, K.E.3    Beachy, P.A.4
  • 57
    • 0031916823 scopus 로고    scopus 로고
    • Regional distribution of Sonic Hedgehog, patched, and smoothened mRNA in the adult rat brain
    • Traiffort E, Charytoniuk DA, Faure H, Ruat M. Regional distribution of Sonic Hedgehog, patched, and smoothened mRNA in the adult rat brain. J Neurochem 1998, 70:1327-1330.
    • (1998) J Neurochem , vol.70 , pp. 1327-1330
    • Traiffort, E.1    Charytoniuk, D.A.2    Faure, H.3    Ruat, M.4
  • 58
    • 0029938854 scopus 로고    scopus 로고
    • Origin of cholesterol in the fetal golden Syrian hamster: Contribution of de novo sterol synthesis and maternal-derived lipoprotein cholesterol
    • Woollett LA. Origin of cholesterol in the fetal golden Syrian hamster: contribution of de novo sterol synthesis and maternal-derived lipoprotein cholesterol. J Lipid Res 1996; 37:1246-1257.
    • (1996) J Lipid Res , vol.37 , pp. 1246-1257
    • Woollett, L.A.1
  • 59
    • 0030957561 scopus 로고    scopus 로고
    • Sources of cholesterol during development of the rat fetus and fetal organs
    • Jurevics HA, Kidwai FZ, Morell P. Sources of cholesterol during development of the rat fetus and fetal organs. J Lipid Res 1997; 38:723-733.
    • (1997) J Lipid Res , vol.38 , pp. 723-733
    • Jurevics, H.A.1    Kidwai, F.Z.2    Morell, P.3
  • 60
    • 0029795699 scopus 로고    scopus 로고
    • Brain does not utilize low density lipoprotein-cholesterol during fetal and neonatal development in the sheep
    • Turley SD, Burns DK, Rosenfeld CR, Dietschy JM. Brain does not utilize low density lipoprotein-cholesterol during fetal and neonatal development in the sheep. J Lipid Res 1996; 37:1953-1961.
    • (1996) J Lipid Res , vol.37 , pp. 1953-1961
    • Turley, S.D.1    Burns, D.K.2    Rosenfeld, C.R.3    Dietschy, J.M.4
  • 61
    • 0028896702 scopus 로고
    • Markedly increased tissue concentrations of 7-dehydrocholesterol combined with low levels of cholesterol are characteristic of the Smith-Lemli-Opitz syndrome
    • Tint GS, Seller M, Hughes-Benzie R, Batta AK, Shefer S, Genest D, et al. Markedly increased tissue concentrations of 7-dehydrocholesterol combined with low levels of cholesterol are characteristic of the Smith-Lemli-Opitz syndrome. J Lipid Res 1995; 36.89-95.
    • (1995) J Lipid Res , vol.36 , pp. 89-95
    • Tint, G.S.1    Seller, M.2    Hughes-Benzie, R.3    Batta, A.K.4    Shefer, S.5    Genest, D.6
  • 62
    • 0031043289 scopus 로고    scopus 로고
    • Smith-Lemli-Opitz syndrome: 30-year follow-up of 'S' of 'RSH' syndrome
    • Pauli RW, Williams MS, Josephson KD, Tint GS. Smith-Lemli-Opitz syndrome: 30-year follow-up of 'S' of 'RSH' syndrome. Am J Med Genet 1997; 68:260-262.
    • (1997) Am J Med Genet , vol.68 , pp. 260-262
    • Pauli, R.W.1    Williams, M.S.2    Josephson, K.D.3    Tint, G.S.4
  • 64
    • 0031810073 scopus 로고    scopus 로고
    • Relationship between abnormal cholesterol synthesis and retarded learning in rats
    • Xu G, Servatius RJ, Shefer S, Tint GS, OBrien WT, Batta AK, Salen G. Relationship between abnormal cholesterol synthesis and retarded learning in rats. Metabolism 1998; 47:878-882. Impaired learning in rats treated with the DHCR7 inhibitor BM15766 provides the first evidence that sterol depletion impairs cognitive brain functions.
    • (1998) Metabolism , vol.47 , pp. 878-882
    • Xu, G.1    Servatius, R.J.2    Shefer, S.3    Tint, G.S.4    Obrien, W.T.5    Batta, A.K.6    Salen, G.7
  • 65
    • 0029835410 scopus 로고    scopus 로고
    • Cholesterol homeostasis in human brain: Evidence for an age-dependent flux of 24S-hydroxycholesterol from the brain into the circulation
    • Lutiohann D, Breuer O, Ahlborg G, Nennesmo I, Siden A, Diczfalusy U, Bjorkhem I Cholesterol homeostasis in human brain: evidence for an age-dependent flux of 24S-hydroxycholesterol from the brain into the circulation. Proc Natl Acad Sci USA 1996; 93 9799-9804.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9799-9804
    • Lutiohann, D.1    Breuer, O.2    Ahlborg, G.3    Nennesmo, I.4    Siden, A.5    Diczfalusy, U.6    Bjorkhem, I.7
  • 67
    • 0027478167 scopus 로고
    • Targeted modification of the apolipoprotein B gene results in hypobetalipoproteinemia and developmental anomalities in mice
    • Homanics GE, Smith TJ, Zhang SH, Lee D, Young SG, Maeda N Targeted modification of the apolipoprotein B gene results in hypobetalipoproteinemia and developmental anomalities in mice. Proc Natl Acad Sci USA 1993; 90:2389-2393.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2389-2393
    • Homanics, G.E.1    Smith, T.J.2    Zhang, S.H.3    Lee, D.4    Young, S.G.5    Maeda, N.6
  • 69
    • 0028229223 scopus 로고
    • The origin of the major cystic fibrosis mutation (ΔF508) in European populations
    • Morral N, Bertranpetit J, Estivill X, Nunes V, Casals T, Gimenez J, et al. The origin of the major cystic fibrosis mutation (ΔF508) in European populations. Nat Genet 1994; 7:169-175.
    • (1994) Nat Genet , vol.7 , pp. 169-175
    • Morral, N.1    Bertranpetit, J.2    Estivill, X.3    Nunes, V.4    Casals, T.5    Gimenez, J.6


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