메뉴 건너뛰기




Volumn 71, Issue 1, 1998, Pages 323-329

Enzymatic and molecular biological analysis of palmitoyl protein thioesterase deficiency in infantile neuronal ceroid lipofuscinosis

Author keywords

Brain; Lymphoblasts; Lysosomal enzyme; mRNA; Palmitoyl protein thioesterase

Indexed keywords

BETA N ACETYLHEXOSAMINIDASE; GLYCOPROTEIN; LYSOSOME ENZYME; OCTAPEPTIDE; PALMITIC ACID; PALMITOYL COENZYME A; PALMITOYL PROTEIN THIOESTERASE; SYNTHETIC PEPTIDE; THIOL ESTER HYDROLASE; UNCLASSIFIED DRUG;

EID: 0031866280     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.71010323.x     Document Type: Article
Times cited : (20)

References (26)
  • 1
    • 0020585939 scopus 로고
    • 0 protein, the major intrinsic protein of rat sciatic nerve myelin
    • 0 protein, the major intrinsic protein of rat sciatic nerve myelin. J. Biol. Chem. 258, 6556-6560.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6556-6560
    • Agrawal, H.C.1    Schmidt, R.E.2    Agrawal, D.3
  • 2
    • 0028980377 scopus 로고
    • 0 glycoprotein and a synthetic peptide containing the palmitoylation site are both autoacylated
    • 0 glycoprotein and a synthetic peptide containing the palmitoylation site are both autoacylated. J. Neurochem. 65, 1805-1815.
    • (1995) J. Neurochem. , vol.65 , pp. 1805-1815
    • Bharadwaj, M.1    Bizzozero, O.A.2
  • 3
    • 0030788654 scopus 로고    scopus 로고
    • The molecular and functional role of protein palmitoylation in the nervous system
    • Bizzozero O. A. (1997) The molecular and functional role of protein palmitoylation in the nervous system. Neuropediatrics 28, 23-26.
    • (1997) Neuropediatrics , vol.28 , pp. 23-26
    • Bizzozero, O.A.1
  • 6
    • 0027518208 scopus 로고
    • Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras
    • Camp L. A. and Hofmann S. L. (1993) Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras. J. Biol. Chem. 268, 22566-22574.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22566-22574
    • Camp, L.A.1    Hofmann, S.L.2
  • 7
    • 0023617348 scopus 로고
    • Apparent cathepsin B deficiency in neuronal ceroid lipofuscinosis can be explained by peroxide inhibition
    • Dawson G. and Glaser P. (1987) Apparent cathepsin B deficiency in neuronal ceroid lipofuscinosis can be explained by peroxide inhibition. Biochem. Biophys. Res. Commun. 147, 267-274.
    • (1987) Biochem. Biophys. Res. Commun. , vol.147 , pp. 267-274
    • Dawson, G.1    Glaser, P.2
  • 8
    • 0030874171 scopus 로고    scopus 로고
    • Low molecular weight storage material in infantile ceroid-lipofuscinosis (CLN1)
    • Dawson G., Cho S., Siakotos A. N., and Kilkus J. (1997) Low molecular weight storage material in infantile ceroid-lipofuscinosis (CLN1). Neuropediatrics 28, 31-32.
    • (1997) Neuropediatrics , vol.28 , pp. 31-32
    • Dawson, G.1    Cho, S.2    Siakotos, A.N.3    Kilkus, J.4
  • 9
    • 0015609956 scopus 로고
    • Protein composition of myelin of the peripheral nerve system
    • Greenfield S., Brostoff S., Eylar E. H., and Morell P. (1973) Protein composition of myelin of the peripheral nerve system. J. Neurochem. 20, 1207-1216.
    • (1973) J. Neurochem. , vol.20 , pp. 1207-1216
    • Greenfield, S.1    Brostoff, S.2    Eylar, E.H.3    Morell, P.4
  • 10
    • 0015596171 scopus 로고
    • Infantile type of so-called neuronal ceroid-lipofuscinosis. Part II. Morphological and biochemical studies
    • Haltia M., Rapola L., Santavuori P., and Keranen A. (1973) Infantile type of so-called neuronal ceroid-lipofuscinosis. Part II. Morphological and biochemical studies. J. Neurol. Sci. 18, 269-285.
    • (1973) J. Neurol. Sci. , vol.18 , pp. 269-285
    • Haltia, M.1    Rapola, L.2    Santavuori, P.3    Keranen, A.4
  • 11
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock J. F., Magee A. I., Childs J. E., and Marshall C. J. (1989) All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57, 1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 12
    • 0029843717 scopus 로고    scopus 로고
    • Human palmitoyl protein thioesterase: Evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis
    • Hellsten E., Vesa J., Olkkonen V. M., Jalanko A., and Peltonen L. (1996) Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis. EMBO J. 15, 5240-5245.
    • (1996) EMBO J. , vol.15 , pp. 5240-5245
    • Hellsten, E.1    Vesa, J.2    Olkkonen, V.M.3    Jalanko, A.4    Peltonen, L.5
  • 13
    • 0030739514 scopus 로고    scopus 로고
    • Palmitoyl-protein thioesterase and the molecular pathogenesis of infantile neuronal ceroid lipofuscinosis
    • Hofmann S. L., Lee L. A., Lu J.-Y., and Verkruyse L. A. (1997) Palmitoyl-protein thioesterase and the molecular pathogenesis of infantile neuronal ceroid lipofuscinosis. Neuropediatrics 28, 27-30.
    • (1997) Neuropediatrics , vol.28 , pp. 27-30
    • Hofmann, S.L.1    Lee, L.A.2    Lu, J.-Y.3    Verkruyse, L.A.4
  • 14
    • 0019827370 scopus 로고
    • Caprine β-mannosidase
    • Jones M. Z. and Dawson G. (1981) Caprine β-mannosidase. J. Biol. Chem. 256, 5185-5188.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5185-5188
    • Jones, M.Z.1    Dawson, G.2
  • 15
    • 0015589883 scopus 로고
    • On the significance of curvilinear bodies in late infantile lipidosis
    • Lenn N. J. and Dawson G. (1973) On the significance of curvilinear bodies in late infantile lipidosis. Am. J. Ment. Defic. 77, 597-606.
    • (1973) Am. J. Ment. Defic. , vol.77 , pp. 597-606
    • Lenn, N.J.1    Dawson, G.2
  • 17
    • 2642666428 scopus 로고
    • Ceramidase deficiency: Farber's lipogranulomatosis
    • Stanbury J. B., Wyngaarden J. B., and Fredrickson D. S., eds. McGraw-Hill, New York
    • Moser H. W. (1978) Ceramidase deficiency: Farber's lipogranulomatosis, in the Metabolic Basis of Inherited Disease (Stanbury J. B., Wyngaarden J. B., and Fredrickson D. S., eds), pp. 707-717. McGraw-Hill, New York.
    • (1978) Metabolic Basis of Inherited Disease , pp. 707-717
    • Moser, H.W.1
  • 20
    • 0026688088 scopus 로고
    • Characterization of a cell line derived from a human oligodendrocyte
    • Post G. R. and Dawson G. (1992) Characterization of a cell line derived from a human oligodendrocyte. Mol. Chem. Neuropathol. 16, 303-317.
    • (1992) Mol. Chem. Neuropathol. , vol.16 , pp. 303-317
    • Post, G.R.1    Dawson, G.2
  • 21
    • 0023645640 scopus 로고
    • Palmitoylation, sulfation and glycosylation of the α-subunit of the sodium channel: Role of post-translational modification in channel assembly
    • Schmidt J. W. and Catterall W. A. (1987) Palmitoylation, sulfation and glycosylation of the α-subunit of the sodium channel: role of post-translational modification in channel assembly. J. Biol. Chem. 262, 13713-13723.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13713-13723
    • Schmidt, J.W.1    Catterall, W.A.2
  • 22
    • 0021056873 scopus 로고
    • Effects of retinoic acid (RA) on the growth and phenotypic expression of several human neuroblastoma cell lines
    • Sidell N., Altman A., Haussler M. R., and Seeger R. C. (1983) Effects of retinoic acid (RA) on the growth and phenotypic expression of several human neuroblastoma cell lines. Exp. Cell Res. 148, 21-30.
    • (1983) Exp. Cell Res. , vol.148 , pp. 21-30
    • Sidell, N.1    Altman, A.2    Haussler, M.R.3    Seeger, R.C.4
  • 23
    • 0029782734 scopus 로고    scopus 로고
    • Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis
    • Sleat D. E., Sohar I., Lackland H., Majercak J., and Lobel P. (1996) Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis. J. Biol. Chem. 271, 19191-19198.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19191-19198
    • Sleat, D.E.1    Sohar, I.2    Lackland, H.3    Majercak, J.4    Lobel, P.5
  • 24
    • 0030009044 scopus 로고    scopus 로고
    • Lysosomal targeting of palmitoyl-protein thioesterase
    • Verkruyse L. A. and Hofmann S. L. (1996) Lysosomal targeting of palmitoyl-protein thioesterase. J. Biol. Chem. 271, 15831-15836.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15831-15836
    • Verkruyse, L.A.1    Hofmann, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.