메뉴 건너뛰기




Volumn 49, Issue 326, 1998, Pages 1463-1472

The protein N-glycosylation in plants

Author keywords

Biosynthesis and function; N linked oligosaccharide; Phytohaemagglutinin

Indexed keywords

PHASEOLUS (ANGIOSPERM);

EID: 0031826473     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/49.326.1463     Document Type: Review
Times cited : (127)

References (48)
  • 1
    • 0030857326 scopus 로고    scopus 로고
    • More than silk and honey - Or, can insect cells serve in the production of therapeutic glycoproteins?
    • Altmann F. 1997. More than silk and honey - or, can insect cells serve in the production of therapeutic glycoproteins? Glycoconjugate Journal 14, 643-6.
    • (1997) Glycoconjugate Journal , vol.14 , pp. 643-646
    • Altmann, F.1
  • 2
    • 0002913516 scopus 로고
    • Glycosylation is not needed for the intracellular transport of phytohaemagglutinin in developping Phaseolus vulgaris cotyledons and for the maintenance of its biological activities
    • Bollini R, Ceriotti A, Daminati MG, Vitale A. 1985. Glycosylation is not needed for the intracellular transport of phytohaemagglutinin in developping Phaseolus vulgaris cotyledons and for the maintenance of its biological activities. Physiologia Plantarum 65, 15-22.
    • (1985) Physiologia Plantarum , vol.65 , pp. 15-22
    • Bollini, R.1    Ceriotti, A.2    Daminati, M.G.3    Vitale, A.4
  • 4
    • 7344261354 scopus 로고
    • Characterization of the endoplasmic reticulum-associated precursor of concanavalin A
    • Chrispeels MJ, Hartl PM, Sturm A, Faye L. 1986. Characterization of the endoplasmic reticulum-associated precursor of concanavalin A. Journal of Biological Chemistry 261, 1021-4.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 1021-1024
    • Chrispeels, M.J.1    Hartl, P.M.2    Sturm, A.3    Faye, L.4
  • 8
    • 0000180083 scopus 로고
    • Primary structure of the xylose-containing N-linked carbohydrate moiety from ascorbic acid oxidase of Cucurbita pepo medullosa
    • D'Andrea G, Bouwstra JB, Kamerling JP, Vliegenthart JFG. 1988. Primary structure of the xylose-containing N-linked carbohydrate moiety from ascorbic acid oxidase of Cucurbita pepo medullosa. Glycoconjugate Journal 5, 151-7.
    • (1988) Glycoconjugate Journal , vol.5 , pp. 151-157
    • D'Andrea, G.1    Bouwstra, J.B.2    Kamerling, J.P.3    Vliegenthart, J.F.G.4
  • 9
    • 0001866453 scopus 로고
    • The role of high-mannose and complex asparagine-linked glycans in the secretion and stability of glycoproteins
    • Driouich A, Gonnet P, Makkie M, Laine AC, Faye L. 1989. The role of high-mannose and complex asparagine-linked glycans in the secretion and stability of glycoproteins. Planta 180, 96-104.
    • (1989) Planta , vol.180 , pp. 96-104
    • Driouich, A.1    Gonnet, P.2    Makkie, M.3    Laine, A.C.4    Faye, L.5
  • 10
    • 0022533179 scopus 로고
    • The position of the oligosaccharide side-chains of phytohaemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Golgi
    • Faye L, Sturm A, Bollini R, Vitale A, Chrispeels MJ. 1986. The position of the oligosaccharide side-chains of phytohaemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Golgi. European Journal of Biochemistry 158, 655-61.
    • (1986) European Journal of Biochemistry , vol.158 , pp. 655-661
    • Faye, L.1    Sturm, A.2    Bollini, R.3    Vitale, A.4    Chrispeels, M.J.5
  • 11
    • 0001142403 scopus 로고
    • Transport and processing of the glycosylated precursor of concanavalin a in jack-bean
    • Faye L, Chrispeels MJ. 1987. Transport and processing of the glycosylated precursor of concanavalin A in jack-bean. Planta 170, 217-24.
    • (1987) Planta , vol.170 , pp. 217-224
    • Faye, L.1    Chrispeels, M.J.2
  • 12
    • 0000724871 scopus 로고
    • Apparent inhibition of β-fructosidase secretion by tunicamycin may be explained by breakdown of the unglycosylated protein during secretion
    • Faye L, Chrispeels MJ. 1989. Apparent inhibition of β-fructosidase secretion by tunicamycin may be explained by breakdown of the unglycosylated protein during secretion. Plant Physiology 89, 845-51.
    • (1989) Plant Physiology , vol.89 , pp. 845-851
    • Faye, L.1    Chrispeels, M.J.2
  • 13
    • 0016818858 scopus 로고
    • Purification of the phytohaemagglutinin family proteins from red kidney beans (Phaseolus vulgaris) by affinity chromatography
    • Felsted RL, Leavitt RD, Bachur NR. 1975. Purification of the phytohaemagglutinin family proteins from red kidney beans (Phaseolus vulgaris) by affinity chromatography. Biochimica et Biophysica Acta 405, 72-81.
    • (1975) Biochimica et Biophysica Acta , vol.405 , pp. 72-81
    • Felsted, R.L.1    Leavitt, R.D.2    Bachur, N.R.3
  • 14
    • 0028103135 scopus 로고
    • Distribution of xylosylation and fucosylation in the plant Golgi apparatus
    • Fitchette-Lainé AC, Gomord V, Chekkafi A, Faye L. 1994. Distribution of xylosylation and fucosylation in the plant Golgi apparatus. The Plant Journal 5, 673-82.
    • (1994) The Plant Journal , vol.5 , pp. 673-682
    • Fitchette-Lainé, A.C.1    Gomord, V.2    Chekkafi, A.3    Faye, L.4
  • 16
    • 3142638352 scopus 로고
    • Protein bodies and vacuoles as lysosomes. Investigations into the role of mannose-6-phosphate in intracellular transport of glycosidases in pea cotyledons
    • Gaudreault PS, Beevers L. 1984. Protein bodies and vacuoles as lysosomes. Investigations into the role of mannose-6-phosphate in intracellular transport of glycosidases in pea cotyledons. Plant Physiology 76, 228-32.
    • (1984) Plant Physiology , vol.76 , pp. 228-232
    • Gaudreault, P.S.1    Beevers, L.2
  • 17
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C, Braakman I, Helenius A. 1994. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proceedings of the National Academy of Sciences, USA 91, 913-17.
    • (1994) Proceedings of the National Academy of Sciences, USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 19
    • 2242442873 scopus 로고
    • Vacuole accumulation of storage protein and lectin expressed in transgenic tobacco seeds
    • Herman EM, Chrispeels MJ, Hoffman LM. 1989. Vacuole accumulation of storage protein and lectin expressed in transgenic tobacco seeds. Cell Biology International Reports 13, 37-45.
    • (1989) Cell Biology International Reports , vol.13 , pp. 37-45
    • Herman, E.M.1    Chrispeels, M.J.2    Hoffman, L.M.3
  • 20
    • 0000592224 scopus 로고
    • Substrate specificities of N-acetylglucosaminyl-, fucosyl-, and xylosyltransferases that modify glycoproteins in the Golgi appparatus of bean cotyledons
    • Johnson KD, Chrispeels MJ. 1987. Substrate specificities of N-acetylglucosaminyl-, fucosyl-, and xylosyltransferases that modify glycoproteins in the Golgi appparatus of bean cotyledons. Plant Physiology 84, 1301-8.
    • (1987) Plant Physiology , vol.84 , pp. 1301-1308
    • Johnson, K.D.1    Chrispeels, M.J.2
  • 21
    • 0025130561 scopus 로고
    • Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells
    • Kaushal GP, Pastuszak I, Hatanaka KI, Elbein AD. 1990a. Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells. The Journal of Biological Chemistry 265, 16271-9.
    • (1990) The Journal of Biological Chemistry , vol.265 , pp. 16271-16279
    • Kaushal, G.P.1    Pastuszak, I.2    Hatanaka, K.I.3    Elbein, A.D.4
  • 22
    • 0025234553 scopus 로고
    • Purification to homogeneity and properties of mannosidase II from mung bean seedlings
    • Kaushal GP, Szumilo T, Pastuszak I, Elbein AD. 1990b. Purification to homogeneity and properties of mannosidase II from mung bean seedlings. Biochemistry 29, 2168-76.
    • (1990) Biochemistry , vol.29 , pp. 2168-2176
    • Kaushal, G.P.1    Szumilo, T.2    Pastuszak, I.3    Elbein, A.D.4
  • 23
  • 24
    • 0031590175 scopus 로고    scopus 로고
    • Identification of the human Lewis a carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.)
    • Melo NS, Nimtz M, Conradt HS, Feveiro PS, Costa J. 1997. Identification of the human Lewis a carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.). FEBS Letters 415, 186-91.
    • (1997) FEBS Letters , vol.415 , pp. 186-191
    • Melo, N.S.1    Nimtz, M.2    Conradt, H.S.3    Feveiro, P.S.4    Costa, J.5
  • 26
    • 0029741668 scopus 로고    scopus 로고
    • Structures and contribution to the antigenicity of oligosaccharides of Japanese cedar (Cryptomeria japonica) pollen allergen Cry j I: Relationship between the structures and antigenic epitopes of plant N-linked complex-type glycans
    • Ogawa H, Hijikata A, Amano M, Kojima K, Fukushima H, Ishizuka I, Kurihara Y, Matsumoto I. 1996. Structures and contribution to the antigenicity of oligosaccharides of Japanese cedar (Cryptomeria japonica) pollen allergen Cry j I: relationship between the structures and antigenic epitopes of plant N-linked complex-type glycans. Glycoconjuguate Journal 13, 555-66.
    • (1996) Glycoconjuguate Journal , vol.13 , pp. 555-566
    • Ogawa, H.1    Hijikata, A.2    Amano, M.3    Kojima, K.4    Fukushima, H.5    Ishizuka, I.6    Kurihara, Y.7    Matsumoto, I.8
  • 29
    • 0030038134 scopus 로고    scopus 로고
    • N-glycosylation of phytohaemagglutinin expressed in bean cotyledons or in transgenic tobacco cells
    • Rayon C, Gomord V, Faye L, Lerouge P. 1996. N-glycosylation of phytohaemagglutinin expressed in bean cotyledons or in transgenic tobacco cells. Plant Physiology and Biochemistry 34, 273-81.
    • (1996) Plant Physiology and Biochemistry , vol.34 , pp. 273-281
    • Rayon, C.1    Gomord, V.2    Faye, L.3    Lerouge, P.4
  • 30
    • 0020472801 scopus 로고
    • The phosphomannosyl recognition system for intracellular and intercellular transport of lysomal enzymes
    • Sly WS, Fischer MD. 1982. The phosphomannosyl recognition system for intracellular and intercellular transport of lysomal enzymes. Journal of Cell Biochemistry 18, 67-85.
    • (1982) Journal of Cell Biochemistry , vol.18 , pp. 67-85
    • Sly, W.S.1    Fischer, M.D.2
  • 31
    • 0029585339 scopus 로고
    • Functional purification and characterization of a GDP-fucose: β-N-acetylglucosamine (Fuc to Asn linked GlcNAc) α-1,3-fucosyltransferase from mung beans
    • Staudacher E, Dalik T, Wawra P, Altmann F, März L. 1995. Functional purification and characterization of a GDP-fucose: β-N-acetylglucosamine (Fuc to Asn linked GlcNAc) α-1,3-fucosyltransferase from mung beans. Glycoconjugate Journal 12, 780-6.
    • (1995) Glycoconjugate Journal , vol.12 , pp. 780-786
    • Staudacher, E.1    Dalik, T.2    Wawra, P.3    Altmann, F.4    März, L.5
  • 32
    • 0000923778 scopus 로고
    • The high mannose oligosaccharide of phytohaemagglutinin is attached to asparagine 12 and the modified oligosaccharide to asparagine 60
    • Sturm A, Chrispeels MJ. 1986. The high mannose oligosaccharide of phytohaemagglutinin is attached to asparagine 12 and the modified oligosaccharide to asparagine 60. Plant Physiology 80, 320-2.
    • (1986) Plant Physiology , vol.80 , pp. 320-322
    • Sturm, A.1    Chrispeels, M.J.2
  • 33
    • 0001455921 scopus 로고
    • Subcellular localization of glycosidases and glycosyl-transferases involved in the processing of N-linked oligosaccharides
    • Sturm A, Johnson KD, Szumilo T, Elbein AD, Chrispeels MJ. 1987a. Subcellular localization of glycosidases and glycosyl-transferases involved in the processing of N-linked oligosaccharides. Plant Physiology 85, 741-5.
    • (1987) Plant Physiology , vol.85 , pp. 741-745
    • Sturm, A.1    Johnson, K.D.2    Szumilo, T.3    Elbein, A.D.4    Chrispeels, M.J.5
  • 34
    • 0023645611 scopus 로고
    • Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side-chains of the bean storage protein phaseolin
    • Sturm A, van Kuik JA, Vliegenthart JFG, Chrispeele MJ. 1987b. Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side-chains of the bean storage protein phaseolin. The Journal of Biological Chemistry 262, 13392-403.
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 13392-13403
    • Sturm, A.1    Van Kuik, J.A.2    Vliegenthart, J.F.G.3    Chrispeele, M.J.4
  • 35
    • 0001096432 scopus 로고
    • Correct glycosylation, Golgi-processing, and targeting to protein bodies of the vacuolar protein phytohaemagglutinin in transgenic tobacco
    • Sturm A, Voelker TA, Hermann EM, Chrispeels MJ. 1988. Correct glycosylation, Golgi-processing, and targeting to protein bodies of the vacuolar protein phytohaemagglutinin in transgenic tobacco. Planta 175, 170-83.
    • (1988) Planta , vol.175 , pp. 170-183
    • Sturm, A.1    Voelker, T.A.2    Hermann, E.M.3    Chrispeels, M.J.4
  • 36
    • 0026610615 scopus 로고
    • 1H-NMR structural determination of the N-linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohaemagglutinin
    • 1H-NMR structural determination of the N-linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohaemagglutinin. European Journal of Biochemistry 204, 313-16.
    • (1992) European Journal of Biochemistry , vol.204 , pp. 313-316
    • Sturm, A.1    Bergwerff, A.A.2    Vliegenthart, J.F.G.3
  • 38
    • 0005034578 scopus 로고
    • Purification and properties of a glycoprotein processing α-mannosidase from mung bean seedling
    • Szumilo T, Kaushal GP,Hori H, Elbein AD. 1986b. Purification and properties of a glycoprotein processing α-mannosidase from mung bean seedling. Plant Physiology 81, 383-9.
    • (1986) Plant Physiology , vol.81 , pp. 383-389
    • Szumilo, T.1    Kaushal, G.P.2    Hori, H.3    Elbein, A.D.4
  • 41
    • 0026593745 scopus 로고
    • Studies on synthetic of xylose-containing N-linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)
    • Tezuka K, Hayashi M, Ishihara H, Akazawa T, Takahashi N. 1992. Studies on synthetic of xylose-containing N-linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.). European Journal of Biochemistry 203, 401-13.
    • (1992) European Journal of Biochemistry , vol.203 , pp. 401-413
    • Tezuka, K.1    Hayashi, M.2    Ishihara, H.3    Akazawa, T.4    Takahashi, N.5
  • 43
    • 0025971611 scopus 로고
    • Analysis of glycoprotein oligosaccharides using high-pH anion exchange chromatography
    • Townsend RR, Hardy MR. 1991. Analysis of glycoprotein oligosaccharides using high-pH anion exchange chromatography. Glycobiology 1, 139-47.
    • (1991) Glycobiology , vol.1 , pp. 139-147
    • Townsend, R.R.1    Hardy, M.R.2
  • 44
    • 0024468302 scopus 로고
    • Glucosylation of glycoproteins by mammalian, plant, fungal and trypanosomatid protozoa microsomal membranes
    • Trombetta SE, Bosch M, Parodi AJ. 1989. Glucosylation of glycoproteins by mammalian, plant, fungal and trypanosomatid protozoa microsomal membranes. Biochemistry 28, 8108-16.
    • (1989) Biochemistry , vol.28 , pp. 8108-8116
    • Trombetta, S.E.1    Bosch, M.2    Parodi, A.J.3
  • 45
    • 0021274996 scopus 로고
    • Transient N-acetylglucosamine in the biosynthesis of phytohaemagglutinin: Attachment in the Golgi apparatus and removal in protein bodies
    • Vitale A, Chrispeels MJ. 1984. Transient N-acetylglucosamine in the biosynthesis of phytohaemagglutinin: attachment in the Golgi apparatus and removal in protein bodies. The Journal of Cell Biology 99, 133-40.
    • (1984) The Journal of Cell Biology , vol.99 , pp. 133-140
    • Vitale, A.1    Chrispeels, M.J.2
  • 46
    • 0011275203 scopus 로고
    • Differences in expression between two seed lectin alleles obtained from normal and lectin-deficient beans are maintened in transgenic tobacco
    • Voelker TA, Sturm A, Chrispeels MJ. 1987. Differences in expression between two seed lectin alleles obtained from normal and lectin-deficient beans are maintened in transgenic tobacco. EMBO Journal 6, 3571-7.
    • (1987) EMBO Journal , vol.6 , pp. 3571-3577
    • Voelker, T.A.1    Sturm, A.2    Chrispeels, M.J.3
  • 47
    • 0024301301 scopus 로고
    • In vitro mutated phytohaemagglutinin genes expressed in tobacco seeds: Role of glycans in protein targeting and stability
    • Voelker TA, Hermann EM, Chrispeels MJ. 1989. In vitro mutated phytohaemagglutinin genes expressed in tobacco seeds: role of glycans in protein targeting and stability. The Plant Cell 1, 95-104.
    • (1989) The Plant Cell , vol.1 , pp. 95-104
    • Voelker, T.A.1    Hermann, E.M.2    Chrispeels, M.J.3
  • 48
    • 0027640147 scopus 로고
    • Isolation of a mutant Arabidopsis plant that lacks N-acetylglucosaminidase I is unable to synthesize Golgi-modified complex N-linked glycans
    • von Schaewen A, Sturm A, O'Neill J, Chrispeels MJ. 1993. Isolation of a mutant Arabidopsis plant that lacks N-acetylglucosaminidase I is unable to synthesize Golgi-modified complex N-linked glycans. Plant Physiology 102, 1109-18.
    • (1993) Plant Physiology , vol.102 , pp. 1109-1118
    • Von Schaewen, A.1    Sturm, A.2    O'Neill, J.3    Chrispeels, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.