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Volumn 1860, Issue 8, 2016, Pages 1608-1614

Glycomics and glycoproteomics focused on aging and age-related diseases - Glycans as a potential biomarker for physiological alterations

Author keywords

Aging; Biomarker; Glycomics; Glycoproteomics; Glycosylation; Longevity

Indexed keywords

BIOLOGICAL MARKER; GLYCAN; GLYCOPROTEIN; IMMUNOGLOBULIN;

EID: 84955604732     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2016.01.013     Document Type: Review
Times cited : (72)

References (79)
  • 1
    • 84903523241 scopus 로고    scopus 로고
    • Lifestyle factors related to mortality and survival: A mini-review
    • D. Rizzuto, and L. Fratiglioni Lifestyle factors related to mortality and survival: a mini-review Gerontology 60 2014 327 335
    • (2014) Gerontology , vol.60 , pp. 327-335
    • Rizzuto, D.1    Fratiglioni, L.2
  • 2
    • 79251489778 scopus 로고    scopus 로고
    • Glycomics hits the big time
    • G.W. Hart, and R.J. Copeland Glycomics hits the big time Cell 143 2010 672 676
    • (2010) Cell , vol.143 , pp. 672-676
    • Hart, G.W.1    Copeland, R.J.2
  • 3
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • K. Ohtsubo, and J.D. Marth Glycosylation in cellular mechanisms of health and disease Cell 126 2006 855 867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 4
    • 53049084874 scopus 로고    scopus 로고
    • N-glycans in cancer progression
    • K.S. Lau, and J.W. Dennis N-glycans in cancer progression Glycobiology 18 2008 750 760
    • (2008) Glycobiology , vol.18 , pp. 750-760
    • Lau, K.S.1    Dennis, J.W.2
  • 5
    • 84906861263 scopus 로고    scopus 로고
    • Sweet and sour: The role of glycosylation for the anti-inflammatory activity of immunoglobulin G
    • S. Bohm, D. Kao, and F. Nimmerjahn Sweet and sour: the role of glycosylation for the anti-inflammatory activity of immunoglobulin G Curr. Top. Microbiol. Immunol. 382 2014 393 417
    • (2014) Curr. Top. Microbiol. Immunol. , vol.382 , pp. 393-417
    • Bohm, S.1    Kao, D.2    Nimmerjahn, F.3
  • 7
    • 77954681104 scopus 로고    scopus 로고
    • Alteration of brain glycoproteins during aging
    • Y. Sato, and T. Endo Alteration of brain glycoproteins during aging Geriatr. Gerontol. Int. 10 Suppl. 1 2010 S32 S40
    • (2010) Geriatr. Gerontol. Int. , vol.10 , pp. S32-S40
    • Sato, Y.1    Endo, T.2
  • 12
    • 34247616380 scopus 로고    scopus 로고
    • Glycome mapping on DNA sequencing equipment
    • W. Laroy, R. Contreras, and N. Callewaert Glycome mapping on DNA sequencing equipment Nat. Protoc. 1 2006 397 405
    • (2006) Nat. Protoc. , vol.1 , pp. 397-405
    • Laroy, W.1    Contreras, R.2    Callewaert, N.3
  • 13
    • 49449095723 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography-based high-throughput sample preparation method for N-glycan analysis from total human plasma glycoproteins
    • L.R. Ruhaak, C. Huhn, W.J. Waterreus, A.R. de Boer, C. Neususs, C.H. Hokke, A.M. Deelder, and M. Wuhrer Hydrophilic interaction chromatography-based high-throughput sample preparation method for N-glycan analysis from total human plasma glycoproteins Anal. Chem. 80 2008 6119 6126
    • (2008) Anal. Chem. , vol.80 , pp. 6119-6126
    • Ruhaak, L.R.1    Huhn, C.2    Waterreus, W.J.3    De Boer, A.R.4    Neususs, C.5    Hokke, C.H.6    Deelder, A.M.7    Wuhrer, M.8
  • 15
    • 65249134633 scopus 로고    scopus 로고
    • Structural glycomics using hydrophilic interaction chromatography (HILIC) with mass spectrometry
    • M. Wuhrer, A.R. de Boer, and A.M. Deelder Structural glycomics using hydrophilic interaction chromatography (HILIC) with mass spectrometry Mass Spectrom. Rev. 28 2009 192 206
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 192-206
    • Wuhrer, M.1    De Boer, A.R.2    Deelder, A.M.3
  • 18
    • 0034948464 scopus 로고    scopus 로고
    • Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment
    • N. Callewaert, S. Geysens, F. Molemans, and R. Contreras Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment Glycobiology 11 2001 275 281
    • (2001) Glycobiology , vol.11 , pp. 275-281
    • Callewaert, N.1    Geysens, S.2    Molemans, F.3    Contreras, R.4
  • 25
    • 84955494519 scopus 로고    scopus 로고
    • And SONIC (Septuagenarians, Octogenarians, Nonagenarians Investigation with Centenarians), Change in N-glycosylation of plasma proteins in Japanese semisupercentenarians
    • Y. Miura, N. Hashii, H. Tsumoto, D. Takakura, Y. Ohta, Y. Abe, Y. Arai, N. Kawasaki, N. Hirose, and T. Endo and SONIC (Septuagenarians, Octogenarians, Nonagenarians Investigation with Centenarians), Change in N-glycosylation of plasma proteins in Japanese semisupercentenarians PLoS One 10 2015 e0142645
    • (2015) PLoS One , vol.10
    • Miura, Y.1    Hashii, N.2    Tsumoto, H.3    Takakura, D.4    Ohta, Y.5    Abe, Y.6    Arai, Y.7    Kawasaki, N.8    Hirose, N.9    Endo, T.10
  • 26
    • 0001697163 scopus 로고
    • Protein-carbohydrate interaction. II. Inhibition studies on the interaction of concanavalin a with polysaccharides
    • I.J. Goldstein, C.E. Hollerman, and E.E. Smith Protein-carbohydrate interaction. II. Inhibition studies on the interaction of concanavalin a with polysaccharides Biochemistry 4 1965 876 883
    • (1965) Biochemistry , vol.4 , pp. 876-883
    • Goldstein, I.J.1    Hollerman, C.E.2    Smith, E.E.3
  • 27
    • 61849168093 scopus 로고    scopus 로고
    • Proteomics-determined differences in the concanavalin-A-fractionated proteome of hippocampus and inferior parietal lobule in subjects with Alzheimer's disease and mild cognitive impairment: Implications for progression of AD
    • J.B. Owen, F. Di Domenico, R. Sultana, M. Perluigi, C. Cini, W.M. Pierce, and D.A. Butterfield Proteomics-determined differences in the concanavalin-A-fractionated proteome of hippocampus and inferior parietal lobule in subjects with Alzheimer's disease and mild cognitive impairment: implications for progression of AD J. Proteome Res. 8 2009 471 482
    • (2009) J. Proteome Res. , vol.8 , pp. 471-482
    • Owen, J.B.1    Di Domenico, F.2    Sultana, R.3    Perluigi, M.4    Cini, C.5    Pierce, W.M.6    Butterfield, D.A.7
  • 28
    • 78049431249 scopus 로고    scopus 로고
    • The wheat germ agglutinin-fractionated proteome of subjects with Alzheimer's disease and mild cognitive impairment hippocampus and inferior parietal lobule: Implications for disease pathogenesis and progression
    • F. Di Domenico, J.B. Owen, R. Sultana, R.A. Sowell, M. Perluigi, C. Cini, J. Cai, W.M. Pierce, and D.A. Butterfield The wheat germ agglutinin-fractionated proteome of subjects with Alzheimer's disease and mild cognitive impairment hippocampus and inferior parietal lobule: implications for disease pathogenesis and progression J. Neurosci. Res. 88 2010 3566 3577
    • (2010) J. Neurosci. Res. , vol.88 , pp. 3566-3577
    • Di Domenico, F.1    Owen, J.B.2    Sultana, R.3    Sowell, R.A.4    Perluigi, M.5    Cini, C.6    Cai, J.7    Pierce, W.M.8    Butterfield, D.A.9
  • 29
    • 79251552289 scopus 로고    scopus 로고
    • Lectin-affinity chromatography brain glycoproteomics and Alzheimer disease: Insights into protein alterations consistent with the pathology and progression of this dementing disorder
    • D.A. Butterfield, and J.B. Owen Lectin-affinity chromatography brain glycoproteomics and Alzheimer disease: insights into protein alterations consistent with the pathology and progression of this dementing disorder Proteomics Clin. Appl. 5 2011 50 56
    • (2011) Proteomics Clin. Appl. , vol.5 , pp. 50-56
    • Butterfield, D.A.1    Owen, J.B.2
  • 32
    • 44549087658 scopus 로고    scopus 로고
    • Structural and quantitative comparison of cerebrospinal fluid glycoproteins in Alzheimer's disease patients and healthy individuals
    • C. Sihlbom, P. Davidsson, M. Sjogren, L.O. Wahlund, and C.L. Nilsson Structural and quantitative comparison of cerebrospinal fluid glycoproteins in Alzheimer's disease patients and healthy individuals Neurochem. Res. 33 2008 1332 1340
    • (2008) Neurochem. Res. , vol.33 , pp. 1332-1340
    • Sihlbom, C.1    Davidsson, P.2    Sjogren, M.3    Wahlund, L.O.4    Nilsson, C.L.5
  • 35
    • 20444501805 scopus 로고    scopus 로고
    • Development of a lectin microarray for the rapid analysis of protein glycopatterns
    • K.T. Pilobello, L. Krishnamoorthy, D. Slawek, and L.K. Mahal Development of a lectin microarray for the rapid analysis of protein glycopatterns Chembiochem 6 2005 985 989
    • (2005) Chembiochem , vol.6 , pp. 985-989
    • Pilobello, K.T.1    Krishnamoorthy, L.2    Slawek, D.3    Mahal, L.K.4
  • 36
    • 58149381931 scopus 로고    scopus 로고
    • Glycosylation changes on serum glycoproteins in ovarian cancer may contribute to disease pathogenesis
    • R. Saldova, M.R. Wormald, R.A. Dwek, and P.M. Rudd Glycosylation changes on serum glycoproteins in ovarian cancer may contribute to disease pathogenesis Dis. Markers 25 2008 219 232
    • (2008) Dis. Markers , vol.25 , pp. 219-232
    • Saldova, R.1    Wormald, M.R.2    Dwek, R.A.3    Rudd, P.M.4
  • 39
    • 84923288088 scopus 로고    scopus 로고
    • Glycans and cancer: Role of N-glycans in cancer biomarker, progression and metastasis, and therapeutics
    • N. Taniguchi, and Y. Kizuka Glycans and cancer: role of N-glycans in cancer biomarker, progression and metastasis, and therapeutics Adv. Cancer Res. 126 2015 11 51
    • (2015) Adv. Cancer Res. , vol.126 , pp. 11-51
    • Taniguchi, N.1    Kizuka, Y.2
  • 41
    • 53849139399 scopus 로고    scopus 로고
    • Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins
    • K. Akasaka-Manya, H. Manya, Y. Sakurai, B.S. Wojczyk, S.L. Spitalnik, and T. Endo Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins Glycoconj. J. 25 2008 775 786
    • (2008) Glycoconj. J. , vol.25 , pp. 775-786
    • Akasaka-Manya, K.1    Manya, H.2    Sakurai, Y.3    Wojczyk, B.S.4    Spitalnik, S.L.5    Endo, T.6
  • 42
    • 61849088987 scopus 로고    scopus 로고
    • Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation
    • I. Perdivara, R. Petrovich, B. Allinquant, L.J. Deterding, K.B. Tomer, and M. Przybylski Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation J. Proteome Res. 8 2009 631 642
    • (2009) J. Proteome Res. , vol.8 , pp. 631-642
    • Perdivara, I.1    Petrovich, R.2    Allinquant, B.3    Deterding, L.J.4    Tomer, K.B.5    Przybylski, M.6
  • 44
    • 0037144422 scopus 로고    scopus 로고
    • Complex N-linked glycosylated nicastrin associates with active gamma-secretase and undergoes tight cellular regulation
    • W.T. Kimberly, M.J. LaVoie, B.L. Ostaszewski, W. Ye, M.S. Wolfe, and D.J. Selkoe Complex N-linked glycosylated nicastrin associates with active gamma-secretase and undergoes tight cellular regulation J. Biol. Chem. 277 2002 35113 35117
    • (2002) J. Biol. Chem. , vol.277 , pp. 35113-35117
    • Kimberly, W.T.1    LaVoie, M.J.2    Ostaszewski, B.L.3    Ye, W.4    Wolfe, M.S.5    Selkoe, D.J.6
  • 45
    • 0037024364 scopus 로고    scopus 로고
    • Complex N-glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments
    • T. Tomita, R. Katayama, R. Takikawa, and T. Iwatsubo Complex N-glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments FEBS Lett. 520 2002 117 121
    • (2002) FEBS Lett. , vol.520 , pp. 117-121
    • Tomita, T.1    Katayama, R.2    Takikawa, R.3    Iwatsubo, T.4
  • 46
    • 0035843950 scopus 로고    scopus 로고
    • Analysis of N-glycans of pathological tau: Possible occurrence of aberrant processing of tau in Alzheimer's disease
    • Y. Sato, Y. Naito, I. Grundke-Iqbal, K. Iqbal, and T. Endo Analysis of N-glycans of pathological tau: possible occurrence of aberrant processing of tau in Alzheimer's disease FEBS Lett. 496 2001 152 160
    • (2001) FEBS Lett. , vol.496 , pp. 152-160
    • Sato, Y.1    Naito, Y.2    Grundke-Iqbal, I.3    Iqbal, K.4    Endo, T.5
  • 47
    • 84891836688 scopus 로고    scopus 로고
    • The role of protein glycosylation in Alzheimer disease
    • S. Schedin-Weiss, B. Winblad, and L.O. Tjernberg The role of protein glycosylation in Alzheimer disease FEBS J. 281 2014 46 62
    • (2014) FEBS J. , vol.281 , pp. 46-62
    • Schedin-Weiss, S.1    Winblad, B.2    Tjernberg, L.O.3
  • 49
    • 84857049234 scopus 로고    scopus 로고
    • Microheterogeneity of some serum glycoproteins in neurodegenerative diseases
    • E. Marklova, Z. Albahri, and M. Valis Microheterogeneity of some serum glycoproteins in neurodegenerative diseases J. Neurol. Sci. 314 2012 20 25
    • (2012) J. Neurol. Sci. , vol.314 , pp. 20-25
    • Marklova, E.1    Albahri, Z.2    Valis, M.3
  • 50
    • 27744553322 scopus 로고    scopus 로고
    • Proteomic analysis of glial fibrillary acidic protein in Alzheimer's disease and aging brain
    • M.A. Korolainen, S. Auriola, T.A. Nyman, I. Alafuzoff, and T. Pirttila Proteomic analysis of glial fibrillary acidic protein in Alzheimer's disease and aging brain Neurobiol. Dis. 20 2005 858 870
    • (2005) Neurobiol. Dis. , vol.20 , pp. 858-870
    • Korolainen, M.A.1    Auriola, S.2    Nyman, T.A.3    Alafuzoff, I.4    Pirttila, T.5
  • 51
    • 0024824922 scopus 로고
    • Patterns of gliosis in Alzheimer's disease and aging cerebrum
    • T.G. Beach, R. Walker, and E.G. McGeer Patterns of gliosis in Alzheimer's disease and aging cerebrum Glia 2 1989 420 436
    • (1989) Glia , vol.2 , pp. 420-436
    • Beach, T.G.1    Walker, R.2    McGeer, E.G.3
  • 54
    • 0015387246 scopus 로고
    • Elevation of glycoprotein fucose in diabetes mellitus
    • D.E. McMillan Elevation of glycoprotein fucose in diabetes mellitus Diabetes 21 1972 863 871
    • (1972) Diabetes , vol.21 , pp. 863-871
    • McMillan, D.E.1
  • 55
    • 0017685261 scopus 로고
    • Serum UDP-galactose: Glycoprotein galactosyltransferase in diabetics with microangiopathy
    • L.P. Lee, A. Prasad, K.J. Bolton, J.B. McKendry, and I. Hynie Serum UDP-galactose: glycoprotein galactosyltransferase in diabetics with microangiopathy Clin. Biochem. 10 1977 111 117
    • (1977) Clin. Biochem. , vol.10 , pp. 111-117
    • Lee, L.P.1    Prasad, A.2    Bolton, K.J.3    McKendry, J.B.4    Hynie, I.5
  • 57
    • 33744913541 scopus 로고    scopus 로고
    • Research agenda for frailty in older adults: Toward a better understanding of physiology and etiology: Summary from the American Geriatrics Society/National Institute on Aging Research Conference on Frailty in Older Adults
    • J. Walston, E.C. Hadley, L. Ferrucci, J.M. Guralnik, A.B. Newman, S.A. Studenski, W.B. Ershler, T. Harris, and L.P. Fried Research agenda for frailty in older adults: toward a better understanding of physiology and etiology: summary from the American Geriatrics Society/National Institute on Aging Research Conference on Frailty in Older Adults J. Am. Geriatr. Soc. 54 2006 991 1001
    • (2006) J. Am. Geriatr. Soc. , vol.54 , pp. 991-1001
    • Walston, J.1    Hadley, E.C.2    Ferrucci, L.3    Guralnik, J.M.4    Newman, A.B.5    Studenski, S.A.6    Ershler, W.B.7    Harris, T.8    Fried, L.P.9
  • 59
    • 0025098286 scopus 로고
    • A genetic defect in the biosynthesis of dermatan sulfate proteoglycan: Galactosyltransferase i deficiency in fibroblasts from a patient with a progeroid syndrome
    • E. Quentin, A. Gladen, L. Roden, and H. Kresse A genetic defect in the biosynthesis of dermatan sulfate proteoglycan: galactosyltransferase I deficiency in fibroblasts from a patient with a progeroid syndrome Proc. Natl. Acad. Sci. U. S. A. 87 1990 1342 1346
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 1342-1346
    • Quentin, E.1    Gladen, A.2    Roden, L.3    Kresse, H.4
  • 60
    • 0032857187 scopus 로고    scopus 로고
    • Molecular basis for the progeroid variant of Ehlers-Danlos syndrome. Identification and characterization of two mutations in galactosyltransferase i gene
    • T. Okajima, S. Fukumoto, K. Furukawa, and T. Urano Molecular basis for the progeroid variant of Ehlers-Danlos syndrome. Identification and characterization of two mutations in galactosyltransferase I gene J. Biol. Chem. 274 1999 28841 28844
    • (1999) J. Biol. Chem. , vol.274 , pp. 28841-28844
    • Okajima, T.1    Fukumoto, S.2    Furukawa, K.3    Urano, T.4
  • 62
    • 0023912648 scopus 로고
    • Age-related galactosylation of the N-linked oligosaccharides of human serum IgG
    • R. Parekh, I. Roitt, D. Isenberg, R. Dwek, and T. Rademacher Age-related galactosylation of the N-linked oligosaccharides of human serum IgG J. Exp. Med. 167 1988 1731 1736
    • (1988) J. Exp. Med. , vol.167 , pp. 1731-1736
    • Parekh, R.1    Roitt, I.2    Isenberg, D.3    Dwek, R.4    Rademacher, T.5
  • 65
    • 0030996004 scopus 로고    scopus 로고
    • Structural changes of immunoglobulin G oligosaccharides with age in healthy human serum
    • E. Yamada, Y. Tsukamoto, R. Sasaki, K. Yagyu, and N. Takahashi Structural changes of immunoglobulin G oligosaccharides with age in healthy human serum Glycoconj. J. 14 1997 401 405
    • (1997) Glycoconj. J. , vol.14 , pp. 401-405
    • Yamada, E.1    Tsukamoto, Y.2    Sasaki, R.3    Yagyu, K.4    Takahashi, N.5
  • 68
  • 69
    • 58149334794 scopus 로고    scopus 로고
    • N-glycan profiles as tools in diagnosis of hepatocellular carcinoma and prediction of healthy human ageing
    • V. Vanhooren, X.E. Liu, C. Franceschi, C.F. Gao, C. Libert, R. Contreras, and C. Chen N-glycan profiles as tools in diagnosis of hepatocellular carcinoma and prediction of healthy human ageing Mech. Ageing Dev. 130 2009 92 97
    • (2009) Mech. Ageing Dev. , vol.130 , pp. 92-97
    • Vanhooren, V.1    Liu, X.E.2    Franceschi, C.3    Gao, C.F.4    Libert, C.5    Contreras, R.6    Chen, C.7
  • 77
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • G.W. Hart, M.P. Housley, and C. Slawson Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins Nature 446 2007 1017 1022
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 78
    • 34547769859 scopus 로고    scopus 로고
    • Metabolic homeostasis and tissue renewal are dependent on beta1,6GlcNAc-branched N-glycans
    • P. Cheung, J. Pawling, E.A. Partridge, B. Sukhu, M. Grynpas, and J.W. Dennis Metabolic homeostasis and tissue renewal are dependent on beta1,6GlcNAc-branched N-glycans Glycobiology 17 2007 828 837
    • (2007) Glycobiology , vol.17 , pp. 828-837
    • Cheung, P.1    Pawling, J.2    Partridge, E.A.3    Sukhu, B.4    Grynpas, M.5    Dennis, J.W.6
  • 79
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes
    • K. Ohtsubo, S. Takamatsu, M.T. Minowa, A. Yoshida, M. Takeuchi, and J.D. Marth Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes Cell 123 2005 1307 1321
    • (2005) Cell , vol.123 , pp. 1307-1321
    • Ohtsubo, K.1    Takamatsu, S.2    Minowa, M.T.3    Yoshida, A.4    Takeuchi, M.5    Marth, J.D.6


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