메뉴 건너뛰기




Volumn 53, Issue 9, 2015, Pages 1315-1320

Possible role of fructosamine 3-kinase genotyping for the management of diabetic patients

Author keywords

deglycation; diabetes; fructosamine 3 kinase (FN3K); glycated hemoglobin (HbA1c); glycation; single nucleotide polymorphisms

Indexed keywords

ENZYME; FRUCTOSAMINE 3 KINASE; UNCLASSIFIED DRUG; FRUCTOSAMINE-3-KINASE; PHOSPHOTRANSFERASE;

EID: 84938487320     PISSN: 14346621     EISSN: 14374331     Source Type: Journal    
DOI: 10.1515/cclm-2015-0207     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 79959936188 scopus 로고    scopus 로고
    • National, regional, and global trends in fasting plasma glucose and diabetes prevalence since 1980: Systematic analysis of health examination surveys and epidemiological studies with 370 country-years and 27 million participants
    • Danaei G, Finucane MM, Lu Y, Singh GM, Cowan MJ, Paciorek CJ, et al. National, regional, and global trends in fasting plasma glucose and diabetes prevalence since 1980: systematic analysis of health examination surveys and epidemiological studies with 370 country-years and 27 million participants. Lancet 2011;378:31-40.
    • (2011) Lancet , vol.378 , pp. 31-40
    • Danaei, G.1    Finucane, M.M.2    Lu, Y.3    Singh, G.M.4    Cowan, M.J.5    Paciorek, C.J.6
  • 2
    • 0034641568 scopus 로고    scopus 로고
    • Association of glycaemia with macrovascular and microvascular complications of type 2 diabetes (UKPDS 35): Prospective observational study
    • Stratton IM, Adler AI, Neil HA, Matthews DR, Manley SE, Cull CA, et al. Association of glycaemia with macrovascular and microvascular complications of type 2 diabetes (UKPDS 35): prospective observational study. Br Med J 2000;321:405-12.
    • (2000) Br Med J , vol.321 , pp. 405-412
    • Stratton, I.M.1    Adler, A.I.2    Neil, H.A.3    Matthews, D.R.4    Manley, S.E.5    Cull, C.A.6
  • 3
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001;414:813-20.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 4
    • 0037184495 scopus 로고    scopus 로고
    • Molecular understanding of hyperglycemia's adverse effects for diabetic complications
    • Sheetz MJ, King GL. Molecular understanding of hyperglycemia's adverse effects for diabetic complications. J Am Med Assoc 2002;288:2579-88.
    • (2002) J Am Med Assoc , vol.288 , pp. 2579-2588
    • Sheetz, M.J.1    King, G.L.2
  • 6
    • 0037099548 scopus 로고    scopus 로고
    • Inactivation of cellular enzymes by carbonyls and protein-bound glycation/glycoxidation products
    • Morgan PE, Dean RT, Davies MJ. Inactivation of cellular enzymes by carbonyls and protein-bound glycation/glycoxidation products. Arch Biochem Biophys 2002;403:259-69.
    • (2002) Arch Biochem Biophys , vol.403 , pp. 259-269
    • Morgan, P.E.1    Dean, R.T.2    Davies, M.J.3
  • 7
    • 0003082473 scopus 로고
    • The maillard reaction
    • In: Hudson BJ, editor. London: Elsevier Applied Science
    • Ames JM. The Maillard reaction. In: Hudson BJ, editor. Progress in food proteins-biochemistry. London: Elsevier Applied Science, 1992:99-153.
    • (1992) Progress in Food Proteins-biochemistry , pp. 99-153
    • Ames, J.M.1
  • 8
    • 0035787070 scopus 로고    scopus 로고
    • Protein glycation, diabetes, and aging
    • Ulrich P, Cerami A. Protein glycation, diabetes, and aging. Recent Prog Horm Res 2001;56:1-21.
    • (2001) Recent Prog Horm Res , vol.56 , pp. 1-21
    • Ulrich, P.1    Cerami, A.2
  • 9
    • 84886235609 scopus 로고    scopus 로고
    • AGEs, rather than hyperglycemia, are responsible for microvascular complications in diabetes: A "glycoxidation-centric" point of view
    • Chilelli NC, Burlina S, Lapolla A. AGEs, rather than hyperglycemia, are responsible for microvascular complications in diabetes: a "glycoxidation-centric" point of view. Nutr Metab Cardiovasc Dis 2013;23:913-9.
    • (2013) Nutr Metab Cardiovasc Dis , vol.23 , pp. 913-919
    • Chilelli, N.C.1    Burlina, S.2    Lapolla, A.3
  • 10
    • 80051988751 scopus 로고    scopus 로고
    • National academy of clinical biochemistry Position statement executive summary: Guidelines and recommendations for laboratory analysis in the diagnosis and management of diabetes mellitus
    • Sacks DB, Arnold M, Bakris GL, Bruns DE, Horvath AR, Kirkman MS, et al.; National Academy of Clinical Biochemistry. Position statement executive summary: guidelines and recommendations for laboratory analysis in the diagnosis and management of diabetes mellitus. Diabetes Care 2011;34:1419-23.
    • (2011) Diabetes Care , vol.34 , pp. 1419-1423
    • Sacks, D.B.1    Arnold, M.2    Bakris, G.L.3    Bruns, D.E.4    Horvath, A.R.5    Kirkman, M.S.6
  • 11
    • 84929145647 scopus 로고    scopus 로고
    • Glycemic targets Sec. 6. In: Standards of medical care in diabetes 2015
    • American Diabetes Association
    • American Diabetes Association. Glycemic targets. Sec. 6. In: Standards of medical care in diabetes 2015. Diabetes Care 2015;38:S33-40.
    • (2015) Diabetes Care , vol.38 , pp. S33-40
  • 12
    • 67650094848 scopus 로고    scopus 로고
    • International Expert Committee report on the role of the A1c assay in the diagnosis of diabetes
    • The International Expert Committee
    • The International Expert Committee. International Expert Committee report on the role of the A1c assay in the diagnosis of diabetes. Diabetes Care 2009;32:1327-34.
    • (2009) Diabetes Care , vol.32 , pp. 1327-1334
  • 13
    • 0037044736 scopus 로고    scopus 로고
    • Identification of a pathway for the utilization of the Amadori product fructoselysine in Escherichia coli
    • Wiame E, Delpierre G, Collard F, Van Schaftingen E. Identification of a pathway for the utilization of the Amadori product fructoselysine in Escherichia coli. J Biol Chem 2002;277:42523-9.
    • (2002) J Biol Chem , vol.277 , pp. 42523-42529
    • Wiame, E.1    Delpierre, G.2    Collard, F.3    Van Schaftingen, E.4
  • 14
    • 0348049817 scopus 로고    scopus 로고
    • Enzymatic deglycation with amadoriase enzymes from Aspergillus sp as a potential strategy against the complications of diabetes and aging
    • Monnier VM, Wu X. Enzymatic deglycation with amadoriase enzymes from Aspergillus sp. as a potential strategy against the complications of diabetes and aging. Biochem Soc Trans 2003;31:1349-53.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1349-1353
    • Monnier, V.M.1    Wu, X.2
  • 15
    • 0033820420 scopus 로고    scopus 로고
    • Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase
    • Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, et al. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes 2000;49:1627-34.
    • (2000) Diabetes , vol.49 , pp. 1627-1634
    • Delpierre, G.1    Rider, M.H.2    Collard, F.3    Stroobant, V.4    Vanstapel, F.5    Santos, H.6
  • 16
    • 0025006127 scopus 로고
    • Identification of sorbitol 3-phosphate and fructose 3-phosphate in normal and diabetic human erythrocytes
    • Petersen A, Szwergold BS, Kappler F, Weingarten M, Brown TR. Identification of sorbitol 3-phosphate and fructose 3-phosphate in normal and diabetic human erythrocytes. J Biol Chem 1990;265:17424-7.
    • (1990) J Biol Chem , vol.265 , pp. 17424-17427
    • Petersen, A.1    Szwergold, B.S.2    Kappler, F.3    Weingarten, M.4    Brown, T.R.5
  • 17
    • 0026748172 scopus 로고
    • Fructose metabolism in the human erythrocyte Phosphorylation to fructose 3-phosphate
    • Petersen A, Kappler F, Szwergold BS, Brown TR. Fructose metabolism in the human erythrocyte. Phosphorylation to fructose 3-phosphate. Biochem J 1992;284:363-6.
    • (1992) Biochem J , vol.284 , pp. 363-366
    • Petersen, A.1    Kappler, F.2    Szwergold, B.S.3    Brown, T.R.4
  • 18
    • 0035464966 scopus 로고    scopus 로고
    • Human fructosamine-3-kinase: Purification, sequencing, substrate specificity, and evidence of activity in vivo
    • Szwergold BS, Howell S, Beisswenger PJ. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. Diabetes 2001;50:2139-47.
    • (2001) Diabetes , vol.50 , pp. 2139-2147
    • Szwergold, B.S.1    Howell, S.2    Beisswenger, P.J.3
  • 19
    • 0345275810 scopus 로고    scopus 로고
    • A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines
    • Collard F, Delpierre G, Stroobant V, Matthijs G, Van Schaftingen E. A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines. Diabetes 2003;52:2888-95.
    • (2003) Diabetes , vol.52 , pp. 2888-2895
    • Collard, F.1    Delpierre, G.2    Stroobant, V.3    Matthijs, G.4    Van Schaftingen, E.5
  • 20
    • 8744307268 scopus 로고    scopus 로고
    • Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein
    • Delplanque J, Delpierre G, Opperdoes FR, Van Schaftingen E. Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein. J Biol Chem 2004:279:46606-13.
    • (2004) J Biol Chem , vol.279 , pp. 46606-46613
    • Delplanque, J.1    Delpierre, G.2    Opperdoes, F.R.3    Van Schaftingen, E.4
  • 21
    • 4544230995 scopus 로고    scopus 로고
    • The expression of the genes for fructosamine-3-kinase and fructosamine-3-kinaserelated protein appears to be constitutive and unaffected by environmental signals
    • Conner JR, Beisswenger PJ, Szwergold BS. The expression of the genes for fructosamine-3-kinase and fructosamine-3-kinaserelated protein appears to be constitutive and unaffected by environmental signals. Biochem Biophys Res Commun 2004;323:932-6.
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 932-936
    • Conner, J.R.1    Beisswenger, P.J.2    Szwergold, B.S.3
  • 22
    • 0036683724 scopus 로고    scopus 로고
    • Fructosamine 3-kinase is involved in an intracellular glycation pathway in human erythrocytes
    • Delpierre G, Collard F, Fortpied J, Van Schaftingen E. Fructosamine 3-kinase is involved in an intracellular glycation pathway in human erythrocytes. Biochem J 2002;365:801-8.
    • (2002) Biochem J , vol.365 , pp. 801-808
    • Delpierre, G.1    Collard, F.2    Fortpied, J.3    Van Schaftingen, E.4
  • 24
    • 77349105279 scopus 로고    scopus 로고
    • Effects of fructosamine-3-kinase deficiency on function and survival of mouse pancreatic islets after prolonged culture in high glucose or ribose concentrations
    • Pascal SM, Veiga-da-Cunha M, Gilon P, Van Schaftingen E, Jonas JC. Effects of fructosamine-3-kinase deficiency on function and survival of mouse pancreatic islets after prolonged culture in high glucose or ribose concentrations. Am J Physiol Endocrinol Metab 2010;298:E586-96.
    • (2010) Am J Physiol Endocrinol Metab , vol.298 , pp. E586-E596
    • Pascal, S.M.1    Veiga-Da-Cunha, M.2    Gilon, P.3    Van Schaftingen, E.4    Jonas, J.C.5
  • 25
    • 3042644024 scopus 로고    scopus 로고
    • Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin
    • Delpierre G, Vertommen D, Communi D, Rider MH, Van Schaftingen E. Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin. J Biol Chem 2004;279:27613-20.
    • (2004) J Biol Chem , vol.279 , pp. 27613-27620
    • Delpierre, G.1    Vertommen, D.2    Communi, D.3    Rider, M.H.4    Van Schaftingen, E.5
  • 27
    • 33646087912 scopus 로고    scopus 로고
    • Variability in erythrocyte fructosamine 3-kinase activity in humans correlates with polymorphisms in the FN3K gene and impacts on haemoglobin glycation at specific sites
    • Delpierre G, Veiga-da-Cunha M, Vertommen D, Buysschaert M, Van Schaftingen E. Variability in erythrocyte fructosamine 3-kinase activity in humans correlates with polymorphisms in the FN3K gene and impacts on haemoglobin glycation at specific sites. Diabetes Metab 2006;32:31-9.
    • (2006) Diabetes Metab , vol.32 , pp. 31-39
    • Delpierre, G.1    Veiga-Da-Cunha, M.2    Vertommen, D.3    Buysschaert, M.4    Van Schaftingen, E.5
  • 28
    • 77949505266 scopus 로고    scopus 로고
    • A polymorphism within the Fructosamine-3-kinase gene is associated with HbA1c levels and the onset of type 2 diabetes mellitus
    • Mohás M, Kisfali P, Baricza E, Mérei A, Maász A, Cseh J, et al. A polymorphism within the Fructosamine-3-kinase gene is associated with HbA1c levels and the onset of type 2 diabetes mellitus. Exp Clin Endocrinol Diabetes 2010;118:209-12.
    • (2010) Exp Clin Endocrinol Diabetes , vol.118 , pp. 209-212
    • Mohás, M.1    Kisfali, P.2    Baricza, E.3    Mérei, A.4    Maász, A.5    Cseh, J.6
  • 29
    • 84891427717 scopus 로고    scopus 로고
    • Genetic variability in enzymes of methabolic pathways conferring protection against non-enzymatic glycation versus diabetes-related morbidity and mortality
    • Tanhäuserová V, Kuricová K, Pácal L, Bartáková V, Rehoová J, Svojanovský J, et al. Genetic variability in enzymes of methabolic pathways conferring protection against non-enzymatic glycation versus diabetes-related morbidity and mortality. Clin Chem Lab Med 2014;52:77-83.
    • (2014) Clin Chem Lab Med , vol.52 , pp. 77-83
    • Tanhäuserová, V.1    Kuricová, K.2    Pácal, L.3    Bartáková, V.4    Rehoová, J.5    Svojanovský, J.6
  • 30
    • 84903787124 scopus 로고    scopus 로고
    • Fructosamine 3-kinase and glyoxalase i polymorphisms and their association with soluble RAGE and adhesion molecules in diabetes
    • Skrha JJr, Muravská A, Fleka M, Horová E, Novák J, Novotný A, et al. Fructosamine 3-kinase and glyoxalase I polymorphisms and their association with soluble RAGE and adhesion molecules in diabetes. Phisiol Res 2014;63:S283-91.
    • (2014) Phisiol Res , vol.63 , pp. S283-S291
    • Skrha, J.1    Muravská, A.2    Fleka, M.3    Horová, E.4    Novák, J.5    Novotný, A.6
  • 32
    • 77954407332 scopus 로고    scopus 로고
    • Genomewide association studies and assessment of the risk of disease
    • Manolio TA. Genomewide association studies and assessment of the risk of disease. N Engl J Med 2010;362:166-76.
    • (2010) N Engl J Med , vol.362 , pp. 166-176
    • Manolio, T.A.1
  • 33
    • 78649461131 scopus 로고    scopus 로고
    • Common genetic variants at 10 genomic loci influence hemoglobin A1c levels via glycemic and nonglycemic pathways
    • Soranzo N, Senna S, Wheeler E, Gieger C, Radke D, Dupuis J, et al. Common genetic variants at 10 genomic loci influence hemoglobin A1c levels via glycemic and nonglycemic pathways. Diabetes 2010;59:3229-39.
    • (2010) Diabetes , vol.59 , pp. 3229-3239
    • Soranzo, N.1    Senna, S.2    Wheeler, E.3    Gieger, C.4    Radke, D.5    Dupuis, J.6
  • 34
    • 84903146362 scopus 로고    scopus 로고
    • Multiple nonglycemic genomic loci are newly associated with blood level of glycated hemoglobin in East Asians
    • Chen P, Takeuchi F, Lee JY, Li H, Wu JY, Liang J. Multiple nonglycemic genomic loci are newly associated with blood level of glycated hemoglobin in East Asians. Diabetes 2014;63:2551-62.
    • (2014) Diabetes , vol.63 , pp. 2551-2562
    • Chen, P.1    Takeuchi, F.2    Lee, J.Y.3    Li, H.4    Wu, J.Y.5    Liang, J.6
  • 35
    • 84923362619 scopus 로고    scopus 로고
    • Integrative analysis of 111 reference human epigenomes
    • Roadmap Epigenomics Consortium
    • Roadmap Epigenomics Consortium, Kundaje A, Meuleman W, Ernst J, Bilenky M, Yen A, et al. Integrative analysis of 111 reference human epigenomes. Nature 2015;518:317-30.
    • (2015) Nature , vol.518 , pp. 317-330
    • Kundaje, A.1    Meuleman, W.2    Ernst, J.3    Bilenky, M.4    Yen, A.5
  • 36
    • 84888321284 scopus 로고    scopus 로고
    • Genetics of diabetes-Are we missing the genes or the disease
    • Groop L, Flemming P. Genetics of diabetes-Are we missing the genes or the disease? Mol Cell Endocrinol 2014;382:726-39.
    • (2014) Mol Cell Endocrinol , vol.382 , pp. 726-739
    • Groop, L.1    Flemming, P.2
  • 38
    • 0035134867 scopus 로고    scopus 로고
    • Effects of haemoglobin variants and chemically modified derivatives on assays for glycohaemoglobin
    • Bry L, Chen PC, Sacks DB. Effects of haemoglobin variants and chemically modified derivatives on assays for glycohaemoglobin. Clin Chem 2001;47:153-63.
    • (2001) Clin Chem , vol.47 , pp. 153-163
    • Bry, L.1    Chen, P.C.2    Sacks, D.B.3
  • 39
    • 79955945923 scopus 로고    scopus 로고
    • Glyoxalase in diabetes, obesity and related disorders
    • Rabbani N, Thornalley PJ. Glyoxalase in diabetes, obesity and related disorders. Semin Cell Dev Biol 2011;22:309-17.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 309-317
    • Rabbani, N.1    Thornalley, P.J.2
  • 40
    • 77953039361 scopus 로고    scopus 로고
    • Biologic variability in plasma glucose, hemoglobin A1c and advanced glycation end products associated with diabetes complications
    • Leslie RD, Cohen RM. Biologic variability in plasma glucose, hemoglobin A1c and advanced glycation end products associated with diabetes complications. J Diabetes Sci Technol 2009;3:635-43.
    • (2009) J Diabetes Sci Technol , vol.3 , pp. 635-643
    • Leslie, R.D.1    Cohen, R.M.2
  • 41
    • 54049105337 scopus 로고    scopus 로고
    • Frequency of HbA1c discordance in estimating blood glucose control
    • Cohen RM, Smith EP. Frequency of HbA1c discordance in estimating blood glucose control. Curr Opin Clin Nutr Metab Care 2008;11:512-7.
    • (2008) Curr Opin Clin Nutr Metab Care , vol.11 , pp. 512-517
    • Cohen, R.M.1    Smith, E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.