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Volumn 45, Issue 11, 1996, Pages 1489-1496

Glycation of insulin in the islets of Langerhans of normal and diabetic animals

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; DIABETES MELLITUS; GLUCOSE BLOOD LEVEL; GLYCATION; GLYCOSYLATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYPERGLYCEMIA; INSULIN RESISTANCE; LIPOGENESIS; MOUSE; NONHUMAN; PANCREAS ISLET CELL; PRIORITY JOURNAL; RADIOIMMUNOASSAY; STREPTOZOCIN DIABETES;

EID: 0029909202     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diab.45.11.1489     Document Type: Article
Times cited : (81)

References (31)
  • 1
    • 0026443080 scopus 로고
    • Nonenzymatic glycation of type I collagen
    • Reiser KM, Amigable MA, Last JA: Nonenzymatic glycation of type I collagen. J Biol Chem 267:24207-24216,1992
    • (1992) J Biol Chem , vol.267 , pp. 24207-24216
    • Reiser, K.M.1    Amigable, M.A.2    Last, J.A.3
  • 2
    • 0023655983 scopus 로고
    • Conformational changes induced in lens α- And γ-crystallins by modification with glucose 6-phosphate
    • Beswick HT, Harding JJ: Conformational changes induced in lens α- and γ-crystallins by modification with glucose 6-phosphate. Biochem J 246:761-769,1987
    • (1987) Biochem J , vol.246 , pp. 761-769
    • Beswick, H.T.1    Harding, J.J.2
  • 4
    • 0026701935 scopus 로고
    • Nonenzymatic glycosylation of macromolecules
    • Brownlee M: Nonenzymatic glycosylation of macromolecules. Diabetes 41 (Suppl. 2):57-60,1992
    • (1992) Diabetes , vol.41 , Issue.2 SUPPL. , pp. 57-60
    • Brownlee, M.1
  • 5
    • 0002602893 scopus 로고
    • Nonenzymatic glycosylation: Role in the pathogenesis of diabetic complications
    • Vlassara H, Brownlee M, Cerami A: Nonenzymatic glycosylation: role in the pathogenesis of diabetic complications. Clin Chem 32:37-41,1986
    • (1986) Clin Chem , vol.32 , pp. 37-41
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 6
    • 85035173373 scopus 로고    scopus 로고
    • Identification of the site of glycation of human insulin
    • In press
    • O'Harte FPM, Højrup P, Flatt PR: Identification of the site of glycation of human insulin. Peptides. In press
    • Peptides
    • O'Harte, F.P.M.1    Højrup, P.2    Flatt, P.R.3
  • 7
    • 0018387812 scopus 로고
    • Preparation and biological properties of glycosylated insulin
    • Dolhofer R, Wieland OH: Preparation and biological properties of glycosylated insulin. FEBS Lett 100:133-136,1979
    • (1979) FEBS Lett , vol.100 , pp. 133-136
    • Dolhofer, R.1    Wieland, O.H.2
  • 10
    • 0006257572 scopus 로고
    • Animal models of diabetes
    • Nattrass M, Ed. Edinburgh, Churchill Livingstone
    • Bailey CJ, Flatt PR: Animal models of diabetes. In Recent Advances in Diabetes. Vol. 2. Nattrass M, Ed. Edinburgh, Churchill Livingstone, 1986, p. 71-89
    • (1986) Recent Advances in Diabetes , vol.2 , pp. 71-89
    • Bailey, C.J.1    Flatt, P.R.2
  • 12
    • 0023002651 scopus 로고
    • Measurement of glycosylated hemoglobin and glycosylated plasma proteins in animal models with diabetes or inappropriate hypoglycemia
    • Gould BJ, Flatt PR, Kotecha S, Collett S, Swanston-Flatt SK: Measurement of glycosylated hemoglobin and glycosylated plasma proteins in animal models with diabetes or inappropriate hypoglycemia. Horm Metab Res 18:7915-799,1986
    • (1986) Horm Metab Res , vol.18 , pp. 7915-8799
    • Gould, B.J.1    Flatt, P.R.2    Kotecha, S.3    Collett, S.4    Swanston-Flatt, S.K.5
  • 13
    • 0019817187 scopus 로고
    • Iodination of proteins, glycoproteins and peptides, using a solid phase oxidizing agent: 1,3,4,6-tetrachloro-3α,6α-diphenylglycouril (Iodogen)
    • Salicinski PRP, McLean C, Sykes JEC, Clement-Jones W, Lowry PJ: Iodination of proteins, glycoproteins and peptides, using a solid phase oxidizing agent: 1,3,4,6-tetrachloro-3α,6α-diphenylglycouril (Iodogen). Ann Biochem 117:136-146,1981
    • (1981) Ann Biochem , vol.117 , pp. 136-146
    • Salicinski, P.R.P.1    McLean, C.2    Sykes, J.E.C.3    Clement-Jones, W.4    Lowry, P.J.5
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal Biochem 72:248-254,1976
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0022919166 scopus 로고
    • High performance liquid chromatography (HPLC): A rapid, flexible and sensitive method for separating islet proinsulin and insulin
    • Halban PA, Rhodes CJ, Shoelson SE: High performance liquid chromatography (HPLC): a rapid, flexible and sensitive method for separating islet proinsulin and insulin. Diabetologia 29:893-896,1989
    • (1989) Diabetologia , vol.29 , pp. 893-896
    • Halban, P.A.1    Rhodes, C.J.2    Shoelson, S.E.3
  • 16
    • 0027185223 scopus 로고
    • Novel, non-crinophagic degradation of connecting peptide in transformed pancreatic beta cells
    • Neerman-Arbez M, Halban PA: Novel, non-crinophagic degradation of connecting peptide in transformed pancreatic beta cells. J Biol Chem 268:16248-16252,1993
    • (1993) J Biol Chem , vol.268 , pp. 16248-16252
    • Neerman-Arbez, M.1    Halban, P.A.2
  • 17
    • 0019471997 scopus 로고
    • Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice
    • Flatt PR, Bailey CJ: Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice. Diabetologia 20:573-577,1981
    • (1981) Diabetologia , vol.20 , pp. 573-577
    • Flatt, P.R.1    Bailey, C.J.2
  • 18
    • 0001360932 scopus 로고
    • Determination of glucose by automatic analyzer
    • Stevens VJ: Determination of glucose by automatic analyzer. Clin Chem 32:9199-9201,1971
    • (1971) Clin Chem , vol.32 , pp. 9199-9201
    • Stevens, V.J.1
  • 19
    • 0027389774 scopus 로고
    • Increased proinsulin/insulin ratio in pancreas extracts of hyperglycemic rats
    • Leahy JL: Increased proinsulin/insulin ratio in pancreas extracts of hyperglycemic rats. Diabetes 42:22-27,1993
    • (1993) Diabetes , vol.42 , pp. 22-27
    • Leahy, J.L.1
  • 20
    • 0020086017 scopus 로고
    • Influence of genetic background and age on the expression of the obese hyperglycaemic syndrome in Aston ob/ob mice
    • Bailey CJ, Flatt PR, Atkins TW: Influence of genetic background and age on the expression of the obese hyperglycaemic syndrome in Aston ob/ob mice. Int J Obesity 6:11-21,1980
    • (1980) Int J Obesity , vol.6 , pp. 11-21
    • Bailey, C.J.1    Flatt, P.R.2    Atkins, T.W.3
  • 21
    • 85035172109 scopus 로고    scopus 로고
    • Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture
    • In press
    • Abdel-Wahab YHA, O'Harte FPM, Barnett CR, Flatt PR: Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture. J Endocrinol. In press
    • J Endocrinol
    • Abdel-Wahab, Y.H.A.1    O'Harte, F.P.M.2    Barnett, C.R.3    Flatt, P.R.4
  • 23
    • 0023692118 scopus 로고
    • Cloning and functional expression in bacteria of a novel glucose transporter present in liver, intestine, kidney and β-pancreatic islet cells
    • Thorens B, Sarkar HK, Kaback HR, Lodish HF: Cloning and functional expression in bacteria of a novel glucose transporter present in liver, intestine, kidney and β-pancreatic islet cells. Cell 55:281-290,1988
    • (1988) Cell , vol.55 , pp. 281-290
    • Thorens, B.1    Sarkar, H.K.2    Kaback, H.R.3    Lodish, H.F.4
  • 24
    • 0002185449 scopus 로고
    • Glucokinase: Signal recognition enzyme for glucose-induced insulin secretion
    • Flatt PR, Ed. London, Portland Press
    • Lenzen S: Glucokinase: signal recognition enzyme for glucose-induced insulin secretion. In Nutrient Regulation of Insulin Secretion. Flatt PR, Ed. London, Portland Press, 1992, p. 101-124
    • (1992) Nutrient Regulation of Insulin Secretion , pp. 101-124
    • Lenzen, S.1
  • 25
    • 0027193121 scopus 로고
    • Identification, purification and genetic deficiencies of the glucose-6-phosphatase system transport proteins
    • Waddell ID, Burchell A: Identification, purification and genetic deficiencies of the glucose-6-phosphatase system transport proteins. Eur J Pediatr 152 (Suppl. 1):S14-S17,1993
    • (1993) Eur J Pediatr , vol.152 , Issue.1 SUPPL.
    • Waddell, I.D.1    Burchell, A.2
  • 26
    • 0017834059 scopus 로고
    • In vitro glycosylation of haemoglobin by different sugars and sugar phosphates
    • Dolhofer R, Wieland OH: In vitro glycosylation of haemoglobin by different sugars and sugar phosphates. FEBS Lett 85:86-90,1978
    • (1978) FEBS Lett , vol.85 , pp. 86-90
    • Dolhofer, R.1    Wieland, O.H.2
  • 28
    • 0027937185 scopus 로고
    • Proinsulin processing in the regulated and the constitutive secretory pathway
    • Halban P: Proinsulin processing in the regulated and the constitutive secretory pathway. Diabetologia 37 (Suppl. 2):S65-S72,1994
    • (1994) Diabetologia , vol.37 , Issue.2 SUPPL.
    • Halban, P.1
  • 29
    • 0027941219 scopus 로고
    • The pathogenesis of NIDDM
    • Hales CN: The pathogenesis of NIDDM. Diabetologia 37 (Suppl. 2):S162-S168,1994
    • (1994) Diabetologia , vol.37 , Issue.2 SUPPL.
    • Hales, C.N.1
  • 31
    • 0028230040 scopus 로고
    • What β-cell defect could lead to hyperproinsulinemia in NIDDM?
    • Rhodes CJ, Alarcon C: What β-cell defect could lead to hyperproinsulinemia in NIDDM? Diabetes 43:511-517,1994
    • (1994) Diabetes , vol.43 , pp. 511-517
    • Rhodes, C.J.1    Alarcon, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.