메뉴 건너뛰기




Volumn 181, Issue 1-2, 1998, Pages 63-69

Non-enzymatic glycosylation of alkaline phosphatase alters its biological properties

Author keywords

Advanced glycation end products; Alkaline phosphatase; Amadori products; Non enzymatic glycosylation

Indexed keywords

ALKALINE PHOSPHATASE; AMINOGUANIDINE; FRUCTOSAMINE; INTESTINE ENZYME; MEMBRANE ENZYME;

EID: 0031932433     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006857309142     Document Type: Article
Times cited : (30)

References (34)
  • 1
    • 0027913005 scopus 로고
    • Glycosylation non-enzymatique des protéines
    • Monnier V: Glycosylation non-enzymatique des protéines. La Presse Médicale 22: 1413-1418, 1993
    • (1993) La Presse Médicale , vol.22 , pp. 1413-1418
    • Monnier, V.1
  • 2
    • 0028272883 scopus 로고
    • Pathogenic effects of advanced glycosylation: Biochemical, biologic, and clinical implications for diabetes and aging
    • Vlassara H, Bucala R, Striker L: Pathogenic effects of advanced glycosylation: Biochemical, biologic, and clinical implications for diabetes and aging. Lab Invest 70: 138-151, 1994
    • (1994) Lab Invest , vol.70 , pp. 138-151
    • Vlassara, H.1    Bucala, R.2    Striker, L.3
  • 3
    • 0025906718 scopus 로고
    • Glycosylation products as toxic mediators of diabetic complications
    • Brownlee M: Glycosylation products as toxic mediators of diabetic complications. Ann Rev Med 42: 159-166, 1991
    • (1991) Ann Rev Med , vol.42 , pp. 159-166
    • Brownlee, M.1
  • 4
    • 0027097908 scopus 로고
    • Role of glycation in aging
    • Lee AT, Cerami A: Role of glycation in aging. Ann NY Acad Sci 663: 63-69, 1992
    • (1992) Ann NY Acad Sci , vol.663 , pp. 63-69
    • Lee, A.T.1    Cerami, A.2
  • 5
    • 0023923007 scopus 로고
    • Glycation of low density lipoproteins enhances cholesteryl ester synthesis in human monocyte-derivedmacrophages
    • Lopes-Virella MF, Klein RL, Lyons TJ, Stevenson HC: Glycation of low density lipoproteins enhances cholesteryl ester synthesis in human monocyte-derivedmacrophages. Diabetes 37: 550-557, 1988
    • (1988) Diabetes , vol.37 , pp. 550-557
    • Lopes-Virella, M.F.1    Klein, R.L.2    Lyons, T.J.3    Stevenson, H.C.4
  • 6
    • 0020789178 scopus 로고
    • Non-enzymatic glycosylation reduces the susceptibility of fibrin to degradation by plasmin
    • Brownlee M, Vlassara H, Cerami A: Non-enzymatic glycosylation reduces the susceptibility of fibrin to degradation by plasmin. Diabetes 32: 680-684, 1983
    • (1983) Diabetes , vol.32 , pp. 680-684
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 7
    • 0021365056 scopus 로고
    • Non-enzymatic glycation of human serum albumin alters its conformation and function
    • Shaklai N, Garlick RL, Bunn HF: Non-enzymatic glycation of human serum albumin alters its conformation and function. J Biol Chem 259: 3812-3817, 1984
    • (1984) J Biol Chem , vol.259 , pp. 3812-3817
    • Shaklai, N.1    Garlick, R.L.2    Bunn, H.F.3
  • 8
    • 0028977862 scopus 로고
    • Changes induced by non-enzymatic glycosylation of IGF-binding protein-3: Effects on its binding properties and on its modulatory effect on IGF-I mitogenic action
    • Cortizo AM, Gagliardino JJ: Changes induced by non-enzymatic glycosylation of IGF-binding protein-3: Effects on its binding properties and on its modulatory effect on IGF-I mitogenic action. J Endocrinol 144: 119-126, 1995
    • (1995) J Endocrinol , vol.144 , pp. 119-126
    • Cortizo, A.M.1    Gagliardino, J.J.2
  • 9
    • 0018742775 scopus 로고
    • Functional properties of the glycosylated minor components of human adult hemoglobin
    • McDonald MJ, Bleichman M, Bunn HF, Noble RW: Functional properties of the glycosylated minor components of human adult hemoglobin. J Biol Chem 254: 702-707, 1979
    • (1979) J Biol Chem , vol.254 , pp. 702-707
    • McDonald, M.J.1    Bleichman, M.2    Bunn, H.F.3    Noble, R.W.4
  • 11
    • 0001430544 scopus 로고
    • Accelerated age-related browning of human collagen in diabetes mellitus
    • Monnier VM, Kohn RR, Cerami A: Accelerated age-related browning of human collagen in diabetes mellitus. Proc Natl Acad Sci USA 81: 583-587, 1984
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 583-587
    • Monnier, V.M.1    Kohn, R.R.2    Cerami, A.3
  • 12
    • 0021816278 scopus 로고
    • Recognition and uptake of human diabetic peripheral nerve myelin by macrophages
    • Vlassara H, Brownlee M, Cerami A: Recognition and uptake of human diabetic peripheral nerve myelin by macrophages. Diabetes 34: 553-557, 1985
    • (1985) Diabetes , vol.34 , pp. 553-557
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 15
    • 0028099997 scopus 로고
    • Interpretation and clinical significance of alkaline phosphatase isoenzyme patterns
    • Van Hoof VO, De Broe ME: Interpretation and clinical significance of alkaline phosphatase isoenzyme patterns. CR in Clinical Lab Sci 31: 197-293, 1994
    • (1994) CR in Clinical Lab Sci , vol.31 , pp. 197-293
    • Van Hoof, V.O.1    De Broe, M.E.2
  • 16
    • 0019328958 scopus 로고
    • Role of phosphatidylinositol in attachment of alkaline phosphatase to membranes
    • Low MG, Zilversmit DB: Role of phosphatidylinositol in attachment of alkaline phosphatase to membranes. Biochemistry 19: 3913-3918, 1980
    • (1980) Biochemistry , vol.19 , pp. 3913-3918
    • Low, M.G.1    Zilversmit, D.B.2
  • 17
    • 0027930471 scopus 로고
    • ALP in hypophosphatasia
    • Whyte MP: ALP in hypophosphatasia. Endo Rev 15: 439-461, 1994
    • (1994) Endo Rev , vol.15 , pp. 439-461
    • Whyte, M.P.1
  • 18
    • 0015360187 scopus 로고
    • Phosphate absorption and alkaline phosphatase activity in the small intestine of the adult mouse and of the chick embryo and hatched chick
    • Moog F, Glazier HS: Phosphate absorption and alkaline phosphatase activity in the small intestine of the adult mouse and of the chick embryo and hatched chick. Com Biochem Physiol A 42: 321-336, 1972
    • (1972) Com Biochem Physiol A , vol.42 , pp. 321-336
    • Moog, F.1    Glazier, H.S.2
  • 19
    • 0019415250 scopus 로고
    • Renal transport of phosphate: Role of alkaline phosphatase
    • Petitclerc C, Plante GE: Renal transport of phosphate: Role of alkaline phosphatase. Can J Physiol Pharmacol 59: 311-323, 1981
    • (1981) Can J Physiol Pharmacol , vol.59 , pp. 311-323
    • Petitclerc, C.1    Plante, G.E.2
  • 20
    • 0005847765 scopus 로고
    • Glicosilación no enzimática de proteinas: Su roi en las complicaciones crónicas de la diabetes y el envejecimiento
    • McCarthy AD: Glicosilación no enzimática de proteinas: Su roi en las complicaciones crónicas de la diabetes y el envejecimiento. Acta Bioquímica Clínica Latinoamericana 29: 173-190, 1995
    • (1995) Acta Bioquímica Clínica Latinoamericana , vol.29 , pp. 173-190
    • McCarthy, A.D.1
  • 21
    • 0030942092 scopus 로고    scopus 로고
    • Effects of advanced glycation end-products on the proliferation and differentiation of osteoblast-like cells
    • McCarthy AD, Etcheverry SB, Bruzzone L, Cortizo AM: Effects of advanced glycation end-products on the proliferation and differentiation of osteoblast-like cells. Mol Cell Biochem 170: 43-51, 1997
    • (1997) Mol Cell Biochem , vol.170 , pp. 43-51
    • McCarthy, A.D.1    Etcheverry, S.B.2    Bruzzone, L.3    Cortizo, A.M.4
  • 22
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M: Rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 23
    • 0015366266 scopus 로고
    • Separation of isoenzymes of alkaline phosphatase by substrate-gel imprint after electrophoresis on cellulose acetate
    • Rhone DP, Mizuno F: Separation of isoenzymes of alkaline phosphatase by substrate-gel imprint after electrophoresis on cellulose acetate. Clin Chem 18: 662-665, 1972
    • (1972) Clin Chem , vol.18 , pp. 662-665
    • Rhone, D.P.1    Mizuno, F.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0026482265 scopus 로고
    • Advanced glycosylation: Chemistry, biology, and implications for diabetes and aging
    • Bucala R, Cerami A: Advanced glycosylation: Chemistry, biology, and implications for diabetes and aging. Adv Pharmacol 23: 1-34, 1992
    • (1992) Adv Pharmacol , vol.23 , pp. 1-34
    • Bucala, R.1    Cerami, A.2
  • 27
    • 0023803163 scopus 로고
    • Oncodevelopmental expression and structure of alkaline phosphatase genes
    • Millan JL: Oncodevelopmental expression and structure of alkaline phosphatase genes. Anticancer Res 8: 955-1004, 1988
    • (1988) Anticancer Res , vol.8 , pp. 955-1004
    • Millan, J.L.1
  • 28
    • 0003326347 scopus 로고
    • Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: Close homology to placental alkaline phosphatase
    • Henthorn PS, Rducha M, Edwards YH, Weiss MJ, Slaughter C, Lafferty MA, Harris H: Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: Close homology to placental alkaline phosphatase. Proc Natl Acad Sci USA 84: 12344-12348, 1987
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 12344-12348
    • Henthorn, P.S.1    Rducha, M.2    Edwards, Y.H.3    Weiss, M.J.4    Slaughter, C.5    Lafferty, M.A.6    Harris, H.7
  • 29
    • 0027452666 scopus 로고
    • Effect of dietary carbohydrate and phenotype on sucrase, maltase, lactase and alkaline phosphatase specific activity in SHR/N-cp rat
    • Wiesenfeld P, Baldwin J III, Szepesi B, Michaelis OEIV: Effect of dietary carbohydrate and phenotype on sucrase, maltase, lactase and alkaline phosphatase specific activity in SHR/N-cp rat. Proc Soc Exp Biol Med 202 (3): 338-344, 1993
    • (1993) Proc Soc Exp Biol Med , vol.202 , Issue.3 , pp. 338-344
    • Wiesenfeld, P.1    Baldwin III, J.2    Szepesi, B.3    Michaelis IV, O.E.4
  • 30
    • 0018861310 scopus 로고
    • Effect of food intake on intestinal absorption and mucosal hydrolases in alloxan diabetic rats
    • Nakabou Y, Ishikawa Y, Misake A, Hagihira H: Effect of food intake on intestinal absorption and mucosal hydrolases in alloxan diabetic rats. Metabolism 29 (2): 181-185, 1980
    • (1980) Metabolism , vol.29 , Issue.2 , pp. 181-185
    • Nakabou, Y.1    Ishikawa, Y.2    Misake, A.3    Hagihira, H.4
  • 31
    • 0025147705 scopus 로고
    • Translocation of intestinal alkaline phosphatase in streptozotocin-induced diabetic rats
    • Unakami S, Komoda T, Sakagishi Y: Translocation of intestinal alkaline phosphatase in streptozotocin-induced diabetic rats. Int J Biochem 22 (11): 1325-1331, 1990
    • (1990) Int J Biochem , vol.22 , Issue.11 , pp. 1325-1331
    • Unakami, S.1    Komoda, T.2    Sakagishi, Y.3
  • 32
    • 0019849147 scopus 로고
    • Alkaline phosphatase activity in chronic streptozotocin-induced insulin deficiency in the rat: Effect of insulin replacement
    • Hough S, Avioli LV, Tietelbaum SL, Fallon MD: Alkaline phosphatase activity in chronic streptozotocin-induced insulin deficiency in the rat: Effect of insulin replacement. Metabolism 30 (12): 1190-1194, 1981
    • (1981) Metabolism , vol.30 , Issue.12 , pp. 1190-1194
    • Hough, S.1    Avioli, L.V.2    Tietelbaum, S.L.3    Fallon, M.D.4
  • 33
    • 0029086328 scopus 로고
    • Advanced glycosylation end products in diabetic complications: Biochemical basis and prospects for therapeutic intervention
    • Bucala R, Cerami A, Vlassara H: Advanced glycosylation end products in diabetic complications: Biochemical basis and prospects for therapeutic intervention. Diabetes Rev 3: 258-268, 1995
    • (1995) Diabetes Rev , vol.3 , pp. 258-268
    • Bucala, R.1    Cerami, A.2    Vlassara, H.3
  • 34
    • 6844248331 scopus 로고
    • Coma hiperosmolar no cetósico
    • M Ruiz (ed). Editorial Akadia
    • Ruiz JV, Traversa M: Coma hiperosmolar no cetósico. In: M Ruiz (ed). Diabetes Mellitus, 2nd edn, Editorial Akadia, 1994, pp 330-341
    • (1994) Diabetes Mellitus, 2nd Edn , pp. 330-341
    • Ruiz, J.V.1    Traversa, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.