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Volumn 524, Issue , 2003, Pages 303-312

Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both involved in regulating the metabolic stability of glucagon-like peptide-1 in vivo

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; GLUCAGON LIKE PEPTIDE 1; MEMBRANE METALLOENDOPEPTIDASE;

EID: 0037687745     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (17)

References (43)
  • 1
    • 0022971804 scopus 로고
    • Glucagon-like peptides GLP-1 and GLP-2, predicted products of the glucagon gene, are secreted separately from pig small intestine but not pancreas
    • Ørskov, C., Holst, J.J., Knuhtsen, S., Baldissera, F.G., Poulsen, S.S., and Nielsen, O.V., 1986, Glucagon-like peptides GLP-1 and GLP-2, predicted products of the glucagon gene, are secreted separately from pig small intestine but not pancreas. Endocrinology 119: 1467-1475
    • (1986) Endocrinology , vol.119 , pp. 1467-1475
    • Ørskov, C.1    Holst, J.J.2    Knuhtsen, S.3    Baldissera, F.G.4    Poulsen, S.S.5    Nielsen, O.V.6
  • 2
    • 0023008693 scopus 로고
    • Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing
    • Mojsov, S., Heinrich, G., Wilson, I.B., Ravazzola, M., Orci, L., and Habener, J.F., 1986, Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing. J Biol Chem 261: 11880-11889
    • (1986) J Biol Chem , vol.261 , pp. 11880-11889
    • Mojsov, S.1    Heinrich, G.2    Wilson, I.B.3    Ravazzola, M.4    Orci, L.5    Habener, J.F.6
  • 3
    • 0027227370 scopus 로고
    • Glucagon-like peptide-1 (7-36)amide and glucose-dependent insulinotropic polypeptide secretion in response to nutrient ingestion in man: Acute post-prandial and 24-h secretion patterns
    • Elliott, R.M., Morgan, L.M., Tredger, J.A., Deacon, S., Wright, J., and Marks, V., 1993, Glucagon-like peptide-1 (7-36)amide and glucose-dependent insulinotropic polypeptide secretion in response to nutrient ingestion in man: acute post-prandial and 24-h secretion patterns. Endocrinology 138: 159-166
    • (1993) Endocrinology , vol.138 , pp. 159-166
    • Elliott, R.M.1    Morgan, L.M.2    Tredger, J.A.3    Deacon, S.4    Wright, J.5    Marks, V.6
  • 4
    • 0026775150 scopus 로고
    • Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1
    • Thorens, B., 1992, Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1. Proc Natl Acad Sci U S A 89: 8641-8645
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8641-8645
    • Thorens, B.1
  • 5
    • 0028198851 scopus 로고
    • Structure-activity studies og glucagon-like peptide-1
    • Adelhorst, K., Hedegaard, B.B., Knudsen, L.B., and Kirk, O., 1994, Structure-activity studies og glucagon-like peptide-1. J Biol Chem 269: 6275-6278
    • (1994) J Biol Chem , vol.269 , pp. 6275-6278
    • Adelhorst, K.1    Hedegaard, B.B.2    Knudsen, L.B.3    Kirk, O.4
  • 6
    • 0023758530 scopus 로고
    • Effect of truncated glucagon-like peptide-1 [proglucagon-(78-107)amide] on endocrine secretion from pig pancreas, antrum and non-antral stomach
    • Ørskov, C., Holst, J.J., and Nielsen, O.V., 1988, Effect of truncated glucagon-like peptide-1 [proglucagon-(78-107)amide] on endocrine secretion from pig pancreas, antrum and non-antral stomach. Endocrinology 123: 2009-2013
    • (1988) Endocrinology , vol.123 , pp. 2009-2013
    • Ørskov, C.1    Holst, J.J.2    Nielsen, O.V.3
  • 7
    • 0024515406 scopus 로고
    • Glucagon-like peptide I (7-37) actions on the endocrine pancreas
    • Weir, G.C., Mojsov, S., Hendrick, G.K., and Habener, J.F., 1989, Glucagon-like peptide I (7-37) actions on the endocrine pancreas. Diabetes 38: 338-342
    • (1989) Diabetes , vol.38 , pp. 338-342
    • Weir, G.C.1    Mojsov, S.2    Hendrick, G.K.3    Habener, J.F.4
  • 8
    • 0344357096 scopus 로고
    • Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in rat islet cell line
    • Drucker, D.J., Philippe, J., Mojsov, S., Chick, W.L., and Habener, J.F., 1987, Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in rat islet cell line. Proc Natl Acad Sci USA 84: 3434-3438
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3434-3438
    • Drucker, D.J.1    Philippe, J.2    Mojsov, S.3    Chick, W.L.4    Habener, J.F.5
  • 9
    • 0026535588 scopus 로고
    • Insulinotropic hormone glucagon-like peptide-I (7-37) stimulation of proinsulin gene expression and proinsulin biosynthesis in insulinoma βTC-1 cells
    • Fehmann, H.C., and Habener, J.F., 1992, Insulinotropic hormone glucagon-like peptide-I (7-37) stimulation of proinsulin gene expression and proinsulin biosynthesis in insulinoma βTC-1 cells. Endocrinology 130: 159-166
    • (1992) Endocrinology , vol.130 , pp. 159-166
    • Fehmann, H.C.1    Habener, J.F.2
  • 10
    • 0027473729 scopus 로고
    • Pancreatic beta cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1 (7-36)
    • Holz, G.G., Kühtreiber, W.M., and Habener, J.F., 1993, Pancreatic beta cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1 (7-36). Nature 361: 362-365
    • (1993) Nature , vol.361 , pp. 362-365
    • Holz, G.G.1    Kühtreiber, W.M.2    Habener, J.F.3
  • 11
    • 0031820844 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 improves the ability of the beta-cell to sense and respond to glucose in subjects with impaired glucose tolerance
    • Byrne, M.M., Gliem, K., Wank, U., Arnold, R., Katschinski, M., Polonsky, K.S., and Göke, B., 1998, Glucagon-like peptide 1 improves the ability of the beta-cell to sense and respond to glucose in subjects with impaired glucose tolerance. Diabetes 47: 1259-1265
    • (1998) Diabetes , vol.47 , pp. 1259-1265
    • Byrne, M.M.1    Gliem, K.2    Wank, U.3    Arnold, R.4    Katschinski, M.5    Polonsky, K.S.6    Göke, B.7
  • 12
    • 0032908809 scopus 로고    scopus 로고
    • Initiation of increased pancreatic islet growth in young normoglycemic mice (Umeå +/?)
    • Edvell, A., and Lindström, P., 1999 Initiation of increased pancreatic islet growth in young normoglycemic mice (Umeå +/?). Endocrinology 140: 778-783
    • (1999) Endocrinology , vol.140 , pp. 778-783
    • Edvell, A.1    Lindström, P.2
  • 13
    • 0001592657 scopus 로고    scopus 로고
    • Activation of GLP-1 receptor signalling is coupled to inhibition of apoptosis in heterologous cell types
    • abstract
    • Hansotia, T., Yusta, B., and Drucker, D.J., 2001, Activation of GLP-1 receptor signalling is coupled to inhibition of apoptosis in heterologous cell types. Diabetes 50 (Suppl 2): A350 (abstract)
    • (2001) Diabetes , vol.50 , Issue.SUPPL. 2
    • Hansotia, T.1    Yusta, B.2    Drucker, D.J.3
  • 15
    • 0034011021 scopus 로고    scopus 로고
    • The effect of glucagon-like peptide-1 on energy expenditure and substrate metabolism in humans
    • Flint, A., Raben, A., Rehfeld, J.F., Holst, J.J., and Astrup, A., 2000, The effect of glucagon-like peptide-1 on energy expenditure and substrate metabolism in humans. Int J Obes Relat Metab Disord 24: 288-298
    • (2000) Int J Obes Relat Metab Disord , vol.24 , pp. 288-298
    • Flint, A.1    Raben, A.2    Rehfeld, J.F.3    Holst, J.J.4    Astrup, A.5
  • 16
    • 0035432607 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 infusion must be maintained for 24 h/day to obtain acceptable glycemia in type 2 diabetic patients who are poorly controlled on sulphonylurea treatment
    • Larsen, J., Hylleberg, B., Ng, K., and Damsbo, P., 2001, Glucagon-like peptide-1 infusion must be maintained for 24 h/day to obtain acceptable glycemia in type 2 diabetic patients who are poorly controlled on sulphonylurea treatment. Diabetes Care 24: 1416-1421
    • (2001) Diabetes Care , vol.24 , pp. 1416-1421
    • Larsen, J.1    Hylleberg, B.2    Ng, K.3    Damsbo, P.4
  • 17
    • 0027248866 scopus 로고
    • Normalization of fasting hyperglycemia by exogenous GLP-1 (7-36amide) in type 2 diabetic patients
    • Nauck, M.A., Kleine, N., Ørskov, C., Holst, J.J., Willms, B., and Creutzfeldt, W., 1993, Normalization of fasting hyperglycemia by exogenous GLP-1 (7-36amide) in type 2 diabetic patients. Diabetologia 36: 741-744
    • (1993) Diabetologia , vol.36 , pp. 741-744
    • Nauck, M.A.1    Kleine, N.2    Ørskov, C.3    Holst, J.J.4    Willms, B.5    Creutzfeldt, W.6
  • 19
    • 0031033531 scopus 로고    scopus 로고
    • Near-normalisation of diurnal glucose concentrations by continuous administration of glucagon-like peptide-1 (GLP-1) in subjects with NIDDM
    • Rachman, J., Barrow, B.A., Levy, J.C., and Turner, R.C., 1997, Near-normalisation of diurnal glucose concentrations by continuous administration of glucagon-like peptide-1 (GLP-1) in subjects with NIDDM. Diabetologia 40: 205-211
    • (1997) Diabetologia , vol.40 , pp. 205-211
    • Rachman, J.1    Barrow, B.A.2    Levy, J.C.3    Turner, R.C.4
  • 20
    • 0029857454 scopus 로고    scopus 로고
    • The antidiabetogenic effect of GLP-1 is maintained during a 7-day treatment period and improves diabetic dyslipoproteinemia in NIDDM patients
    • Juntti-Berggren, L., Pigon, J., Karpe, F., Hamsten, A., Gutniak, M., Vignati, L., and Efendic, S., 1996, The antidiabetogenic effect of GLP-1 is maintained during a 7-day treatment period and improves diabetic dyslipoproteinemia in NIDDM patients. Diabetes Care 19: 1200-1206
    • (1996) Diabetes Care , vol.19 , pp. 1200-1206
    • Juntti-Berggren, L.1    Pigon, J.2    Karpe, F.3    Hamsten, A.4    Gutniak, M.5    Vignati, L.6    Efendic, S.7
  • 21
    • 0037045845 scopus 로고    scopus 로고
    • Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in type 2 diabetes: A parallel-group study
    • Zander M, Madsbad S, Madsen JL, Holst JJ., 2002, Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in type 2 diabetes: a parallel-group study. Lancet 359: 824-830
    • (2002) Lancet , vol.359 , pp. 824-830
    • Zander, M.1    Madsbad, S.2    Madsen, J.L.3    Holst, J.J.4
  • 22
    • 0029797540 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 undergoes differential tissue-specific metabolism in the anesthetized pig
    • Deacon, C.F., Pridal, L., Klarskov, L., Olesen, M, and Holst, J.J., 1996, Glucagon-like peptide-1 undergoes differential tissue-specific metabolism in the anesthetized pig. Am J Physiol 271: E458-E464
    • (1996) Am J Physiol , vol.271
    • Deacon, C.F.1    Pridal, L.2    Klarskov, L.3    Olesen, M.4    Holst, J.J.5
  • 23
    • 0027157849 scopus 로고
    • Biological effects and metabolic rates of glucagonlike peptide- 1 7-36 amide and glucagonlike peptide- 1 7-37 in healthy subjects are indistinguishable
    • Ørskov, C., wettergren, A., and Holst, J.J., 1993, Biological effects and metabolic rates of glucagonlike peptide- 1 7-36 amide and glucagonlike peptide- 1 7-37 in healthy subjects are indistinguishable. Diabetes 42: 658-661
    • (1993) Diabetes , vol.42 , pp. 658-661
    • Ørskov, C.1    Wettergren, A.2    Holst, J.J.3
  • 24
    • 0029118049 scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • Kieffer, T.J., McIntosh, C.H., and Pederson, R.A., 1995, Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology 136: 3585-3596
    • (1995) Endocrinology , vol.136 , pp. 3585-3596
    • Kieffer, T.J.1    McIntosh, C.H.2    Pederson, R.A.3
  • 25
    • 0002130372 scopus 로고
    • Analysis of the degradation of insulinotropin [GLP-1 (7-37)] in human plasma and production of degradation resistant analogs
    • abstract
    • Buckley, D.I., and Lundquist, P., 1992, Analysis of the degradation of insulinotropin [GLP-1 (7-37)] in human plasma and production of degradation resistant analogs. Regul Pept 40: 117 (abstract)
    • (1992) Regul Pept , vol.40 , pp. 117
    • Buckley, D.I.1    Lundquist, P.2
  • 26
    • 0027215348 scopus 로고
    • Dipeptidyl peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1 (7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein, R., Gallwitz, B. and Schmidt, W.E., 1993, Dipeptidyl peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1 (7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. 214: 829-835
    • (1993) Eur J Biochem , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 27
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26) - Role in the inactivation of regulatory peptides
    • Mentlein, R., 1999, Dipeptidyl-peptidase IV (CD26) - role in the inactivation of regulatory peptides. Regul Pept. 85: 9-24
    • (1999) Regul Pept , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 28
    • 0036081143 scopus 로고    scopus 로고
    • GLP-1 (9-36)amide reduces blood glucose in anesthetized pigs by a mechanism that does not involve insulin secretion
    • Deacon, C.F., Plamboeck, A., Møller, S., and Holst, J.J., 2002a, GLP-1 (9-36)amide reduces blood glucose in anesthetized pigs by a mechanism that does not involve insulin secretion. Am J Physiol 282: E873-E879
    • (2002) Am J Physiol , vol.282
    • Deacon, C.F.1    Plamboeck, A.2    Møller, S.3    Holst, J.J.4
  • 29
    • 0028953577 scopus 로고
    • Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide which is a major endogenous metabolite in vivo
    • Deacon, C.F., Johnsen, A.H., and Holst, J.J., 1995, Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide which is a major endogenous metabolite in vivo. J Clin Endocrinol Metab 80: 952-957
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 952-957
    • Deacon, C.F.1    Johnsen, A.H.2    Holst, J.J.3
  • 31
    • 0029111540 scopus 로고
    • Characterisation of the processing by human neutral endopeptidase 24.11 of GLP-1(7-36) amide and comparison of the substrate specificity of the enzyme for other glucagon-like peptides
    • Hupe-Sodmann, K., McGregor, G.P., Bridenbaugh, R., Göke, R., Göke, B., Thole, H., Zimmermann, B., and Voigt, K., 1995, Characterisation of the processing by human neutral endopeptidase 24.11 of GLP-1(7-36) amide and comparison of the substrate specificity of the enzyme for other glucagon-like peptides. Regul Pept. 58: 149-156.
    • (1995) Regul Pept , vol.58 , pp. 149-156
    • Hupe-Sodmann, K.1    McGregor, G.P.2    Bridenbaugh, R.3    Göke, R.4    Göke, B.5    Thole, H.6    Zimmermann, B.7    Voigt, K.8
  • 32
    • 0030758090 scopus 로고    scopus 로고
    • Endoproteolysis of glucagon-like peptide (GLP)-1 (7-36) amide by ectopeptidases in RINm5F cells
    • Hupe-Sodmann, K., Göke, R., Göke, B., Thole, H.H., Zimmermann, B., Voigt, K., and McGregor, G.P., 1997, Endoproteolysis of glucagon-like peptide (GLP)-1 (7-36) amide by ectopeptidases in RINm5F cells. Peptides 18: 625-632.
    • (1997) Peptides , vol.18 , pp. 625-632
    • Hupe-Sodmann, K.1    Göke, R.2    Göke, B.3    Thole, H.H.4    Zimmermann, B.5    Voigt, K.6    McGregor, G.P.7
  • 33
    • 0021853198 scopus 로고
    • An immunoradiometric assay for endopeptidase-24.11 shows it to be a widely distributed enzyme in pig tissues
    • Gee, N.S., Bowes, M.A., Buck, P., and Kenny, A.J., 1985, An immunoradiometric assay for endopeptidase-24.11 shows it to be a widely distributed enzyme in pig tissues. Biochem J 228: 119-126
    • (1985) Biochem J , vol.228 , pp. 119-126
    • Gee, N.S.1    Bowes, M.A.2    Buck, P.3    Kenny, A.J.4
  • 35
    • 0038200220 scopus 로고
    • Verfahren zur Herstellung neuer Inhibitoren der Dipeptidyl Peptidase IV. German Patent Application Number DD 296 075 A5
    • Neubert, K., Born, I., Faust, J., Heins, J., Barth, A., Demuth, H.U., Rahfeld, J.U., and Steinmetzer, T., 1983, Verfahren zur Herstellung neuer Inhibitoren der Dipeptidyl Peptidase IV. German Patent Application Number DD 296 075 A5
    • (1983)
    • Neubert, K.1    Born, I.2    Faust, J.3    Heins, J.4    Barth, A.5    Demuth, H.U.6    Rahfeld, J.U.7    Steinmetzer, T.8
  • 36
    • 0031916924 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide-1 in anesthetized pigs
    • Deacon, C.F., Hughes, T.E., and Holst, J.J., 1998, Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide-1 in anesthetized pigs. Diabetes 47: 764-769
    • (1998) Diabetes , vol.47 , pp. 764-769
    • Deacon, C.F.1    Hughes, T.E.2    Holst, J.J.3
  • 37
    • 0000135759 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 (7-36 amide) concentrations and improves oral glucose tolerance in obese Zucker rats
    • Balkan, B., Kwasnik, L., Miserendino, R., Holst, J.J., and Li, X., 1999, Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 (7-36 amide) concentrations and improves oral glucose tolerance in obese Zucker rats. Diabetologia 42: 1324-1331
    • (1999) Diabetologia , vol.42 , pp. 1324-1331
    • Balkan, B.1    Kwasnik, L.2    Miserendino, R.3    Holst, J.J.4    Li, X.5
  • 38
    • 0036188070 scopus 로고    scopus 로고
    • Preservation of active incretin hormones by inhibition of dipeptidyl peptidase IV suppresses meal-induced incretin secretion in dogs
    • Deacon, C.F., Wamberg, S., Bie, P., Hughes, T.E., and Holst, J.J., 2002b, Preservation of active incretin hormones by inhibition of dipeptidyl peptidase IV suppresses meal-induced incretin secretion in dogs. J Endocrinol 172: 355-362
    • (2002) J Endocrinol , vol.172 , pp. 355-362
    • Deacon, C.F.1    Wamberg, S.2    Bie, P.3    Hughes, T.E.4    Holst, J.J.5
  • 39
    • 0031870418 scopus 로고    scopus 로고
    • Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isuleucine thiazolidide
    • Pederson, R.A., White, H.A., Schlenzig D., Pauly, R.P., McIntosh, C.H., and Demuth, H.U., 1998, Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isuleucine thiazolidide. Diabetes 47: 1253-1258
    • (1998) Diabetes , vol.47 , pp. 1253-1258
    • Pederson, R.A.1    White, H.A.2    Schlenzig, D.3    Pauly, R.P.4    McIntosh, C.H.5    Demuth, H.U.6
  • 40
    • 0036228243 scopus 로고    scopus 로고
    • Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and beta-cell glucose responsiveness in VDF (fa/fa) Zucker rats
    • Pospisilik, J.A., Stafford, S.G., Demuth, H.U., Brownsey, R., Parkhouse, W., Finegood, D.T., McIntosh, C.H., and Pederson, R.A., 2002, Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and beta-cell glucose responsiveness in VDF (fa/fa) Zucker rats. Diabetes 51: 943-950
    • (2002) Diabetes , vol.51 , pp. 943-950
    • Pospisilik, J.A.1    Stafford, S.G.2    Demuth, H.U.3    Brownsey, R.4    Parkhouse, W.5    Finegood, D.T.6    McIntosh, C.H.7    Pederson, R.A.8
  • 41
    • 0036312876 scopus 로고    scopus 로고
    • Chronic inhibition of circulating dipeptidyl peptidase IV by FE 999011 delays the occurrence of diabetes in male zucker diabetic fatty rats
    • Sudre, B, Broqua, P., White, R.B., Ashworth, D., Evans, D.M., Haigh, R., Junien, J.L., and Aubert, M.L., 2002, Chronic inhibition of circulating dipeptidyl peptidase IV by FE 999011 delays the occurrence of diabetes in male zucker diabetic fatty rats. Diabetes 51: 1461-1469
    • (2002) Diabetes , vol.51 , pp. 1461-1469
    • Sudre, B.1    Broqua, P.2    White, R.B.3    Ashworth, D.4    Evans, D.M.5    Haigh, R.6    Junien, J.L.7    Aubert, M.L.8
  • 43
    • 0030845208 scopus 로고    scopus 로고
    • Formation and kinetics of the active drug candoxatrilat in mouse, rabbit, dog and man following administration of the prodrug candoxatril
    • Kaye, B., Brearley, C.J., Cussans, N.J., Herron, M., Humphrey, M.J., and Mollatt, A.R., 1997, Formation and kinetics of the active drug candoxatrilat in mouse, rabbit, dog and man following administration of the prodrug candoxatril. Xenobiotica 27: 1091-1102
    • (1997) Xenobiotica , vol.27 , pp. 1091-1102
    • Kaye, B.1    Brearley, C.J.2    Cussans, N.J.3    Herron, M.4    Humphrey, M.J.5    Mollatt, A.R.6


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