Effect of glycosylation on biodistribution of radiolabeled glucagon-like peptide 1

Annals of Nuclear Medicine

Volumn 26, Issue 2, 2012, Pages 184-191

  Watanabe, Ayahisa ^a,b   Nishijima, Ken Ichi ^a   Zhao, Songji ^a   Tanaka, Yoshikazu ^b   Itoh, Takeshi ^b   Takemoto, Hiroshi ^b   Tamaki, Nagara ^a,c   Kuge, Yuji ^a,c  

^a HOKKAIDO UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b SHIONOGI AND CO LTD   (Japan)

^c HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Biodistribution; Glucagon like peptide 1; Glycosylation; Noninvasive imaging

Indexed keywords

ALPHA2,6 SIALYL N ACETYLLACTOSAMINE GLUCAGON LIKE PEPTIDE 1 IODINE 123; GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 1 IODINE 123; IODINE 123; TRICHLOROACETIC ACID; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; AREA UNDER THE CURVE; ARTICLE; CONTROLLED STUDY; DRUG DISTRIBUTION; EX VIVO STUDY; GEL PERMEATION CHROMATOGRAPHY; GLYCOSYLATION; ISOTOPE LABELING; MALE; MAXIMUM PLASMA CONCENTRATION; NON INSULIN DEPENDENT DIABETES MELLITUS; NON INVASIVE PROCEDURE; NONHUMAN; PRIORITY JOURNAL; RADIOACTIVITY; RADIOIODINATION; RAT; SCINTILLATION CAMERA; STATISTICAL SIGNIFICANCE; TIME TO MAXIMUM PLASMA CONCENTRATION;

AMINO ACID SEQUENCE; ANIMALS; CARBOHYDRATE SEQUENCE; GLUCAGON-LIKE PEPTIDE 1; GLYCOSYLATION; IODINE RADIOISOTOPES; LIVER; MALE; MOLECULAR SEQUENCE DATA; RADIOPHARMACEUTICALS; RATS; RATS, WISTAR; TISSUE DISTRIBUTION;

EID: 84858708247     PISSN: 09147187     EISSN: 18646433     Source Type: Journal    
DOI: 10.1007/s12149-011-0558-z     Document Type: Article

References (34)

1. Deacon CF. Therapeutic strategies based on glucagon-like peptide1. Diabetes. 2004;53:2181-9. (Pubitemid 39145569)
2. Arulmozhi DK, Portha B. GLP-1 based therapy for type 2 diabetes. Eur J Pharm Sci. 2006;28:96-108.
3. Holst JJ, Ørskov C. The incretin approach for diabetes treatment: modulation of islet hormone release by GLP-1 agonism. Diabetes. 2004;53:S197-204. (Pubitemid 39564544)
4. Holst JJ, Deacon CF, Vilsbøll T, Krarup T, Madsbad S. Glucagon-like peptide-1, glucose homeostasis and diabetes. Trends Mol Med. 2008;14:161-8.
5. Kieffer TJ, Habener JF. The glucagon-like peptides. Endocr Rev. 1999;20:876-913. (Pubitemid 30647076)
6. Meier JJ, Nauck MA. Glucagon-like peptide 1 (GLP-1) in biology and pathology. Diabetes Metab Res Rev. 2005;21:91-117. (Pubitemid 40467658)
7. Nauck MA, Meier JJ. Glucagon-like peptide 1 and its derivatives in the treatment of diabetes. Regul Pept. 2005;128:135-48. (Pubitemid 40380914)
8. Simonsen L, Holst JJ, Deacon CF. Exendin-4, but not glucagonlike peptide-1, is cleared exclusively by glomerular filtration in anaesthetised pigs. Diabetologia. 2006;49:706-12. (Pubitemid 43357544)
9. Deacon CF, Pridal L, Klarskov L, Olesen M, Holst JJ. Glucagonlike peptide 1 undergoes differential tissue-specific metabolism in the anesthetized pig. Am J Physiol. 1996;271:E458-64.
10. Deacon CF, Johnsen AH, Holst JJ. Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo. J Clin Endocrinol Metab. 1995;80:952-7.
11. Kieffer TJ, McIntosh CHS, Pederson RA. Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology. 1995;136:3585-96.
12. Mentlein R, Gallwitz B, Schmidt WE. 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. 1993;214:829-35. (Pubitemid 23188160)
13. Hupe-Sodmann K, McGregor GP, Bridenbaugh R, Göke R, Göke B, Thole H, et al. Characterization 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. 1995;58:149-56.
14. Hupe-Sodmann K, Göke R, Göke B, Thole HH, Zimmermann B, Voigt K, et al. Endoproteolysis of glucagon-like peptide (GLP)-1 (7-36) amide by ectopeptidases in RINm5F cells. Peptides. 1997;18:625-32. (Pubitemid 27319773)
15. Plamboeck A, Holst JJ, Carr RD, Deacon CF. Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetised pig. Diabetologia. 2005;48:1882-90. (Pubitemid 41317844)
16. O'Harte FP, Mooney MH, Lawlor A, Flatt PR. N-terminally modified glucagon-like peptide-1 (7-36) amide exhibits resistance to enzymatic degradation while maintaining its antihyperglycaemic activity in vivo. Biochim Biophys Acta. 2000;1474:13-22. (Pubitemid 30103527)
17. Deacon CF, Knudsen LB, Madsen K, Wiberg FC, Jacobsen O, Holst JJ. Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity. Diabetologia. 1998;41:271-8. (Pubitemid 28254820)
18. Chae SY, Chun YG, Lee S, Jin CH, Lee ES, Lee KC, et al. Pharmacokinetic and pharmacodynamic evaluation of site-specific PEGylated glucagon-like peptide-1 analogs as flexible postprandial-glucose controllers. J Pharm Sci. 2009;98:1556-67.
19. Lee SH, Lee S, Youn YS, Na DH, Chae SY, Byun Y, et al. Synthesis, characterization, and pharmacokinetic studies of PEGylated glucagon-like peptide-1. Bioconj Chem. 2005;16:377-82. (Pubitemid 40388214)
20. Göke R, Fehmann HC, Linn T, Schmidt H, Krause M, Eng J, et al. Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting beta-cells. J Biol Chem. 1993;268:19650-5. (Pubitemid 23270754)
21. Thum A, Hupe-Sodmann K, Göke R, Voigt K, Göke B, McGregor GP. Endoproteolysis by isolated membrane peptidases reveal metabolic stability of glucagon-like peptide-1 analogs, exendins-3 and -4. Exp Clin Endocrinol Diabetes. 2002;110:113-8. (Pubitemid 34461416)
22. Young AA, Gedulin BR, Bhavsar S, Bodkin N, Jodka C, Hansen B, et al. Glucose-lowering and insulin-sensitizing actions of exendin-4: studies in obese diabetic (ob/ob, db/db) mice, diabetic fatty Zucker rats, and diabetic rhesus monkeys (Macaca mulatta). Diabetes. 1999;48:1026-34. (Pubitemid 29226349)
23. Sato M, Furuike T, Sadamoto R, Fujitani N, Nakahara T, Niikura K, et al. Glycoinsulins: dendritic sialyloligosaccharide-displaying insulins showing a prolonged blood-sugar-lowering activity. J Am Chem Soc. 2004;126:14013-22. (Pubitemid 39447078)
24. Sinclair AM, Elliott S. Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J Pharm Sci. 2005;94:1626-35. (Pubitemid 41360859)
25. Elliott S, Lorenzini T, Asher S, Aoki K, Brankow D, Buck L, et al. Enhancement of therapeutic protein in vivo activities through glycoengineering. Nat Biotechnol. 2003;21:414-21. (Pubitemid 36397662)
26. Macdougall IC, Gray SJ, Elston O, Breen C, Jenkins B, Browne J, et al. Pharmacokinetics of novel erythropoiesis stimulating protein compared with epoetin alfa in dialysis patients. J Am Soc Nephrol. 1999;10:2392-5. (Pubitemid 29501473)
27. Ueda T, Tomita K, Notsu Y, Ito T, Fumoto M, Takakura T, et al. Chemoenzymatic synthesis of glycosylated glucagon-like peptide 1: effect of glycosylation on proteolytic resistance and in vivo blood glucose-lowering activity. J Am Chem Soc. 2009;131:6237-45.
28. Hunter R. Standardization of the chloramine-T method of protein iodination. Proc Soc Exp Biol Med. 1970;133:989-92.
29. Webster R, Taberner J, Edgington A, Guhan S, Varghese J, Feeney H, et al. Role of sialylation in determining the pharmacokinetics of neutrophil inhibitory factor (NIF) in the Fischer 344 rat. Xenobiotica. 1999;29:1141-55.
30. Gabizon A, Papahadjopoulos D. The role of surface charge and hydrophilic groups on liposome clearance in vivo. Biochim Biophys Acta. 1992;10:94-100.
31. Mentlein R. Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regul Pept. 1999;85:9-24. (Pubitemid 29505281)
32. Drucker DJ, Buse JB, Taylor K, Kendall DM, Trautmann M, Zhuang D, et al. Exenatide once weekly versus twice daily for the treatment of type 2 diabetes: a randomised, open-label, noninferiority study. Lancet. 2008;372:1240-50.
33. Davies B, Morris T. Physiological parameters in laboratory animals and humans. Pharm Res. 1993;10:1093-5. (Pubitemid 23211439)
34. 111In-labeled peptides. J Nucl Med. 2010;51:973-7.