{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T02:04:40Z","timestamp":1791252280941,"version":"4.1.0"},"reference-count":29,"publisher":"Elsevier BV","content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Peptides"],"published-print":{"date-parts":[[2014,5]]},"DOI":"10.1016\/j.peptides.2014.01.020","type":"journal-article","created":{"date-parts":[[2014,2,1]],"date-time":"2014-02-01T21:15:48Z","timestamp":1391289348000},"page":"52-57","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":56,"special_numbering":"C","title":["GLP-1 amidation efficiency along the length of the intestine in mice, rats and pigs and in GLP-1 secreting cell lines"],"prefix":"10.1016","volume":"55","author":[{"given":"Rune Ehrenreich","family":"Kuhre","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4230-5753","authenticated-orcid":false,"given":"Nicolai Wewer","family":"Albrechtsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johanne Agerlin","family":"Windel\u00f8v","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Berit","family":"Svendsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bolette","family":"Hartmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jens Juul","family":"Holst","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.peptides.2014.01.020_bib0005","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1210\/jc.2007-1369","article-title":"Measurements of islet function and glucose metabolism with the dipeptidyl peptidase 4 inhibitor vildagliptin in patients with type 2 diabetes","volume":"93","author":"Azuma","year":"2008","journal-title":"J Clin Endocrinol Metab"},{"key":"10.1016\/j.peptides.2014.01.020_bib0010","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1007\/BF02899698","article-title":"NCI-H716 cells as a model for endocrine differentiation in colorectal cancer","volume":"62","author":"Bru\u00efne","year":"1992","journal-title":"Virchows Archiv B: Cell Pathol"},{"key":"10.1016\/j.peptides.2014.01.020_bib0015","first-page":"952","article-title":"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","volume":"80","author":"Deacon","year":"1995","journal-title":"J Clin Endocrinol Metab"},{"key":"10.1016\/j.peptides.2014.01.020_bib0020","doi-asserted-by":"crossref","first-page":"E458","DOI":"10.1152\/ajpendo.1996.271.3.E458","article-title":"Glucagon-like peptide 1 undergoes differential tissue-specific metabolism in the anesthetized pig","volume":"271","author":"Deacon","year":"1996","journal-title":"Am J Physiol Endocrinol Metab"},{"key":"10.1016\/j.peptides.2014.01.020_bib0025","first-page":"1646","article-title":"Activation of proglucagon gene transcription by protein kinase-A in a novel mouse enteroendocrine cell line","volume":"8","author":"Drucker","year":"1994","journal-title":"Mol Endocrinol"},{"key":"10.1016\/j.peptides.2014.01.020_bib0030","first-page":"E662","article-title":"Inhibition of pancreatic proglucagon gene expression in mice bearing subcutaneous endocrine tumors","author":"Ehrlich","year":"1994","journal-title":"Am J Physiol"},{"key":"10.1016\/j.peptides.2014.01.020_bib0035","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1677\/JOE-08-0528","article-title":"A selective small molecule glucagon-like peptide-1 secretagogue acting via depolarization-coupled Ca(2+) influx","volume":"201","author":"Eiki","year":"2009","journal-title":"J Endocrinol"},{"key":"10.1016\/j.peptides.2014.01.020_bib0040","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1111\/j.1365-2362.1992.tb01464.x","article-title":"Glucagon-like peptide-1 cells in the gastrointestinal tract and pancreas of rat, pig and man","volume":"22","author":"Eissele","year":"1992","journal-title":"Eur J Clin Invest"},{"key":"10.1016\/j.peptides.2014.01.020_bib0045","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1097\/00006676-199103000-00013","article-title":"GLP-1 and GLP-17\u201336 amide influences on basal and stimulated insulin and glucagon secretion in the mouse","volume":"6","author":"Fridolf","year":"1991","journal-title":"Pancreas"},{"key":"10.1016\/j.peptides.2014.01.020_bib0050","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.2337\/diabetes.52.5.1147","article-title":"A novel glucose-sensing mechanism contributing to glucagon-like peptide-1 secretion from the GLUTag cell line","volume":"52","author":"Gribble","year":"2003","journal-title":"Diabetes"},{"key":"10.1016\/j.peptides.2014.01.020_bib0055","doi-asserted-by":"crossref","first-page":"5356","DOI":"10.1210\/endo.140.11.7143","article-title":"Glucagon-like peptide-1-(7\u201336)amide is transformed to glucagon-like peptide-1-(9\u201336)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine","volume":"140","author":"Hansen","year":"1999","journal-title":"Endocrinology"},{"key":"10.1016\/j.peptides.2014.01.020_bib0060","doi-asserted-by":"crossref","first-page":"2206","DOI":"10.1007\/s00125-011-2168-7","article-title":"Dipeptidyl peptidase-4 inhibition increases portal concentrations of intact glucagon-like peptide-1 (GLP-1) to a greater extent than peripheral concentrations in anaesthetised pigs","volume":"54","author":"Hj\u00f8llund","year":"2011","journal-title":"Diabetologia"},{"key":"10.1016\/j.peptides.2014.01.020_bib0065","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1007\/s10735-010-9304-4","article-title":"Density distribution of free fatty acid receptor 2 (FFA2)-expressing and GLP-1-producing enteroendocrine L cells in human and rat lower intestine, and increased cell numbers after ingestion of fructo-oligosaccharide","volume":"42","author":"Kaji","year":"2011","journal-title":"J Mol Histol"},{"key":"10.1016\/j.peptides.2014.01.020_bib0070","doi-asserted-by":"crossref","first-page":"3585","DOI":"10.1210\/endo.136.8.7628397","article-title":"Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV","volume":"136","author":"Kieffer","year":"1995","journal-title":"Endocrinology"},{"key":"10.1016\/j.peptides.2014.01.020_bib0075","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1111\/j.1463-1326.2011.01357.x","article-title":"An overview of once-weekly glucagon-like peptide-1 receptor agonists-available efficacy and safety data and perspectives for the future","volume":"13","author":"Madsbad","year":"2011","journal-title":"Diabetes Obes Metab"},{"key":"10.1016\/j.peptides.2014.01.020_bib0080","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1111\/j.1432-1033.1993.tb17986.x","article-title":"Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7\u201336)amide, peptide histidine methionine and is responsible for their degradation in human serum","volume":"214","author":"Mentlein","year":"1993","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.peptides.2014.01.020_bib0085","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1083\/jcb.121.1.23","article-title":"COOH-terminal signals mediate the trafficking of a peptide processing enzyme in endocrine cells","volume":"121","author":"Milgram Sl","year":"1993","journal-title":"J Cell Biol"},{"key":"10.1016\/j.peptides.2014.01.020_bib0090","doi-asserted-by":"crossref","first-page":"11880","DOI":"10.1016\/S0021-9258(18)67324-7","article-title":"Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing","volume":"261","author":"Mojsov","year":"1986","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2014.01.020_bib0095","doi-asserted-by":"crossref","first-page":"8001","DOI":"10.1016\/S0021-9258(19)39030-1","article-title":"Both amidated and nonamidated forms of glucagon-like peptide I are synthesized in the rat intestine and the pancreas","volume":"265","author":"Mojsov","year":"1990","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2014.01.020_bib0100","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/S0167-0115(03)00125-3","article-title":"GLP-1 and GIP are colocalized in a subset of endocrine cells in the small intestine","volume":"114","author":"Mortensen","year":"2003","journal-title":"Regul Pept"},{"key":"10.1016\/j.peptides.2014.01.020_bib0105","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1002\/(SICI)1096-9136(1998110)15:11<937::AID-DIA701>3.0.CO;2-0","article-title":"Normalization of fasting glycaemia by intravenous GLP-1 ([7\u201336 amide] or [7\u201337]) in type 2 diabetic patients","volume":"15","author":"Nauck","year":"1998","journal-title":"Diabet Med"},{"key":"10.1016\/j.peptides.2014.01.020_bib0110","doi-asserted-by":"crossref","first-page":"535","DOI":"10.2337\/diab.43.4.535","article-title":"Tissue and plasma concentrations of amidated and glycine-extended glucagon-like peptide I in humans","volume":"43","author":"Orskov","year":"1994","journal-title":"Diabetes"},{"key":"10.1016\/j.peptides.2014.01.020_bib0115","doi-asserted-by":"crossref","first-page":"656","DOI":"10.2337\/diab.42.5.658","article-title":"Biological effects and metabolic rates of glucagonlike peptide-1 7\u201336 amide and glucagonlike peptide-1 7\u201337 in healthy subjects are indistinguishable","volume":"42","author":"Orskov","year":"1993","journal-title":"Diabetes"},{"key":"10.1016\/j.peptides.2014.01.020_bib0120","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/BF03190278","article-title":"Glucagon-like peptide-1(7\u201337) has a larger volume of distribution than glucagon-like peptide-1(7\u201336)amide in dogs and is degraded more quickly in vitro by dog plasma","volume":"21","author":"Pridal","year":"1996","journal-title":"Eur J Metab Pharmacokinet"},{"key":"10.1016\/j.peptides.2014.01.020_bib0125","first-page":"125","volume":"vol. 50","author":"Rehfeld","year":"2010"},{"key":"10.1016\/j.peptides.2014.01.020_bib0130","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1677\/joe.1.06557","article-title":"Meat hydrolysate and essential amino acid-induced glucagon-like peptide-1 secretion, in the human NCI-H716 enteroendocrine cell line, is regulated by extracellular signal-regulated kinase1\/2 and p38 mitogen-activated protein kinases","volume":"191","author":"Reimer","year":"2006","journal-title":"J Endocrinol"},{"key":"10.1016\/j.peptides.2014.01.020_bib0135","first-page":"15","article-title":"Development of neuroendocrine tumors in the gastrointestinal tract of transgenic mice","volume":"136","author":"Rindi","year":"1990","journal-title":"Am J Pathol"},{"key":"10.1016\/j.peptides.2014.01.020_bib0140","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1007\/s00125-004-1342-6","article-title":"Incretins, insulin secretion and type 2 diabetes mellitus","volume":"47","author":"Vilsboll","year":"2004","journal-title":"Diabeteologia"},{"key":"10.1016\/j.peptides.2014.01.020_bib0145","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0167-0115(98)00044-5","article-title":"Amidated and non-amidated glucagon-like peptide-1 (GLP-1): non-pancreatic effects (cephalic phase acid secretion) and stability in plasma in humans","volume":"16","author":"Wettergren","year":"1998","journal-title":"Regul Pept"}],"container-title":["Peptides"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978114000345?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978114000345?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,3,25]],"date-time":"2022-03-25T02:04:08Z","timestamp":1648173848000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0196978114000345"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,5]]},"references-count":29,"alternative-id":["S0196978114000345"],"URL":"https:\/\/doi.org\/10.1016\/j.peptides.2014.01.020","relation":{},"ISSN":["0196-9781"],"issn-type":[{"value":"0196-9781","type":"print"}],"subject":[],"published":{"date-parts":[[2014,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"GLP-1 amidation efficiency along the length of the intestine in mice, rats and pigs and in GLP-1 secreting cell lines","name":"articletitle","label":"Article Title"},{"value":"Peptides","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.peptides.2014.01.020","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}