Measurement of nonsulfated cholecystokinins

References

• Wold F. In vivo chemical modification of proteins: post-translational modification. Ann Rev Biochem 1981;50: 783–814.
   PubMed Web of Science ®Google Scholar
• Kannicht C. Posttranslational modifications of proteins. Methods Mol Biol 2008;446:1–390.
   PubMedGoogle Scholar
• Kastin AJ. (ed.) Handbook of biologically active peptides, 2nd edn. Amsterdam: Academic Press/Elsevier, 2013; pp. 1–1911.
   Google Scholar
• Rehfeld JF. Cholecystokinin. Best Pract Res Clin Endocrinol Metab 2004;18:569–86.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF, Friis-Hansen L, Goetze JP, Hansen TvO. The biology of cholecystokinin and gastrin peptides. Curr Top Med Chem 2007;7:1154–65.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF. Immunochemical studies on cholecystokinin II. Distribution and molecular heterogeneity in the central nervous system and small intestine of man and hog. J Biol Chem 1978;253:4022–30.
   PubMed Web of Science ®Google Scholar
• Larsson LI, Rehfeld JF. Localisation and molecular heterogeneity of cholecystokinin in the central and peripheral nervous systems. Brain Res 1979;165:201–18.
   PubMed Web of Science ®Google Scholar
• Mutt V, Jorpes JE. Structure of porcine cholecystokinin-pancreozymin. 1. Cleavage with thrombin and with trypsin. Eur J Biochem 1968;6:156–62.
   PubMedGoogle Scholar
• Mutt V, Jorpes JE. Hormonal polypeptides of the upper intestine. Biochem J 1971;125:57P–8P.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF. Cholecystokinin. In: Schultz SG, Makhlouf GM, editors. Handbook of physiology: the gastrointestinal system. Bethesda, MD: American Physiology Society; 1989. pp. 337–58.
   Google Scholar
• Gregory H, Hardy PM, Jones DS, Kenner GW, Sheppard RC. The antral hormone gastrin. Structure of gastrin. Nature 1964;204:931–33.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF. The endoproteolytic maturation of progastrin and procholecystokinin. J Mol Med 2006;84:544–50.
   PubMed Web of Science ®Google Scholar
• Kopin AS, Lee YM, McBride EW, Miller LJ, Lu M, Lin HY, Kolakowski jr. LF, Beinborn M. Expression cloning and characterization of the canine parietal cell gastrin receptor. Proc Natl Acad Sci USA 1992;89:3605–9.
   PubMed Web of Science ®Google Scholar
• Wank SA, Harkins R, Jensen RT, Shapira H, de Weerth A, Slattery T. Purification, molecular cloning, and functional expression of the cholecystokinin receptor from rat pancreas. Proc Natl Acad Sci USA 1992;89:3125–9.
   PubMed Web of Science ®Google Scholar
• Wank SA. Cholecystokinin receptors. Amer J Physiol 1995;269:G628–46.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF. Accurate measurement of cholecystokinin in plasma. Clin Chem 1998;44:991–1001.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF. Immunochemical studies on cholecystokinin. I. Development of sequence-specific radioimmunoassays for porcine triacontatriapeptide cholecystokinin. J Biol Chem 1978;253:4016–21.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF, Stadil F, Rubin B. Production and evaluation of antibodies for the radioimmunoassay of gastrin. Scand J Clin Lab Invest 1972;30:221–32.
   PubMed Web of Science ®Google Scholar
• Scatchard G. The attraction of proteins for small molecules and ions. Ann NY Acad Sci 1949;51:660–72.
   Web of Science ®Google Scholar
• Ekins R, Newman B. Theoretical aspects of saturation analysis. Acta Endocrinol 1970;147:11–36.
   Google Scholar
• Rehfeld JF, Bardram L, Cantor P, Hilsted L, Johnsen AH. The unique specificity of antibodies in modern radioimmunochemistry. Scand J Clin Lab Invest 1989;49(Suppl.): 41–4.
   Google Scholar
• Hilsted L, Rehfeld JF. Measurement of precursors for α-amidated hormones by radioimmunoassay of glycine- extended peptides after trypsin-carboxypeptidase B cleavage. Analyt Biochem 1986;152:119–26.
   PubMed Web of Science ®Google Scholar
• Hosoda H, Kojima M, Matsuo H. Ghrelin and des-acyl ghrelin: two major forms of a ghrelin peptide in gastrointestinal tissue. Biochem Biophys Res Comm 2000;279:909–13.
   PubMed Web of Science ®Google Scholar
• Kojima M, Kangawa K. Ghrelin: structure and function. Physiol Rev 2005;85:495–522.
   PubMed Web of Science ®Google Scholar
• Kumar R, Salehi A, Rehfeld JF, Höglund P, Lindström E, Håkanson R. Proghrelin peptides: Desacyl ghrelin is a powerful inhibitor of acylated ghrelin, likely to impair physiological effects of ghrelin but not of obestatin. A study of pancreatic polypeptide secretion from isolated mouse islets. Regul Peptides 2010;164:65–70.
   PubMedGoogle Scholar
• Semenov AG, Postnikov AB, Tamm NN, Seferian KR, Karpova NS, Bloshchitsyna MN, Koshkina EV, Krasnoselsky MI, Serebryanaya DV, Katrukha AG. Processing of pro-brain natriuretic peptide is suppressed by O-glycosylation in the region close to the cleavage site. Clin Chem 2009;55:489–98.
   PubMed Web of Science ®Google Scholar
• Jiang J, Pristera N, Wang W, Zhang X, Wu Q. Effect of sialylated O-glycans in pro-brain natriuretic peptide stability. Clin Chem 2010;56:959–66.
   PubMed Web of Science ®Google Scholar
• Hunter I, Alehagen U, Dahlström U, Rehfeld JF, Crimmins DL, Goetze JP. N-terminal pro-atrial natriuretic peptide measurement in plasma suggests covalent modification. Clin Chem 2011;57:1327–30.
   PubMed Web of Science ®Google Scholar
• Ryan MT, Naylor DJ, Hoogenrad NJ, Høj PB. Affinity purification, overexpression, and characterization of chaperonin-10 homologues synthesized with and without N-terminal acetylation. J Biol Chem 1995;270:22037–43.
   PubMed Web of Science ®Google Scholar
• Smyth DG, Massey DE, Zakarian S, Finnie MD. Endorphins are stored in biologically active and inactive forms: isolation of alpha-N-acetyl peptides. Nature 1979;279: 252–4.
   PubMed Web of Science ®Google Scholar
• Wilkinson CW. Roles of acetylation and other post- translational modifications in melanocortin function and interactions with endorphins. Peptides 2006;27:453–71.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF, Johnsen AH, Ødum L, Bardram L, Schifter S, Scopsi L. Non-sulphated cholecystokinin in human medullary thyroid carcinomas. J Endocrinol 1990;124:501–6.
   PubMed Web of Science ®Google Scholar
• Bonetto V, Jörnvall H, Andersson M, Renlund S, Mutt V, Sillard R. Isolation and characterization of sulphated and nonsulphated forms of cholecystokinin-58 and their action on gallbladder contraction. Eur J Biochem 1999;264: 336–40.
   PubMedGoogle Scholar
• Reeve Jr JR, Liddle RA, McVey DC, Vigna SR, Solomon TE, Keire DA, Rosenquist G, Shively JE, Lee TD, Green GM, Coskun T. Identification of nonsulfated cholecystokinin-58 in canine intestinal extracts and its biological properties. Am J Physiol 2004;287:G326–33.
   Google Scholar
• Johnsen AH. Phylogeny of the cholecystokinin/gastrin family. Front Neuroendocrinol 1998;19:73–99.
   PubMed Web of Science ®Google Scholar
• Friis-Hansen L, Rehfeld JF. Ileal expression of gastrin and cholecystokinin – in search of a related hormone. FEBS Lett 1994;343:115–9.
   PubMed Web of Science ®Google Scholar
• Jensen RT, Niederle B, Mitry E, Ramage JK, Steinmüller T, Lewington V, Scarpa A, Sundin A, Perren A, Gross D, O’Connor JM, Pauwels S, Klöppel G. Gastrinoma (duodenal and pancreatic). Neuroendocrinology 2006;84:173–82.
   PubMed Web of Science ®Google Scholar
• Pipeleers-Marichal M, Somers G, Willems G, Foulis A, Imrie C, Bishop AE, Polak JM, Häcki WH, Stamm B, Heitz PU, Klöppel G. Gastrinomas in the duodenums of patients with multiple endocrine neoplasia type 1 and the Zollinger-Ellison syndrome. N Engl J Med 1990;332:723–7.
   Google Scholar
• Rehfeld JF, Federspiel B, Bardram L. A neuroendocrine tumor syndrome caused by cholecystokinin secretion. N Engl J Med 2013;368:1165–6.
   PubMed Web of Science ®Google Scholar
• Jacobsen SH, Olesen SC, Dirksen C, Jørgensen NB, Bojsen-Møller KN, Kielgast U, Worm D, Almdal T, Naver LS, Hvolris LE, Rehfeld JF, Wulff BS, Clausen TR, Hansen DL, Holst JJ, Madsbad S. Changes in gastrointestinal hormone responses, insulin sensitivity, and beta-cell function within 2 weeks after gastric bypass in non-diabetic subjects. Obes Surg 2012;22:1084–96.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF. Incretin physiology beyond glucagon-like peptide 1 and glucose-dependent insulinotropic polypeptide: cholecystokinin and gastrin peptides. Acta Physiol 2011;201:1327–30.
   Web of Science ®Google Scholar
• Bardram L, Rehfeld JF. Processing-independent radioimmunoanalysis: a general analytical principle applied to progastrin and its products. Analyt Biochem 1988;175: 537–43.
   PubMed Web of Science ®Google Scholar
• Rehfeld JF, Bardram L. Processing-independent analysis (PIA) – A new diagnostic tool. Scand J Clin Lab Invest 1991;204(Suppl.):9–16.
   Google Scholar
• Goetze JP, Hunter I, Lippert SK, Bardram L, Rehfeld JF. Processing-independent analysis of peptide hormones and prohormones in plasma. Front Biosci 2012;17: 1804–15.
   Web of Science ®Google Scholar
• Rehfeld JF, Agersnap M. Unsulfated cholecystokinin: an overlooked hormone? Regul Peptides 2012;173:1–5.
   PubMedGoogle Scholar