Advertisement
Journal of Biological Chemistry
Open access logo
Advanced searchSave search
Research Article| Volume 264, ISSUE 12, P6648-6654, April 25, 1989

Download started.

Ok

Binding of Monoiodinated Neuropeptide Y to Hippocampal Membranes and Human Neuroblastoma Cell Lines

Open AccessPublished:April 25, 1989DOI:https://doi.org/10.1016/S0021-9258(18)83476-7
Binding of Monoiodinated Neuropeptide Y to Hippocampal Membranes and Human Neuroblastoma Cell Lines
Previous ArticleDirect Evidence for Intra- and Intermolecular Disulfide Bond Formation in the Human Glucocorticoid Receptor
Next ArticleComplete Amino Acid Sequence and Structure Characterization of the Taste-modifying Protein, Miraculin
      This paper is only available as a PDF. To read, Please Download here.
      Monoiodinated radioligands of the homologous 36-amino acid peptides, neuropeptide Y (NPY) and peptide YY, were prepared by reverse phase high performance liquid chromatography with isocratic elution. [125I-Tyr1]- and [125I-Tyr36]monoiodoNPY bound equally well to a single class of high affinity binding sites on synaptosomal membranes prepared from porcine hippocampus (Kd = 1.0 × 10-10 M) whereas iodine substitution in Tyr27, for example, partly interfered with the receptor binding. The receptors on the hippocampal membranes did not distinguish between neuropeptide Y and peptide YY either in their monoiodinated or in their unlabeled forms. Six out of twelve human neuroblastoma cell lines had high affinity binding sites for monoiodinated NPY ranging from 2 to 145 × 10(3) sites per cell. The NPY binding to three of the cell lines, SMS-MSN, SMS-KAN, and CHP-234 was of relatively high affinity (Kd = 1.3 to 6.1 × 10-10 M), and, as in the hippocampal membranes, the long C-terminal fragment, NPY(13–36)peptide was also a relatively potent ligand for these receptors. Two other neuroblastoma cell lines, MC-IXC and CHP-212, expressed NPY receptors characterized by a lower affinity (Kd = 4.8 and 24.6 × 10-9 M) and negligible cross-reactivity with the C-terminal fragment. It is concluded that monoiodinated radioligands of the tyrosine-rich neuropeptide Y can be prepared and that receptors for these ligands in two apparently different subtypes are found on a series of human neuroblastoma cell lines.

      REFERENCES

        • O'Donohue T.L.
        • Cornwall B.M.
        • Pruss R.M.
        • Mezey E.
        • Kiss J.Z.
        • Eiden L.E.
        • Massari V.J.
        • Tessel R.E.
        • Pickel V.M.
        • DiMaggio D.A.
        Peptides. 1985; 6: 755-768
        • Wood S.P.
        • Pitts J.E.
        • Blundell T.L.
        • Tickle I.J.
        • Jenkins J.A.
        J. Biockem. (Tokyo). 1977; 78: 119-126
        • Blundell T.L.
        • Pitts J.E.
        • Tickle I.J.
        • Wood S.P.
        • Wu C.-W.
        Proc. Natl. Acad. Sci. U. S. A. 1981; 78: 4175-4179
        • Glover I.
        • Haneef I.
        • Pitts J.
        • Wood S.
        • Moss D.
        • Tickle I.
        • Blundell T.
        Biopolymers. 1983; 22: 293-304
        • Glover I.D.
        • Barlow D.J.
        • Pitts J.E.
        • Wood S.P.
        • Tickle I.J.
        • Blundell T.L.
        • Tatemoto K.
        • Kimmel J.R.
        • Wollmer A.
        • Strassburger W.
        • Zhang Y.-S.
        Eur. J. Biochem. 1985; 142: 379-385
        • Krstenansky J.L.
        • Buck S.H.
        Neuropeptides. 1987; 10: 77-85
        • Tatemoto K.
        Proc. Natl. Acad. Sci. U. S. A. 1982; 79: 5485-5489
        • Polak J.M.
        • Bloom S.R.
        Peptides. 1984; 5: 79-89
        • Tatemoto K.
        Proc. Natl. Acad. Sci. U. S. A. 1982; 79: 2514-2518
        • Lundberg J.M.
        • Tatemoto K.
        • Terenius L.
        • Hellstrøm P.M.
        • Mutt V.
        • Høkfelt T.
        • Hamberger B.
        Proc. Natl. Acad. Sci. U. S. A. 1982; 79: 4471-4475
        • Böttcher G.
        • Sjölund K.
        • Moghimzadeh E.
        • Håkanson R.
        • Schwartz T.W.
        • Sundler F.
        Regul. Pept. 1984; 8: 261-266
        • Stanley B.G.
        • Leibowitz S.F.
        Proc. Natl. Acad. Sci. U. S. A. 1985; 82: 3940-3943
        • Morley J.E.
        • Levine A.S.
        • Gosnell B.A.
        • Kneip J.
        • Grace M.
        Am. J. Physiol. 1987; 252: R599-R609
        • Wahlestedt C.
        • Edvinsson L.
        • Ekblad E.
        • Håkanson R.
        J. Pharmacol. Exp. Ther. 1985; 234: 735-741
        • Lundberg J.
        • Terenius L.
        • Hökfelt T.
        • Martling C.-R.
        • Tatemoto K.
        • Mutt V.
        • Polak J.
        • Bloom S.R.
        • Goldstein M.
        Acta Physiol. Scand. 1982; 116: 477-480
        • Ekblad E.
        • Edvinsson L.
        • Wahlestedt C.
        • Uddman R.
        • Håkanson R.
        • Sundler F.
        Regul. Pept. 1984; 8: 225-235
        • Sheikh S.
        • Holst J.J.
        • Skak-Nielsen T.
        • Knigge U.
        • Warberg J.
        • Theodorsson-Norheim E.
        • Hökfelt T.
        • Lundberg J.
        • Schwartz T.W.
        Am. J. Physiol. 1988; 255: G46-G54
        • Edvinsson L.
        • Emson P.
        • McGulloch J.
        • Tatemoto K.
        • Uddman R.
        Neurosci. Lett. 1983; 43: 79-84
        • Lundberg J.M.
        • Stjärne L.
        Acta Physiol. Scand. 1984; 120: 477-479
        • Wahlestedt C.
        • Yanaihara N.
        • Håkanson R.
        Regul. Pept. 1986; 13: 307-318
        • Lundberg J.M.
        • Hemsen A.
        • Larsson O.
        • Rudehill A.
        • Saria A.
        • Fredholm B.B.
        Eur. J. Pharmacol. 1988; 145: 21-29
        • Undén A.
        • Tatemoto K.
        • Mutt V.
        • Bartfai T.
        Eur. J. Biochem. 1984; 145: 525-530
        • Undén A.
        • Bartfai T.
        FEBS Lett. 1984; 177: 125-128
        • Chang R.S.V.
        • Lotti V.J.
        • Chen T.B.
        • Cerino D.J.
        • Kling P.J.
        Life Sci. 1985; 37: 2111-2122
        • Saria A.
        • Theodorsson-Norheim E.
        • Lundberg J.M.
        Eur. J. Pharmacol. 1985; 107: 105-107
        • Goldstein M.
        • Kusano N.
        • Adler C.
        • Meller E.
        Hökfelt T. Fuxe K. Pernow B. Progress in Brain Research. Vol. 68. Elsevier Science Publishing Co., Inc., New York1986: 331-335
        • Inui A.
        • Oya M.
        • Okita M.
        • Inoue T.
        • Sakatani N.
        • Morioka H.
        • Shi K.
        • Yokono K.
        • Mizuno N.
        • Baba S.
        Biochem. Biophys. Res. Commun. 1988; 150: 25-32
        • Laburthe M.
        • Chenut B.
        • Rouyer-Fessard C.
        • Tatemoto C.
        • Couvineau A.
        • Servin A.
        • Amiranoff B.
        Endocrinology. 1986; 118: 1910-1917
        • Schwartz T.W.
        • Sheikh S.P.
        • O'Hare M.M.T.
        FEBS Lett. 1987; 225: 209-214
        • Lundberg J.
        • Tatemoto K.
        Acta Physiol. Scand. 1982; 116: 393-402
        • Allen J.M.
        • Yeats J.C.
        • Adrian T.E.
        • Bloom S.R.
        Regul Pept. 1984; 8: 61-70
        • Fraker J.
        • Speck J.C.
        Biochem. Biophys. Res. Commun. 1978; 80: 849-857
        • Huttner W.B.
        Methods Enzymol. 1984; 107: 200-223
        • Gray E.G.
        • Whittaker V.P.
        J. Anat. 1962; 96: 79-96
        • Biedler J.L.
        • Roffler-Tarlov S.
        • Schachner M.
        • Freedman L.S.
        Cancer Res. 1978; 38: 3751-3757
        • Biedler J.L.
        • Rozen M.G.
        • El-Badry O.
        • Meyers M.B.
        • Melera P.W.
        • Ross R.A.
        • Spengler B.A.
        Evans A.E. Advances in Neuroblastoma Research. Alan R. Liss, Inc., New York1985: 209-221
        • Schlesinger H.R.
        • Gerson J.M.
        • Moorhead P.S.
        • Maguire H.
        • Hummeler K.
        Cancer Res. 1976; 36: 3094-3100
        • West G.J.
        • Uki J.
        • Herschmann H.R.
        • Seeger R.C.
        Cancer Res. 1977; 37: 1372-1376
        • Amano T.
        • Richelson E.
        • Nirenberg M.
        Proc. Natl. Acad. Sci. U. S. A. 1972; 69: 258-263
        • Taylor T.C.
        • Kimmel J.R.
        Anal. Biochem. 1987; 166: 194-203
        • Kilborn M.J.
        • Potter E.K.
        • McClosky D.I.
        Regul. Pept. 1985; 12: 155-161
        • Corder R.
        • Lowry P.J.
        • Withrington P.G.
        Br. J. Pharmacol. 1987; 90: 785-790
        • Whitsett J.A.
        • Noguchi A.
        • Neely J.E.
        • Johnson C.L.
        • Moore J.J.
        Brain Res. 1981; 216: 73-87
        • Yu V.C.
        • Richards M.L.
        • Sadée W.
        J. Biol. Chem. 1986; 261: 1065-1070
        • Helmeste D.M.
        • Hammonds R.G.
        • Li C.H.
        Proc. Natl. Acad. Sci. U. S. A. 1986; 83: 4622-4625

      Article info

      Publication history

      Published online: April 25, 1989
      Received: October 18, 1988

      Identification

      DOI: https://doi.org/10.1016/S0021-9258(18)83476-7

      Copyright

      © 1989 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.

      User license

      Creative Commons Attribution (CC BY 4.0) |
      How you can reuse Information Icon
      Creative Commons Attribution (CC BY 4.0)

      Permitted

      • Read, print & download
      • Redistribute or republish the final article
      • Text & data mine
      • Translate the article
      • Reuse portions or extracts from the article in other works
      • Sell or re-use for commercial purposes

      Elsevier's open access license policy

      ScienceDirect

      Access this article on ScienceDirect

      ASBMB  ASBMB  ASBMB  ASBMB

      ISSN 0021-9258
      We use cookies to help provide and enhance our service and tailor content. To update your cookie settings, please visit the for this site.
      Copyright © 2022 Elsevier Inc. except certain content provided by third parties. The content on this site is intended for healthcare professionals.


      RELX