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Volumn 26, Issue 12, 2005, Pages 2616-2623

Isolation and characterization of a glycine-extended form of calcitonin receptor-stimulating peptide-1: Another biologically active form of calcitonin receptor-stimulating peptide-1

Author keywords

Calcitonin receptor; Calcitonin receptor stimulating peptide; cAMP; Glycine extended form of calcitonin receptor stimulating peptide; Isolation; Radioimmunoassay

Indexed keywords

ANTISERUM; CALCITONIN RECEPTOR; CALCITONIN RECEPTOR STIMULATING PEPTIDE 1; CYCLIC AMP; GLYCINE; N CYSTEINE CALCITONIN RECEPTOR STIMULATING PEPTIDE 2[29-37]AMIDE; N CYSTEINE CALCITONIN RECEPTOR STIMULATING PEPTIDE 3[29-37]AMIDE; N TYROSINE CALCITONIN RECEPTOR STIMULATING PEPTIDE 1[29-37]AMIDE; N TYROSINE CALCITONIN RECEPTOR STIMULATING PEPTIDE 3[29-37]AMIDE; PEPTIDE; UNCLASSIFIED DRUG;

EID: 27944475961     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2005.06.004     Document Type: Article
Times cited : (4)

References (24)
  • 1
    • 0026734904 scopus 로고
    • Expression of peptidylglycine alpha-amidating monooxygenase: An in situ hybridization and immunocytochemical study
    • K.M. Braas, S.A. Harakall, L. Ouafik, B.A. Eipper, and V. May Expression of peptidylglycine alpha-amidating monooxygenase: an in situ hybridization and immunocytochemical study Endocrinology 130 1992 2778 2788
    • (1992) Endocrinology , vol.130 , pp. 2778-2788
    • Braas, K.M.1    Harakall, S.A.2    Ouafik, L.3    Eipper, B.A.4    May, V.5
  • 2
    • 0024429540 scopus 로고
    • Tissue specific expression of rat peptidylglycine alpha-amidating monooxygenase activity and mRNA
    • K.M. Braas, D.A. Stoffers, B.A. Eipper, and V. May Tissue specific expression of rat peptidylglycine alpha-amidating monooxygenase activity and mRNA Mol Endocrinol 3 1989 1387 1398
    • (1989) Mol Endocrinol , vol.3 , pp. 1387-1398
    • Braas, K.M.1    Stoffers, D.A.2    Eipper, B.A.3    May, V.4
  • 3
    • 0021114751 scopus 로고
    • Substrate specificity of an amidating enzyme in porcine pituitary
    • A.F. Bradbury, and D.G. Smyth Substrate specificity of an amidating enzyme in porcine pituitary Biochem Biophys Res Commun 112 1983 372 377
    • (1983) Biochem Biophys Res Commun , vol.112 , pp. 372-377
    • Bradbury, A.F.1    Smyth, D.G.2
  • 4
    • 0035902440 scopus 로고    scopus 로고
    • Turn structures in CGRP C-terminal analogues promote stable arrangements of key residue side chains
    • K.A. Carpenter, R. Schmidt, B. von Mentzer, U. Haglund, E. Roberts, and C. Walpole Turn structures in CGRP C-terminal analogues promote stable arrangements of key residue side chains Biochemistry 40 2001 17 25
    • (2001) Biochemistry , vol.40 , pp. 17-25
    • Carpenter, K.A.1    Schmidt, R.2    Von Mentzer, B.3    Haglund, U.4    Roberts, E.5    Walpole, C.6
  • 6
    • 0024828976 scopus 로고
    • Non-amidated forms of VIP (glycine-extended VIP and VIP-free acid) have full bioactivity on smooth muscle
    • J. Fahrenkrug, B. Ottesen, and C. Palle Non-amidated forms of VIP (glycine-extended VIP and VIP-free acid) have full bioactivity on smooth muscle Regul Pept 26 1989 235 239
    • (1989) Regul Pept , vol.26 , pp. 235-239
    • Fahrenkrug, J.1    Ottesen, B.2    Palle, C.3
  • 7
    • 0013859674 scopus 로고
    • 9-Deamidooxytocin, an analog of the hormone containing a glycine residue in place of the glycinamide residue
    • B.M. Ferrier, and V. du Vigneaud 9-Deamidooxytocin, an analog of the hormone containing a glycine residue in place of the glycinamide residue J Med Chem 9 1966 55 57
    • (1966) J Med Chem , vol.9 , pp. 55-57
    • Ferrier, B.M.1    Du Vigneaud, V.2
  • 8
    • 0024160209 scopus 로고
    • Isolation and characterization of a variant form of vasoactive intestinal polypeptide
    • G. Gafvelin, M. Andersson, R. Dimaline, H. Jornvall, and V. Mutt Isolation and characterization of a variant form of vasoactive intestinal polypeptide Peptides 9 1988 469 474
    • (1988) Peptides , vol.9 , pp. 469-474
    • Gafvelin, G.1    Andersson, M.2    Dimaline, R.3    Jornvall, H.4    Mutt, V.5
  • 9
    • 0017052382 scopus 로고
    • The origin and characteristics of a pig kidney cell strain, LLC-PK
    • R.N. Hull, W.R. Cherry, and G.W. Weaver The origin and characteristics of a pig kidney cell strain, LLC-PK In Vitro 12 1976 670 677
    • (1976) In Vitro , vol.12 , pp. 670-677
    • Hull, R.N.1    Cherry, W.R.2    Weaver, G.W.3
  • 10
    • 0042665965 scopus 로고    scopus 로고
    • Identification of second and third calcitonin receptor-stimulating peptide in porcine brain
    • T. Katafuchi, K. Hamano, K. Kikumoto, and N. Minamino Identification of second and third calcitonin receptor-stimulating peptide in porcine brain Biochem Biophys Res Commun 308 2003 445 451
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 445-451
    • Katafuchi, T.1    Hamano, K.2    Kikumoto, K.3    Minamino, N.4
  • 11
    • 0346850787 scopus 로고    scopus 로고
    • Identifcation, structural determination, and biological activity of bovine and canine calcitonin receptor-stimulating peptides
    • T. Katafuchi, K. Hamano, and N. Minamino Identifcation, structural determination, and biological activity of bovine and canine calcitonin receptor-stimulating peptides Biochem Biophys Res Commun 313 2004 74 79
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 74-79
    • Katafuchi, T.1    Hamano, K.2    Minamino, N.3
  • 12
    • 0038187671 scopus 로고    scopus 로고
    • Calcitonin receptor-stimulating peptide, a new member of the calcitonin gene-related peptide family. Its isolation from porcine brain, structure, tissue distribution, and biological activity
    • T. Katafuchi, K. Kikumoto, K. Hamano, K. Kangawa, H. Matsuo, and N. Minamino Calcitonin receptor-stimulating peptide, a new member of the calcitonin gene-related peptide family. Its isolation from porcine brain, structure, tissue distribution, and biological activity J Biol Chem 278 2003 12046 12054
    • (2003) J Biol Chem , vol.278 , pp. 12046-12054
    • Katafuchi, T.1    Kikumoto, K.2    Hamano, K.3    Kangawa, K.4    Matsuo, H.5    Minamino, N.6
  • 13
    • 0037300990 scopus 로고    scopus 로고
    • Specificity of porcine calcitonin receptor and calcitonin receptor-like receptor in the presence of receptor-activity-modifying proteins
    • K. Kikumoto, T. Katafuchi, and N. Minamino Specificity of porcine calcitonin receptor and calcitonin receptor-like receptor in the presence of receptor-activity-modifying proteins Hypertens Res 26 2003 S15 S23
    • (2003) Hypertens Res , vol.26
    • Kikumoto, K.1    Katafuchi, T.2    Minamino, N.3
  • 14
    • 0032539746 scopus 로고    scopus 로고
    • The intermediate form of glycine-extended adrenomedullin is the major circulating molecular form in human plasma
    • K. Kitamura, J. Kato, M. Kawamoto, M. Tanaka, N. Chino, and K. Kangawa The intermediate form of glycine-extended adrenomedullin is the major circulating molecular form in human plasma Biochem Biophys Res Commun 244 1998 551 555
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 551-555
    • Kitamura, K.1    Kato, J.2    Kawamoto, M.3    Tanaka, M.4    Chino, N.5    Kangawa, K.6
  • 15
    • 0026342822 scopus 로고
    • Expression cloning of an adenylate cyclase-coupled calcitonin receptor
    • H.Y. Lin, T.L. Harris, M.S. Flannery, A. Aruffo, E.H. Kaji, and A. Gorn Expression cloning of an adenylate cyclase-coupled calcitonin receptor Science 254 1991 1022 1024
    • (1991) Science , vol.254 , pp. 1022-1024
    • Lin, H.Y.1    Harris, T.L.2    Flannery, M.S.3    Aruffo, A.4    Kaji, E.H.5    Gorn, A.6
  • 16
    • 0025310869 scopus 로고
    • Immunocytochemical and in situ hybridization studies of peptidylglycine alpha-amidating monooxygenase in pituitary gland
    • V. May, L. Ouafik, B.A. Eipper, and K.M. Braas Immunocytochemical and in situ hybridization studies of peptidylglycine alpha-amidating monooxygenase in pituitary gland Endocrinology 127 1990 358 364
    • (1990) Endocrinology , vol.127 , pp. 358-364
    • May, V.1    Ouafik, L.2    Eipper, B.A.3    Braas, K.M.4
  • 17
    • 0015321357 scopus 로고
    • Physiological and immunological studies with desamidogastrin
    • J.E. McGuigan, and H.F. Thomas Physiological and immunological studies with desamidogastrin Gastroenterology 62 1972 553 558
    • (1972) Gastroenterology , vol.62 , pp. 553-558
    • McGuigan, J.E.1    Thomas, H.F.2
  • 18
    • 0024155975 scopus 로고
    • Production of a biologically active variant form of recombinant human secretin
    • H. Olson, P. Lind, G. Pohl, C. Henrichson, V. Mutt, and H. Jornvall Production of a biologically active variant form of recombinant human secretin Peptides 9 1988 301 307
    • (1988) Peptides , vol.9 , pp. 301-307
    • Olson, H.1    Lind, P.2    Pohl, G.3    Henrichson, C.4    Mutt, V.5    Jornvall, H.6
  • 19
    • 0025258485 scopus 로고
    • Release of thyrotropin and prolactin by a thyrotropin-releasing hormone (TRH) precursor, TRH-Gly: Conversion to TRH is sufficient for in vivo effects
    • A.E. Pekary, R. Stephens, M. Simard, X.P. Pang, V. Smith, and J. DiStefano Jr. Release of thyrotropin and prolactin by a thyrotropin-releasing hormone (TRH) precursor, TRH-Gly: conversion to TRH is sufficient for in vivo effects Neuroendocrinology 52 1990 618 625
    • (1990) Neuroendocrinology , vol.52 , pp. 618-625
    • Pekary, A.E.1    Stephens, R.2    Simard, M.3    Pang, X.P.4    Smith, V.5    DiStefano Jr., J.6
  • 20
    • 0030699146 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of peptidylglycine alpha-hydroxylating monooxygenase
    • S.T. Prigge, A.S. Kolhekar, B.A. Eipper, R.E. Mains, and L.M. Amzel Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase Science 278 1997 1300 1305
    • (1997) Science , vol.278 , pp. 1300-1305
    • Prigge, S.T.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 21
    • 0000821179 scopus 로고    scopus 로고
    • New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function
    • S.T. Prigge, R.E. Mains, B.A. Eipper, and L.M. Amzel New insights into copper monooxygenases and peptide amidation: structure, mechanism and function Cell Mol Life Sci 57 2000 1236 1259
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1236-1259
    • Prigge, S.T.1    Mains, R.E.2    Eipper, B.A.3    Amzel, L.M.4
  • 22
    • 0017238954 scopus 로고
    • Structure-activity relationship of human calcitonin. III. Biological activity of synthetic analogues with shortened or terminally modified peptide chains
    • W. Rittel, R. Maier, M. Brugger, B. Kamber, B. Riniker, and P. Sieber Structure-activity relationship of human calcitonin. III. Biological activity of synthetic analogues with shortened or terminally modified peptide chains Experientia 32 1976 246 248
    • (1976) Experientia , vol.32 , pp. 246-248
    • Rittel, W.1    Maier, R.2    Brugger, M.3    Kamber, B.4    Riniker, B.5    Sieber, P.6
  • 23
    • 0024802639 scopus 로고
    • Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus
    • A.N. Roberts, B. Leighton, J.A. Todd, D. Cockburn, P.N. Schofield, and R. Sutton Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus Proc Natl Acad Sci USA 86 1989 9662 9666
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9662-9666
    • Roberts, A.N.1    Leighton, B.2    Todd, J.A.3    Cockburn, D.4    Schofield, P.N.5    Sutton, R.6
  • 24
    • 0028102660 scopus 로고
    • Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase
    • K. Tateishi, F. Arakawa, Y. Misumi, A.M. Treston, M. Vos, and Y. Matsuoka Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase Biochem Biophys Res Commun. 205 1994 282 290
    • (1994) Biochem Biophys Res Commun. , vol.205 , pp. 282-290
    • Tateishi, K.1    Arakawa, F.2    Misumi, Y.3    Treston, A.M.4    Vos, M.5    Matsuoka, Y.6


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