메뉴 건너뛰기




Volumn 13, Issue 2, 1996, Pages 130-139

Relationship between native and recombinant cholecystokinin receptors: Role of differential glycosylation

Author keywords

Chinese hamster ovary (CHO) cell line; G protein coupled receptor; Type A cholecystokinin receptor

Indexed keywords

AGGLUTININ; CHOLECYSTOKININ A RECEPTOR; CHOLECYSTOKININ OCTAPEPTIDE; GUANOSINE TRIPHOSPHATE DERIVATIVE; N ACETYL BETA GLUCOSAMINIDASE; RECOMBINANT CHOLECYSTOKININ RECEPTOR; TETRAGASTRIN; UNCLASSIFIED DRUG;

EID: 0029791442     PISSN: 08853177     EISSN: None     Source Type: Journal    
DOI: 10.1097/00006676-199608000-00003     Document Type: Article
Times cited : (102)

References (42)
  • 1
    • 0026559686 scopus 로고
    • Purification, molecular cloning, and functional expression of the cholecystokinin receptor from rat pancreas
    • Wank SA, Harkins R. Jansen 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.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3125-3129
    • Wank, S.A.1    Harkins, R.2    Jansen, R.T.3    Shapira, H.4    De Weerth, A.5    Slattery, T.6
  • 3
    • 0026535933 scopus 로고
    • Expression cloning and characterization of the canine parietal cell gastrin receptor
    • Kopin AS, Lee YM, McBride EW, et al. Expression cloning and characterization of the canine parietal cell gastrin receptor. Proc Natl Acad Sci USA 1992;89:3605-9.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3605-3609
    • Kopin, A.S.1    Lee, Y.M.2    McBride, E.W.3
  • 4
    • 0020964422 scopus 로고
    • Identification and localization of cholecystokinin-binding sites on rat pancreatic plasma membranes and acinar cells: A biochemical and autoradiographic study
    • Rosenzweig SA, Miller LJ, Jamieson JD. Identification and localization of cholecystokinin-binding sites on rat pancreatic plasma membranes and acinar cells: a biochemical and autoradiographic study. J Cell Biol 1983;96:1288-97.
    • (1983) J Cell Biol , vol.96 , pp. 1288-1297
    • Rosenzweig, S.A.1    Miller, L.J.2    Jamieson, J.D.3
  • 5
    • 0023125680 scopus 로고
    • Affinity labeling of a novel cholecystokinin-binding protein in rat pancreatic plasmalemma using new short probes for the receptor
    • Pearson RK, Miller LJ. Affinity labeling of a novel cholecystokinin-binding protein in rat pancreatic plasmalemma using new short probes for the receptor. J Biol Chem 1987; 262:869-76.
    • (1987) J Biol Chem , vol.262 , pp. 869-876
    • Pearson, R.K.1    Miller, L.J.2
  • 6
    • 0025231280 scopus 로고
    • Gallbladder CCK receptors: Species differences in glycosylation of similar protein cores
    • Schjoldager B, Molero X, Miller LJ. Gallbladder CCK receptors: species differences in glycosylation of similar protein cores. Regul Pept 1990;28:265-72.
    • (1990) Regul Pept , vol.28 , pp. 265-272
    • Schjoldager, B.1    Molero, X.2    Miller, L.J.3
  • 7
    • 0028233158 scopus 로고
    • The marked disparity between the sizes of angiotensin type 2 receptors from different tissues is related to different degrees of N-glycosylation
    • Servant G, Dudley DT, Escher E, Guillemette G. The marked disparity between the sizes of angiotensin type 2 receptors from different tissues is related to different degrees of N-glycosylation. Mol Pharmacol 1994;45:1112-8.
    • (1994) Mol Pharmacol , vol.45 , pp. 1112-1118
    • Servant, G.1    Dudley, D.T.2    Escher, E.3    Guillemette, G.4
  • 8
    • 0027609719 scopus 로고
    • Receptor cloning and heterologous expression - Towards a new tool for drug discovery
    • Luyten WHML, Leysen JE. Receptor cloning and heterologous expression - towards a new tool for drug discovery. Trends Biotechnol 1993;11:247-54.
    • (1993) Trends Biotechnol , vol.11 , pp. 247-254
    • Luyten, W.H.M.L.1    Leysen, J.E.2
  • 9
    • 0028116553 scopus 로고
    • Cloning by function: Expression cloning in mammalian cells
    • Simonsen H, Lodish HF. Cloning by function: expression cloning in mammalian cells. Trends Pharmacol Sci 1994;15: 437-41.
    • (1994) Trends Pharmacol Sci , vol.15 , pp. 437-441
    • Simonsen, H.1    Lodish, H.F.2
  • 10
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol Biol Cell 1994;5:253-65.
    • (1994) Mol Biol Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 11
    • 0028944878 scopus 로고
    • Conformational implications of asparagine-linked glycosylation
    • Imperiali B, Richert KW. Conformational implications of asparagine-linked glycosylation. Proc Natl Acad Sci USA 1995;92:97-101.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 97-101
    • Imperiali, B.1    Richert, K.W.2
  • 12
    • 0028232090 scopus 로고
    • Glycosylation of the GLP-1 receptor is a prerequisite for regular receptor function
    • Göke R, Just R, Lankat-Buttgereit B, Göke B. Glycosylation of the GLP-1 receptor is a prerequisite for regular receptor function. Peptides 1994;15:675-81.
    • (1994) Peptides , vol.15 , pp. 675-681
    • Göke, R.1    Just, R.2    Lankat-Buttgereit, B.3    Göke, B.4
  • 13
    • 0028289785 scopus 로고
    • Specific roles for the asparagine-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal transduction
    • Bishop LA, Robertson DM, Cahir N, Schofield PR. Specific roles for the asparagine-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal transduction. Mol Endocrinol 1994;8:722-31.
    • (1994) Mol Endocrinol , vol.8 , pp. 722-731
    • Bishop, L.A.1    Robertson, D.M.2    Cahir, N.3    Schofield, P.R.4
  • 14
    • 0028354244 scopus 로고
    • Structure and function in rhodopsin: The role of asparagine-linked glycosylation
    • Kaushal S, Ridge KD, Khorana HG. Structure and function in rhodopsin: the role of asparagine-linked glycosylation. Proc Natl Acad Sci USA 1994;91:4024-8.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4024-4028
    • Kaushal, S.1    Ridge, K.D.2    Khorana, H.G.3
  • 15
    • 0027473919 scopus 로고
    • Structural and functional analysis of the human vasoactive intestinal peptide receptor glycosylation. Alteration of receptor function by wheat germ agglutinin
    • Chochola J, Fabre C, Bellan C, et al. Structural and functional analysis of the human vasoactive intestinal peptide receptor glycosylation. Alteration of receptor function by wheat germ agglutinin. J Biol Chem 1993;268:2312-8.
    • (1993) J Biol Chem , vol.268 , pp. 2312-2318
    • Chochola, J.1    Fabre, C.2    Bellan, C.3
  • 16
    • 0028852748 scopus 로고
    • Characterization of the substance P (NK-1) receptor in tunicamycin-treated transfected cells using a photoaffinity analogue of substance P
    • Kage R, Hershey AD, Krause JE, Boyd ND, Leeman SE. Characterization of the substance P (NK-1) receptor in tunicamycin-treated transfected cells using a photoaffinity analogue of substance P. J Neurochem 1995;64:316-21.
    • (1995) J Neurochem , vol.64 , pp. 316-321
    • Kage, R.1    Hershey, A.D.2    Krause, J.E.3    Boyd, N.D.4    Leeman, S.E.5
  • 17
    • 0023645714 scopus 로고
    • Analysis of the carbohydrate composition of the pancreatic plasmalemmal glycoprotein affinity labeled by short probes for the cholecystokinin receptor
    • Pearson RK, Miller LJ, Hadac EM, Powers SP. Analysis of the carbohydrate composition of the pancreatic plasmalemmal glycoprotein affinity labeled by short probes for the cholecystokinin receptor. J Biol Chem 1987;262:13850-6.
    • (1987) J Biol Chem , vol.262 , pp. 13850-13856
    • Pearson, R.K.1    Miller, L.J.2    Hadac, E.M.3    Powers, S.P.4
  • 18
    • 0024009303 scopus 로고
    • Use of N,O-bis-Fmoc-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides
    • Powers SP, Pinon DI, Miller LJ. Use of N,O-bis-Fmoc-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides. Int J Pept Protein Res 1988;31:429-34.
    • (1988) Int J Pept Protein Res , vol.31 , pp. 429-434
    • Powers, S.P.1    Pinon, D.I.2    Miller, L.J.3
  • 20
    • 0028922371 scopus 로고
    • Dual pathways of internalization of the cholecystokinin receptor
    • Roettger BF, Rentsch RU, Pinon D, et al. Dual pathways of internalization of the cholecystokinin receptor. J Cell Biol 1995;128:1029-42.
    • (1995) J Cell Biol , vol.128 , pp. 1029-1042
    • Roettger, B.F.1    Rentsch, R.U.2    Pinon, D.3
  • 21
    • 0026615926 scopus 로고
    • CircumVent thermal cycle sequencing and alternative manual and automated DNA sequencing protocols using the highly thermostable Vent (exo-) DNA polymerase
    • Sears L, Moran L, Kissinger C, et al. CircumVent thermal cycle sequencing and alternative manual and automated DNA sequencing protocols using the highly thermostable Vent (exo-) DNA polymerase. BioTechnology 1992;13:626-33.
    • (1992) BioTechnology , vol.13 , pp. 626-633
    • Sears, L.1    Moran, L.2    Kissinger, C.3
  • 22
    • 0024455623 scopus 로고
    • Purification and characterization of the rat pancreatic cholecystokinin receptor
    • Duong LT, Hadac EM, Miller LJ, Vlasuk GP. Purification and characterization of the rat pancreatic cholecystokinin receptor. J Biol Chem 1989;264:17990-6.
    • (1989) J Biol Chem , vol.264 , pp. 17990-17996
    • Duong, L.T.1    Hadac, E.M.2    Miller, L.J.3    Vlasuk, G.P.4
  • 24
    • 0021895138 scopus 로고
    • A new generation of calcium indicators with greatly improved fluorescence properties
    • Grynkiewicz G, Poenie M, Tsien RY. A new generation of calcium indicators with greatly improved fluorescence properties. J Biol Chem 1985;260:3440-50.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 25
    • 0019799491 scopus 로고
    • 125I-desaminotyrosyl)CCK-8, and its interactions with pancreatic acini
    • 125I-desaminotyrosyl)CCK-8, and its interactions with pancreatic acini. J Biol Chem 1981;256:12417-23.
    • (1981) J Biol Chem , vol.256 , pp. 12417-12423
    • Miller, L.J.1    Rosenzweig, S.A.2    Jamieson, J.D.3
  • 26
    • 0019061918 scopus 로고
    • LIGAND: A versatile computerized approach for characterization of ligand-binding systems
    • Munson PJ, Rodbard D. LIGAND: a versatile computerized approach for characterization of ligand-binding systems. Anal Biochem 1980;107:220-39.
    • (1980) Anal Biochem , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0024455863 scopus 로고
    • Protease peptide mapping of affinity-labeled rat pancreatic cholecystokinin-binding proteins
    • Klueppelberg UG, Powers SP, Miller LJ. Protease peptide mapping of affinity-labeled rat pancreatic cholecystokinin-binding proteins. Biochemistry 1989;28:7124-9.
    • (1989) Biochemistry , vol.28 , pp. 7124-7129
    • Klueppelberg, U.G.1    Powers, S.P.2    Miller, L.J.3
  • 29
    • 0027468925 scopus 로고
    • Dose-dependent recruitment of pancreatic acinar cells during receptor-mediated calcium mobilization
    • Willems PHGM, VanEmst-DeVries SE, VanOs CH, DePont JJHHM. Dose-dependent recruitment of pancreatic acinar cells during receptor-mediated calcium mobilization. Cell Calcium 1993;14:145-59.
    • (1993) Cell Calcium , vol.14 , pp. 145-159
    • Willems, P.H.G.M.1    VanEmst-DeVries, S.E.2    VanOs, C.H.3    DePont, J.J.H.H.M.4
  • 31
    • 0025166633 scopus 로고
    • The role of carbohydrate moieties of cholecystokinin receptors in cholecystokinin octapeptide binding: Alteration of binding data by specific lectins
    • Santer R, Leung YK, Alliet P, Lebenthal E, Lee PC. The role of carbohydrate moieties of cholecystokinin receptors in cholecystokinin octapeptide binding: alteration of binding data by specific lectins. Biochim Biophys Acta 1990;1051: 78-83.
    • (1990) Biochim Biophys Acta , vol.1051 , pp. 78-83
    • Santer, R.1    Leung, Y.K.2    Alliet, P.3    Lebenthal, E.4    Lee, P.C.5
  • 32
    • 0026063530 scopus 로고
    • The gall bladder cholecystokinin receptor exists in two guanine nucleotide-binding protein-regulated affinity states
    • Molero X, Miller LJ. The gall bladder cholecystokinin receptor exists in two guanine nucleotide-binding protein-regulated affinity states. Mol Pharmacol 1991;39:150-6.
    • (1991) Mol Pharmacol , vol.39 , pp. 150-156
    • Molero, X.1    Miller, L.J.2
  • 33
    • 0020459349 scopus 로고
    • 125I]cholecystokinin to pancreatic plasma membranes. Evidence for a disulfide-linked Mr 76 000 peptide in cholecystokinin receptors
    • 125I]cholecystokinin to pancreatic plasma membranes. Evidence for a disulfide-linked Mr 76 000 peptide in cholecystokinin receptors. Regul Pept 1982;4:163-72.
    • (1982) Regul Pept , vol.4 , pp. 163-172
    • Svoboda, M.1    Lambert, M.2    Furnelle, J.3    Christophe, J.4
  • 34
    • 0021331106 scopus 로고
    • Pancreatic CCK receptors: Characterization of covalently labeled subunits
    • Sakamoto C, Goldfine ID, Williams JA. Pancreatic CCK receptors: characterization of covalently labeled subunits. Biochem Biophys Res Commun 1984;118:623-8.
    • (1984) Biochem Biophys Res Commun , vol.118 , pp. 623-628
    • Sakamoto, C.1    Goldfine, I.D.2    Williams, J.A.3
  • 35
    • 0026092259 scopus 로고
    • Use of photoaffinity probes containing poly(ethylene glycol) spacers for topographical mapping of the cholecystokinin receptor complex
    • Powers SP, Foo I, Pinon D, Klueppelberg UG, Hedstrom JF, Miller LJ. Use of photoaffinity probes containing poly(ethylene glycol) spacers for topographical mapping of the cholecystokinin receptor complex. Biochemistry 1991;30: 676-82.
    • (1991) Biochemistry , vol.30 , pp. 676-682
    • Powers, S.P.1    Foo, I.2    Pinon, D.3    Klueppelberg, U.G.4    Hedstrom, J.F.5    Miller, L.J.6
  • 36
    • 0024604460 scopus 로고
    • Use of a nitrotryptophan-containing peptide for photoaffinity labeling the pancreatic cholecystokinin receptor
    • Klueppelberg UG, Gaisano HY, Powers SP, Miller LJ. Use of a nitrotryptophan-containing peptide for photoaffinity labeling the pancreatic cholecystokinin receptor. Biochemistry 1989;28:3463-8.
    • (1989) Biochemistry , vol.28 , pp. 3463-3468
    • Klueppelberg, U.G.1    Gaisano, H.Y.2    Powers, S.P.3    Miller, L.J.4
  • 38
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins: Organizers of transmembrane signals
    • Neer EJ. Heterotrimeric G proteins: organizers of transmembrane signals. Cell 1995;80:249-57.
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 39
    • 0024398662 scopus 로고
    • Regulation of high density lipoproteins of muscarinic acetylcholine receptor function in chick heart cells cultured in defined medium
    • Subers EM, Nathanson NM. Regulation of high density lipoproteins of muscarinic acetylcholine receptor function in chick heart cells cultured in defined medium. J Biol Chem 1989;264:19685-93.
    • (1989) J Biol Chem , vol.264 , pp. 19685-19693
    • Subers, E.M.1    Nathanson, N.M.2
  • 40
    • 0024330573 scopus 로고
    • The lipid environment of the nicotinic acetyloline receptor in native and reconstituted membranes
    • Barrantes FJ. The lipid environment of the nicotinic acetyloline receptor in native and reconstituted membranes. Crit Rev Biochem Mol Biol 1989;24:437-78.
    • (1989) Crit Rev Biochem Mol Biol , vol.24 , pp. 437-478
    • Barrantes, F.J.1
  • 41
    • 0015050875 scopus 로고
    • Composition of cellular membranes in the pancreas of the guinea pig. II. Lipids
    • Meldolesi J, Jamieson JD, Palade GE. Composition of cellular membranes in the pancreas of the guinea pig. II. Lipids. J Cell Biol 1971;49:130-49.
    • (1971) J Cell Biol , vol.49 , pp. 130-149
    • Meldolesi, J.1    Jamieson, J.D.2    Palade, G.E.3
  • 42
    • 0027156128 scopus 로고
    • Determination of plasma membrane lipid mass and composition in cultured Chinese hamster ovary cells using high gradient magnetic affinity chromatography
    • Warnock DE, Roberts C, Lutz MS, Blackburn WA, Young WW, Baenziger JU. Determination of plasma membrane lipid mass and composition in cultured Chinese hamster ovary cells using high gradient magnetic affinity chromatography. J Biol Chem 1993;268:10145-53.
    • (1993) J Biol Chem , vol.268 , pp. 10145-10153
    • Warnock, D.E.1    Roberts, C.2    Lutz, M.S.3    Blackburn, W.A.4    Young, W.W.5    Baenziger, J.U.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.