메뉴 건너뛰기




Volumn 137, Issue 12, 1996, Pages 5502-5508

Intracellular retention and rapid degradation of human calcitonin receptors overexpressed in COS cells

Author keywords

[No Author keywords available]

Indexed keywords

CALCITONIN; CALCITONIN RECEPTOR; N ACETYL BETA GLUCOSAMINIDASE; RECEPTOR PROTEIN; SALCATONIN;

EID: 0030457776     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.137.12.8940377     Document Type: Article
Times cited : (9)

References (28)
  • 1
    • 0029450581 scopus 로고
    • 25 years of salmon calcitonin: From synthesis to therapeutic use
    • Azria M, Copp DH, Zanelli JM 1995 25 years of salmon calcitonin: from synthesis to therapeutic use. Calcif Tissue Int 57:405-408
    • (1995) Calcif Tissue Int , vol.57 , pp. 405-408
    • Azria, M.1    Copp, D.H.2    Zanelli, J.M.3
  • 3
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin JM 1993 The probable arrangement of the helices in G protein-coupled receptors. EMBO J 12:1693-1703
    • (1993) EMBO J , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 4
    • 0027745212 scopus 로고
    • Receptors for secretin, calcitonin, parathyroid hormone (PTH)/PTH-related peptide, vasoactive intestinal peptide, glucagon-like peptide 1, growth hormone-releasing hormone, and glucagon belong to a newly discovered G-protein-linked receptor family
    • Segre GV, Goldring SR 1993 Receptors for secretin, calcitonin, parathyroid hormone (PTH)/PTH-related peptide, vasoactive intestinal peptide, glucagon-like peptide 1, growth hormone-releasing hormone, and glucagon belong to a newly discovered G-protein-linked receptor family. Trends Hndocrinol Metab 4:309-314
    • (1993) Trends Hndocrinol Metab , vol.4 , pp. 309-314
    • Segre, G.V.1    Goldring, S.R.2
  • 7
    • 0028844199 scopus 로고
    • Molecular cloning and functional expression of a third isoform of the human calcitonin receptor and partial characterization of the calcitonin receptor gene
    • Albrandt K, Brady EMG, Moore CX, Mull E, Sierzega ME, Beaumont K 1995 Molecular cloning and functional expression of a third isoform of the human calcitonin receptor and partial characterization of the calcitonin receptor gene. Endocrinology 136:5377-5384
    • (1995) Endocrinology , vol.136 , pp. 5377-5384
    • Albrandt, K.1    Brady, E.M.G.2    Moore, C.X.3    Mull, E.4    Sierzega, M.E.5    Beaumont, K.6
  • 8
    • 0029013212 scopus 로고
    • Expression of two human skeletal calcitonin receptor isoforms cloned from a giant cell tumor of bone. the first intracellular domain modulates ligand binding and signal transduction
    • Gorn AH, Rudolph SM, Flannery MR, Morion CC, Weremowicz S, Wang J-T, Krane SM, Goldring SR 1995 Expression of two human skeletal calcitonin receptor isoforms cloned from a giant cell tumor of bone. The first intracellular domain modulates ligand binding and signal transduction. J Clin Invest 95:2680-2691
    • (1995) J Clin Invest , vol.95 , pp. 2680-2691
    • Gorn, A.H.1    Rudolph, S.M.2    Flannery, M.R.3    Morion, C.C.4    Weremowicz, S.5    Wang, J.-T.6    Krane, S.M.7    Goldring, S.R.8
  • 9
    • 0028126645 scopus 로고
    • Inhibition of inositol phosphate second messenger formation by intracellular loop one of a human calcitonin receptor. Expression and mutational analysis of synthetic receptor genes
    • Nussenzveig DR, Thaw CN, Gershengorn MC 1994 Inhibition of inositol phosphate second messenger formation by intracellular loop one of a human calcitonin receptor. Expression and mutational analysis of synthetic receptor genes. J Biol Chem 269:28123-28129
    • (1994) J Biol Chem , vol.269 , pp. 28123-28129
    • Nussenzveig, D.R.1    Thaw, C.N.2    Gershengorn, M.C.3
  • 10
    • 0019917993 scopus 로고
    • Covalent cross-linking of a photoactive derivative of calcitonin to human breast cancer cell receptors
    • Moseley JM, Findlay DM, Martin TJ, Gorman JJ 1982 Covalent cross-linking of a photoactive derivative of calcitonin to human breast cancer cell receptors. J Biol Chem 257:5846-5851
    • (1982) J Biol Chem , vol.257 , pp. 5846-5851
    • Moseley, J.M.1    Findlay, D.M.2    Martin, T.J.3    Gorman, J.J.4
  • 11
  • 13
    • 0025607860 scopus 로고
    • Expression cloning of a cDNA encoding the mouse pituitary thyrotropin-releasing hormone receptor
    • Straub RE, Frech GC, Joho RH, Gershengorn MC 1990 Expression cloning of a cDNA encoding the mouse pituitary thyrotropin-releasing hormone receptor, Proc Natl Acad Sci USA 87:9514-9518
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9514-9518
    • Straub, R.E.1    Frech, G.C.2    Joho, R.H.3    Gershengorn, M.C.4
  • 14
    • 0026496893 scopus 로고
    • Thyrotropinreleasing hormone binding to the mouse pituitary receptor does not involve ionic interactions. A model for neutral binding to G protein-coupled receptors
    • Perlman JH, Nussenzveig DR, Osman R, Gershengorn MC 1992 Thyrotropinreleasing hormone binding to the mouse pituitary receptor does not involve ionic interactions. A model for neutral binding to G protein-coupled receptors. J Biol Chem 267:24413-24417
    • (1992) J Biol Chem , vol.267 , pp. 24413-24417
    • Perlman, J.H.1    Nussenzveig, D.R.2    Osman, R.3    Gershengorn, M.C.4
  • 15
    • 8044252443 scopus 로고
    • Immunoprecipitation of FLAG fusion proteins with the anti-FLAG M1 and M2 antibodies
    • Shelness GS 1992 Immunoprecipitation of FLAG fusion proteins with the anti-FLAG M1 and M2 antibodies. Epitope 1:11-12
    • (1992) Epitope , vol.1 , pp. 11-12
    • Shelness, G.S.1
  • 16
    • 0028925811 scopus 로고
    • Chimeric human calcitonin and glucagon receptors reveal two dissociable calcitonin interaction sites
    • Stroop SD, Kuestner RE, Serwold TF, Chen L, Moore EE 1995 Chimeric human calcitonin and glucagon receptors reveal two dissociable calcitonin interaction sites. Biochemistry 34:1050-1057
    • (1995) Biochemistry , vol.34 , pp. 1050-1057
    • Stroop, S.D.1    Kuestner, R.E.2    Serwold, T.F.3    Chen, L.4    Moore, E.E.5
  • 17
    • 0030043737 scopus 로고    scopus 로고
    • Deletions of portions of the extracellular loops of the lutropin choriogonadotropin receptor decrease the binding affinity for ovine luteinizing hormone, but not human choriogonadotropin, by preventing the formation of mature cell surface receptor
    • Abell A, Liu XB, Segaloff DL 1996 Deletions of portions of the extracellular loops of the lutropin choriogonadotropin receptor decrease the binding affinity for ovine luteinizing hormone, but not human choriogonadotropin, by preventing the formation of mature cell surface receptor. J Biol Chem 271:4518-4527
    • (1996) J Biol Chem , vol.271 , pp. 4518-4527
    • Abell, A.1    Liu, X.B.2    Segaloff, D.L.3
  • 18
    • 0028842897 scopus 로고
    • Intracellular retention of mutant gonadotropin receptors results in loss of hormone binding activity of the follitropin receptor but not the lutropin/choriogonadotropin receptor
    • Rozell TG, Wang HY, Liu XB, Segaloff DL 1995 Intracellular retention of mutant gonadotropin receptors results in loss of hormone binding activity of the follitropin receptor but not the lutropin/choriogonadotropin receptor. Mol Endocrinol 9:1727-1736
    • (1995) Mol Endocrinol , vol.9 , pp. 1727-1736
    • Rozell, T.G.1    Wang, H.Y.2    Liu, X.B.3    Segaloff, D.L.4
  • 19
    • 0028138240 scopus 로고
    • Structure and function in rhodopsin. Requirements of a specific structure for the intradiscal domain
    • Anukanth A, Khorana HG 1994 Structure and function in rhodopsin. Requirements of a specific structure for the intradiscal domain. J Biol Chem 269:19738-19744
    • (1994) J Biol Chem , vol.269 , pp. 19738-19744
    • Anukanth, A.1    Khorana, H.G.2
  • 20
    • 0028354244 scopus 로고
    • Structure and function in rhodopsin: The role of asparagine-linked glycosylation
    • Kaushal S, Ridge KD, Khorana HG 1994 Structure and function in rhodopsin: the role of asparagine-linked glycosylation. Proc Natl Acad Sci USA 91:4024-4028
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4024-4028
    • Kaushal, S.1    Ridge, K.D.2    Khorana, H.G.3
  • 21
    • 0025306687 scopus 로고
    • Role of the intradiscal domain in rhodopsin assembly and function
    • Doi T, Molday RS, Khorana HG 1990 Role of the intradiscal domain in rhodopsin assembly and function. Proc Natl Acad Sci USA 87:4991-4995
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4991-4995
    • Doi, T.1    Molday, R.S.2    Khorana, H.G.3
  • 22
    • 0026511824 scopus 로고
    • Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells
    • Dorner AJ, Walsey LC, Kaufman RJ 1992 Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J 11:1563-1571
    • (1992) EMBO J , vol.11 , pp. 1563-1571
    • Dorner, A.J.1    Walsey, L.C.2    Kaufman, R.J.3
  • 23
    • 0028321726 scopus 로고
    • Protein disulficle isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A, Gilbert HF 1994 Protein disulficle isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J Biol Chem 269:7764-7771
    • (1994) J Biol Chem , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 24
    • 0028242359 scopus 로고
    • The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulficle isomerase
    • Puig A, Lyles MM, Noiva R, Gilbert HF 1994 The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulficle isomerase. J Biol Chem 269:19128-19135
    • (1994) J Biol Chem , vol.269 , pp. 19128-19135
    • Puig, A.1    Lyles, M.M.2    Noiva, R.3    Gilbert, H.F.4
  • 25
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley NJ, Baker EK, Stamnes MA, Zuker CS 1991 The cyclophilin homolog ninaA is required in the secretory pathway. Cell 67:255-263
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1    Baker, E.K.2    Stamnes, M.A.3    Zuker, C.S.4
  • 26
    • 0028143610 scopus 로고
    • The cyclophilin homolog nina a functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker EK, Colley NJ, Zuker CS 1994 The cyclophilin homolog nina A functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J 13:4886-4895
    • (1994) EMBO J , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 27
    • 0019845444 scopus 로고
    • Mutation that selectively affects rhodopsin concentration in the peripheral photoreceptors of Drosophila melanogaster
    • Larrivee DC 1981 Mutation that selectively affects rhodopsin concentration in the peripheral photoreceptors of Drosophila melanogaster. J Gen Physiol 78:521-545
    • (1981) J Gen Physiol , vol.78 , pp. 521-545
    • Larrivee, D.C.1
  • 28
    • 0029112610 scopus 로고
    • Retina-specifically expressed novel subtypes of bovine cyclophilin
    • Ferreira PA, Horn JT, Pak WL 1995 Retina-specifically expressed novel subtypes of bovine cyclophilin. J Biol Chem 270:23179-23188
    • (1995) J Biol Chem , vol.270 , pp. 23179-23188
    • Ferreira, P.A.1    Horn, J.T.2    Pak, W.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.