메뉴 건너뛰기




Volumn 149, Issue 1-2, 1999, Pages 85-92

Regulation of prolactin receptor glycosylation and its role in receptor location

Author keywords

Glycosylation; Nitric oxide; Prolactin receptor; Receptor up regulation

Indexed keywords

ALPHA MANNOSIDASE; GLUCAN SYNTHASE; N ACETYLGLUCOSAMINYLTRANSFERASE; NITRIC OXIDE; PROLACTIN RECEPTOR;

EID: 0345517103     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(98)00251-2     Document Type: Article
Times cited : (9)

References (49)
  • 1
    • 0023404002 scopus 로고
    • CAMP-mediated protein phosphorylation of microsomal membranes increases mannosylphosphodolichol synthase activity
    • Banerjee D.K., Kousvelari E.E., Baum B.J. cAMP-mediated protein phosphorylation of microsomal membranes increases mannosylphosphodolichol synthase activity. Proc. Natl. Acad. Sci. USA. 84:1987;6389-6393.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6389-6393
    • Banerjee, D.K.1    Kousvelari, E.E.2    Baum, B.J.3
  • 2
    • 0021255202 scopus 로고
    • Enhanced hormonal responsiveness in mammary glands from parous mice: Molecular mechanisms
    • Bolander F.F. Enhanced hormonal responsiveness in mammary glands from parous mice: molecular mechanisms. Mol. Cell. Endocrinol. 35:1984;221-227.
    • (1984) Mol. Cell. Endocrinol. , vol.35 , pp. 221-227
    • Bolander, F.F.1
  • 3
    • 0028115058 scopus 로고
    • Regulation of the mouse mammary tumor virus receptor by phosphorylation and internalization in mammary epithelial cells
    • Bolander F.F. Regulation of the mouse mammary tumor virus receptor by phosphorylation and internalization in mammary epithelial cells. J. Cell. Physiol. 161:1994;124-128.
    • (1994) J. Cell. Physiol. , vol.161 , pp. 124-128
    • Bolander, F.F.1
  • 4
    • 0343923630 scopus 로고    scopus 로고
    • Second messengers induced by the envelope protein of a retrovirus
    • Bolander F.F. Second messengers induced by the envelope protein of a retrovirus. Mol. Cell. Endocrinol. 129:1997;27-32.
    • (1997) Mol. Cell. Endocrinol. , vol.129 , pp. 27-32
    • Bolander, F.F.1
  • 5
    • 0031795036 scopus 로고    scopus 로고
    • Transduction pathways involved in rapid hormone receptor regulation in the mammary epithelium
    • Bolander F.F. Transduction pathways involved in rapid hormone receptor regulation in the mammary epithelium. Am. J. Physiol. 275:1998;E553-E557.
    • (1998) Am. J. Physiol. , vol.275
    • Bolander, F.F.1
  • 6
    • 0016692793 scopus 로고
    • Growth hormone covalently bound to Sepharose or glass: Analysis of ligand release rates and characterization of soluble radiolabelled products
    • Bolander F.F., Fellows R.E. Growth hormone covalently bound to Sepharose or glass: analysis of ligand release rates and characterization of soluble radiolabelled products. Biochemistry. 14:1975;2938-2943.
    • (1975) Biochemistry , vol.14 , pp. 2938-2943
    • Bolander, F.F.1    Fellows, R.E.2
  • 7
    • 0019406538 scopus 로고
    • The asynchronous hormonal induction of lactose synthase components, α-lactalbumin and galactosyltransferase, in relation to lactose secretion by mouse mammary explants
    • Bolander F.F., Topper Y.J. The asynchronous hormonal induction of lactose synthase components, α-lactalbumin and galactosyltransferase, in relation to lactose secretion by mouse mammary explants. Endocrinology. 108:1981;1594-1596.
    • (1981) Endocrinology , vol.108 , pp. 1594-1596
    • Bolander, F.F.1    Topper, Y.J.2
  • 8
    • 0000498387 scopus 로고
    • A rapid method for the isolation of L-cell surface membranes using an aqueous two-phase polymer system
    • Brunette D.M., Till J.E. A rapid method for the isolation of L-cell surface membranes using an aqueous two-phase polymer system. J. Membr. Biol. 5:1990;215-224.
    • (1990) J. Membr. Biol. , vol.5 , pp. 215-224
    • Brunette, D.M.1    Till, J.E.2
  • 9
    • 0032230254 scopus 로고    scopus 로고
    • N-Glycosylation of the prolactin receptor is not required for activation of gene transcription but is crucial for its cell surface targeting
    • Buteau H., Pezet A., Ferrag F., Perrot-Applanat M., Kelly P.A., Edery M. N-Glycosylation of the prolactin receptor is not required for activation of gene transcription but is crucial for its cell surface targeting. Mol. Endocrinol. 12:1998;544-555.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 544-555
    • Buteau, H.1    Pezet, A.2    Ferrag, F.3    Perrot-Applanat, M.4    Kelly, P.A.5    Edery, M.6
  • 10
    • 0028108747 scopus 로고
    • Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system
    • Cahoreau C., Garnier L., Djiane J., Devauchelle G., Cerutti M. Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system. FEBS Lett. 350:1994;230-234.
    • (1994) FEBS Lett. , vol.350 , pp. 230-234
    • Cahoreau, C.1    Garnier, L.2    Djiane, J.3    Devauchelle, G.4    Cerutti, M.5
  • 11
    • 0030054870 scopus 로고    scopus 로고
    • Mevalonic acid is limiting for N-linked glycosylation and translocation of the insulin-like growth factor-1 receptor to the cell surface: Evidence for a new link between 3-hydroxy-3-methylglutarylcoenzyme A reductase and cell growth
    • Carlberg M., Dricy A., Blegen H., Wang M., Hjertman M., Zickert P., Höög A., Larsson O. Mevalonic acid is limiting for N-linked glycosylation and translocation of the insulin-like growth factor-1 receptor to the cell surface: evidence for a new link between 3-hydroxy-3-methylglutarylcoenzyme A reductase and cell growth. J. Biol. Chem. 271:1996;17453-17462.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17453-17462
    • Carlberg, M.1    Dricy, A.2    Blegen, H.3    Wang, M.4    Hjertman, M.5    Zickert, P.6    Höög, A.7    Larsson, O.8
  • 12
    • 0030020795 scopus 로고    scopus 로고
    • Stimulatory effect of PDGF on HMG-CoA reductase activity and N-linked glycosylation contributes to increased expression of IGF-1 receptors in human fibroblasts
    • Carlberg M., Larsson O. Stimulatory effect of PDGF on HMG-CoA reductase activity and N-linked glycosylation contributes to increased expression of IGF-1 receptors in human fibroblasts. Exp. Cell Res. 223:1996;142-148.
    • (1996) Exp. Cell Res. , vol.223 , pp. 142-148
    • Carlberg, M.1    Larsson, O.2
  • 13
    • 0027216945 scopus 로고
    • Changes in prolactin receptor expression during pregnancy in the mouse ovary
    • Clarke D.L., Linzer D.I.H. Changes in prolactin receptor expression during pregnancy in the mouse ovary. Endocrinology. 133:1993;224-232.
    • (1993) Endocrinology , vol.133 , pp. 224-232
    • Clarke, D.L.1    Linzer, D.I.H.2
  • 14
    • 0027261430 scopus 로고
    • Specific glycosylation site mutations of the insulin receptor α subunit impair intracellular transport
    • Collier E., Carpentier J.L., Beitz L., Carol H., Taylor S.I., Gorden P. Specific glycosylation site mutations of the insulin receptor α subunit impair intracellular transport. Biochemistry. 32:1993;7818-7823.
    • (1993) Biochemistry , vol.32 , pp. 7818-7823
    • Collier, E.1    Carpentier, J.L.2    Beitz, L.3    Carol, H.4    Taylor, S.I.5    Gorden, P.6
  • 15
    • 0030051035 scopus 로고    scopus 로고
    • Mutagenesis of N-glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane
    • Couvineau A., Fabre C., Gaudin P., Maoret J.J., Laburthe M. Mutagenesis of N-glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane. Biochemistry. 35:1996;1745-1752.
    • (1996) Biochemistry , vol.35 , pp. 1745-1752
    • Couvineau, A.1    Fabre, C.2    Gaudin, P.3    Maoret, J.J.4    Laburthe, M.5
  • 16
    • 0024560550 scopus 로고
    • Expression of multiple forms of the prolactin receptor in mouse liver
    • Davis J.A., Linzer D.I.H. Expression of multiple forms of the prolactin receptor in mouse liver. Mol. Endocrinol. 3:1989;674-680.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 674-680
    • Davis, J.A.1    Linzer, D.I.H.2
  • 17
    • 0029557613 scopus 로고
    • The epidermal growth factor receptor is covalently linked to ubiquitin
    • Galcheva-Gargova Z., Theroux S.J., Davis R.J. The epidermal growth factor receptor is covalently linked to ubiquitin. Oncogene. 11:1995;2649-2655.
    • (1995) Oncogene , vol.11 , pp. 2649-2655
    • Galcheva-Gargova, Z.1    Theroux, S.J.2    Davis, R.J.3
  • 18
    • 0029913968 scopus 로고    scopus 로고
    • Glycosylation, palmitoylation, and localization of the human D2S receptor in baculovirus-infected insect cells
    • Grünewald S., Haase W., Reiländer H., Michel H. Glycosylation, palmitoylation, and localization of the human D2S receptor in baculovirus-infected insect cells. Biochemistry. 35:1996;15149-15161.
    • (1996) Biochemistry , vol.35 , pp. 15149-15161
    • Grünewald, S.1    Haase, W.2    Reiländer, H.3    Michel, H.4
  • 19
    • 0031031039 scopus 로고    scopus 로고
    • Surface expression of the AMPA receptor subunits GluR1, GluR2, and GluR4 in stably transfected baby hamster kidney cells
    • Hall R.A., Hansen A., Andersen P.H., Soderling T.R. Surface expression of the AMPA receptor subunits GluR1, GluR2, and GluR4 in stably transfected baby hamster kidney cells. J. Neurochem. 68:1997;625-630.
    • (1997) J. Neurochem. , vol.68 , pp. 625-630
    • Hall, R.A.1    Hansen, A.2    Andersen, P.H.3    Soderling, T.R.4
  • 20
    • 0020074305 scopus 로고
    • A dot-immunoblotting assay for monoclonal and other antibodies
    • Hawkes R., Niday E., Gordon J. A dot-immunoblotting assay for monoclonal and other antibodies. Anal. Biochem. 119:1982;142-147.
    • (1982) Anal. Biochem. , vol.119 , pp. 142-147
    • Hawkes, R.1    Niday, E.2    Gordon, J.3
  • 21
    • 0025830641 scopus 로고
    • Prolactin receptor gene expression in rat mammary gland and liver during pregnancy and lactation
    • Jahn G.A., Edery M., Belair L., Kelly P.A., Djiane J. Prolactin receptor gene expression in rat mammary gland and liver during pregnancy and lactation. Endocrinology. 128:1991;2976-2984.
    • (1991) Endocrinology , vol.128 , pp. 2976-2984
    • Jahn, G.A.1    Edery, M.2    Belair, L.3    Kelly, P.A.4    Djiane, J.5
  • 22
  • 23
    • 0028194854 scopus 로고
    • Glycosidase inhibitors in study of glycoconjugates
    • Kaushal G.P., Elbein A.D. Glycosidase inhibitors in study of glycoconjugates. Methods Enzymol. 230:1994;316-329.
    • (1994) Methods Enzymol. , vol.230 , pp. 316-329
    • Kaushal, G.P.1    Elbein, A.D.2
  • 24
    • 0018749518 scopus 로고
    • Estimation of total prolactin-binding sites after in vitro desaturation
    • Kelly P.A., Leblanc G., Djiane J. Estimation of total prolactin-binding sites after in vitro desaturation. Endocrinology. 104:1979;1631-1638.
    • (1979) Endocrinology , vol.104 , pp. 1631-1638
    • Kelly, P.A.1    Leblanc, G.2    Djiane, J.3
  • 25
    • 0343833263 scopus 로고    scopus 로고
    • Inhibition of IGF II-induced redistribution of mannose 6-phosphate receptors by the phosphatidylinositol 3-kinase inhibitor, wortmannin
    • Körner C., Braulke T. Inhibition of IGF II-induced redistribution of mannose 6-phosphate receptors by the phosphatidylinositol 3-kinase inhibitor, wortmannin. Mol. Cell. Endocrinol. 118:1996;201-205.
    • (1996) Mol. Cell. Endocrinol. , vol.118 , pp. 201-205
    • Körner, C.1    Braulke, T.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0028437091 scopus 로고
    • Differences in both glycosylation and binding properties between rat and mouse liver prolactin receptors
    • Lascols O., Cherqui G., Munier A., Picard J., Capeau J. Differences in both glycosylation and binding properties between rat and mouse liver prolactin receptors. Cell. Mol. Biol. 40:1994;359-371.
    • (1994) Cell. Mol. Biol. , vol.40 , pp. 359-371
    • Lascols, O.1    Cherqui, G.2    Munier, A.3    Picard, J.4    Capeau, J.5
  • 29
    • 0018845674 scopus 로고
    • Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides
    • Michael J.M., Kornfeld S. Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides. Arch. Biochem. Biophys. 199:1980;249-258.
    • (1980) Arch. Biochem. Biophys. , vol.199 , pp. 249-258
    • Michael, J.M.1    Kornfeld, S.2
  • 31
    • 0028158499 scopus 로고
    • Ligand-dependent polyubiquitination of c-kit gene product: A possible mechanism of receptor down modulation in M07e cells
    • Miyazama K., Toyama K., Gotoh A., Hendrie P.C., Mantel C., Broxmeyer H.E. Ligand-dependent polyubiquitination of c-kit gene product: a possible mechanism of receptor down modulation in M07e cells. Blood. 83:1994;137-145.
    • (1994) Blood , vol.83 , pp. 137-145
    • Miyazama, K.1    Toyama, K.2    Gotoh, A.3    Hendrie, P.C.4    Mantel, C.5    Broxmeyer, H.E.6
  • 32
    • 8244254368 scopus 로고    scopus 로고
    • The regulation of the prolactin receptor gene expression in the mammary gland of early pregnant mouse
    • Mizoguchi Y., Kim J.Y., Enami J., Sakai S. The regulation of the prolactin receptor gene expression in the mammary gland of early pregnant mouse. Endocr. J. 44:1997;53-58.
    • (1997) Endocr. J. , vol.44 , pp. 53-58
    • Mizoguchi, Y.1    Kim, J.Y.2    Enami, J.3    Sakai, S.4
  • 34
    • 0028200640 scopus 로고
    • Tissue distribution and regulation of rat prolactin receptor gene expression: Quantitative analysis by polymerase chain reaction
    • Nagano M., Kelly P.A. Tissue distribution and regulation of rat prolactin receptor gene expression: quantitative analysis by polymerase chain reaction. J. Biol. Chem. 269:1994;13337-13345.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13337-13345
    • Nagano, M.1    Kelly, P.A.2
  • 36
    • 0028036423 scopus 로고
    • Progesterone and EGF inhibit mouse mammary gland prolactin receptor and β-casein gene expression
    • Nishikawa S., Moore R.C., Nonomura N., Oka T. Progesterone and EGF inhibit mouse mammary gland prolactin receptor and β-casein gene expression. Am. J. Physiol. 267:1994;C1467-C1472.
    • (1994) Am. J. Physiol. , vol.267
    • Nishikawa, S.1    Moore, R.C.2    Nonomura, N.3    Oka, T.4
  • 37
    • 0018891215 scopus 로고
    • The differential actions of cortisol on the accumulation of α-lactalbumin and casein in midpregnant mouse mammary gland in culture
    • Ono M., Oka T. The differential actions of cortisol on the accumulation of α-lactalbumin and casein in midpregnant mouse mammary gland in culture. Cell. 19:1980;473-480.
    • (1980) Cell , vol.19 , pp. 473-480
    • Ono, M.1    Oka, T.2
  • 38
    • 0026602414 scopus 로고
    • Molecular cloning and characterization of the mouse UDP-N-acetylglucosamine:α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I gene
    • Pownall S., Kozak C.A., Schappert K., Sarkar M., Hull E., Schachter H., Marth J.D. Molecular cloning and characterization of the mouse UDP-N-acetylglucosamine:α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I gene. Genomics. 12:1992;699-704.
    • (1992) Genomics , vol.12 , pp. 699-704
    • Pownall, S.1    Kozak, C.A.2    Schappert, K.3    Sarkar, M.4    Hull, E.5    Schachter, H.6    Marth, J.D.7
  • 39
    • 0028844558 scopus 로고
    • The role of N-glycosylation for functional expression of the human platelet-activating factor receptor: Glycosylation is required for efficient membrane trafficking
    • Rodríguez C.G., Cundell D.R., Tuomanen E.I., Kolakowski L.E., Gerard C., Gerard N.P. The role of N-glycosylation for functional expression of the human platelet-activating factor receptor: glycosylation is required for efficient membrane trafficking. J. Biol. Chem. 270:1995;25178-25184.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25178-25184
    • Rodríguez, C.G.1    Cundell, D.R.2    Tuomanen, E.I.3    Kolakowski, L.E.4    Gerard, C.5    Gerard, N.P.6
  • 40
    • 0028017849 scopus 로고
    • Characterization of plasma and intracellular membrane prolactin receptor in lactating mouse mammary cells
    • Sakai S., Mizoguchi Y., Kim J.Y. Characterization of plasma and intracellular membrane prolactin receptor in lactating mouse mammary cells. Endocr. J. 41:1994;249-256.
    • (1994) Endocr. J. , vol.41 , pp. 249-256
    • Sakai, S.1    Mizoguchi, Y.2    Kim, J.Y.3
  • 41
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • Scatchard G. The attractions of proteins for small molecules and ions. Ann. NY Acad. Sci. 51:1949;660-672.
    • (1949) Ann. NY Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 42
    • 0027284439 scopus 로고
    • The nitric oxide and cGMP signal transduction system: Regulation and mechanism of action
    • Schmidt H.H.H.W., Lohmann S.M., Walter U. The nitric oxide and cGMP signal transduction system: regulation and mechanism of action. Biochim. Biophys. Acta. 1178:1993;153-175.
    • (1993) Biochim. Biophys. Acta , vol.1178 , pp. 153-175
    • Schmidt, H.H.H.W.1    Lohmann, S.M.2    Walter, U.3
  • 43
    • 0030832293 scopus 로고    scopus 로고
    • Prolactin receptor heterogeneity in bovine fetal and maternal tissues
    • Schuler L.A., Nagel R.J., Gao J., Horseman N.D., Kessler M.A. Prolactin receptor heterogeneity in bovine fetal and maternal tissues. Endocrinology. 138:1997;3187-3194.
    • (1997) Endocrinology , vol.138 , pp. 3187-3194
    • Schuler, L.A.1    Nagel, R.J.2    Gao, J.3    Horseman, N.D.4    Kessler, M.A.5
  • 44
    • 0031971883 scopus 로고    scopus 로고
    • Enzyme action in glycoprotein synthesis
    • Sears P., Wong C.H. Enzyme action in glycoprotein synthesis. Cell. Mol. Life. Sci. 54:1998;223-252.
    • (1998) Cell. Mol. Life. Sci. , vol.54 , pp. 223-252
    • Sears, P.1    Wong, C.H.2
  • 45
    • 0025287809 scopus 로고
    • Developmental regulation of glucosidase I, an enzyme involved in the processing of asparagine-linked glycoproteins in rat mammary gland
    • Shailubhai K., Saxena E.S., Balapure A.K., Vijay I.K. Developmental regulation of glucosidase I, an enzyme involved in the processing of asparagine-linked glycoproteins in rat mammary gland. J. Biol. Chem. 265:1990;9701-9706.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9701-9706
    • Shailubhai, K.1    Saxena, E.S.2    Balapure, A.K.3    Vijay, I.K.4
  • 46
    • 0018801562 scopus 로고
    • Purification and characterization of a rat liver Golgi α-mannosidase capable of processing asparagine-linked oligosaccharides
    • Tabas I., Kornfeld S. Purification and characterization of a rat liver Golgi α-mannosidase capable of processing asparagine-linked oligosaccharides. J. Biol. Chem. 254:1979;11655-11663.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11655-11663
    • Tabas, I.1    Kornfeld, S.2
  • 47
    • 0019414318 scopus 로고
    • Glycosyl transferases of baby-hamster-kidney (BHK) cells and ricin-resistant mutants
    • Vischer P., Hughes R.C. Glycosyl transferases of baby-hamster-kidney (BHK) cells and ricin-resistant mutants. Eur. J. Biochem. 117:1981;275-284.
    • (1981) Eur. J. Biochem. , vol.117 , pp. 275-284
    • Vischer, P.1    Hughes, R.C.2
  • 48
    • 0022016967 scopus 로고
    • Isolation, characterization, and regulation of the prolactin receptor
    • Vonderhaar B.K., Bhattacharya A., Alhadi T. et al. Isolation, characterization, and regulation of the prolactin receptor. J. Dairy Sci. 68:1985;466-488.
    • (1985) J. Dairy Sci. , vol.68 , pp. 466-488
    • Vonderhaar, B.K.1    Bhattacharya, A.2    Alhadi, T.3
  • 49
    • 0015935064 scopus 로고
    • An early effect of prolactin on the formation of α-lactalbumin by mouse mammary epithelial cells
    • Vonderhaar B.K., Owens I.S., Topper Y.J. An early effect of prolactin on the formation of α-lactalbumin by mouse mammary epithelial cells. J. Biol. Chem. 248:1973;467-471.
    • (1973) J. Biol. Chem. , vol.248 , pp. 467-471
    • Vonderhaar, B.K.1    Owens, I.S.2    Topper, Y.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.