메뉴 건너뛰기




Volumn 141, Issue 1-2, 1998, Pages 163-177

Casein secretion in mammary tissue: Tonic regulation of basal secretion by protein kinase A

Author keywords

Casein; Lactation; Mammary tissue; Protein kinase A; Secretion

Indexed keywords

CASEIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; MEMBRANE ENZYME;

EID: 0032566067     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(98)00080-X     Document Type: Article
Times cited : (16)

References (64)
  • 1
    • 0025367731 scopus 로고
    • A method for measuring protein kinase C activity in permeabilized T lymphocytes by using peptide substrates: Evidence for multiple pathways of kinase activation
    • Alexander D.R., Graves J.D., Lucas S.C., Cantrell D.A., Crumpton M.J. A method for measuring protein kinase C activity in permeabilized T lymphocytes by using peptide substrates: evidence for multiple pathways of kinase activation. Biochem. J. 268:1990;303-308.
    • (1990) Biochem. J. , vol.268 , pp. 303-308
    • Alexander, D.R.1    Graves, J.D.2    Lucas, S.C.3    Cantrell, D.A.4    Crumpton, M.J.5
  • 2
    • 0031577590 scopus 로고    scopus 로고
    • N-myristoylation of the catalytic subunit of cAMP-dependent protein kinase in Caenorhabditis elegans
    • Aspbury R.A., Fisher M.J., Rees H.H., Clegg R.A. N-myristoylation of the catalytic subunit of cAMP-dependent protein kinase in Caenorhabditis elegans. Biochem. Biophys. Res. Commun. 238:1997;523-527.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 523-527
    • Aspbury, R.A.1    Fisher, M.J.2    Rees, H.H.3    Clegg, R.A.4
  • 3
    • 0028491081 scopus 로고
    • The cAMP-dependent protein kinases and cAMP signal transduction
    • Beebe S.J. The cAMP-dependent protein kinases and cAMP signal transduction. Sem. Cancer Biol. 5:1994;285-294.
    • (1994) Sem. Cancer Biol. , vol.5 , pp. 285-294
    • Beebe, S.J.1
  • 4
    • 0023259178 scopus 로고
    • Measurement of acetyl-CoA carboxylase activity in isolated hepatocytes
    • Bijleveld C., Geelen M.J.H. Measurement of acetyl-CoA carboxylase activity in isolated hepatocytes. Biochim. Biophys. Acta. 918:1987;274-283.
    • (1987) Biochim. Biophys. Acta. , vol.918 , pp. 274-283
    • Bijleveld, C.1    Geelen, M.J.H.2
  • 5
    • 0027271929 scopus 로고
    • Exocytosis of vacuolar apical compartment VAC in Madin-Darby canine kidney epithelial cells: CAMP is involved as a second messenger
    • Brignoni M., Podesta E.J., Mele P., Rodriguez M.L., Vega-Salas D.E., Salas P.J.I. Exocytosis of vacuolar apical compartment VAC in Madin-Darby canine kidney epithelial cells: cAMP is involved as a second messenger. Exp. Cell Res. 205:1993;171-178.
    • (1993) Exp. Cell Res. , vol.205 , pp. 171-178
    • Brignoni, M.1    Podesta, E.J.2    Mele, P.3    Rodriguez, M.L.4    Vega-Salas, D.E.5    Salas, P.J.I.6
  • 8
    • 0023744786 scopus 로고
    • Regulation of fatty acid uptake and synthesis in mammary and adipose tissues: Contrasting roles for cyclic AMP
    • Clegg R.A. Regulation of fatty acid uptake and synthesis in mammary and adipose tissues: contrasting roles for cyclic AMP. Curr. Top. Cell. Reg. 29:1988;77-128.
    • (1988) Curr. Top. Cell. Reg. , vol.29 , pp. 77-128
    • Clegg, R.A.1
  • 9
    • 0030696349 scopus 로고    scopus 로고
    • Cellular uptake and metabolism of myristoylated N-terminal peptides of PKA C-subunit
    • Clegg R.A., Beattie J. Cellular uptake and metabolism of myristoylated N-terminal peptides of PKA C-subunit. Biochem. Soc. Trans. 35:1997;S679.
    • (1997) Biochem. Soc. Trans. , vol.35 , pp. 679
    • Clegg, R.A.1    Beattie, J.2
  • 10
    • 0025856049 scopus 로고
    • Cyclic AMP-dependent protein kinase in mammary epithelial cells: Activity and subcellular distribution are acutely modulated by isoprenaline
    • Clegg R.A., Connor K. Cyclic AMP-dependent protein kinase in mammary epithelial cells: activity and subcellular distribution are acutely modulated by isoprenaline. Cell. Signal. 3:1991;201-208.
    • (1991) Cell. Signal. , vol.3 , pp. 201-208
    • Clegg, R.A.1    Connor, K.2
  • 11
    • 0022386766 scopus 로고
    • Acute change in the cyclic AMP content of rat mammary acinin in vitro: Influence of physiological and pharmacological agents
    • Clegg R.A., Mullaney I. Acute change in the cyclic AMP content of rat mammary acinin in vitro: influence of physiological and pharmacological agents. Biochem. J. 230:1985;239-246.
    • (1985) Biochem. J. , vol.230 , pp. 239-246
    • Clegg, R.A.1    Mullaney, I.2
  • 12
    • 0022997284 scopus 로고
    • Modulation of intracellular cyclic AMP content and rate of lipogenesis in mammary acini in vitro
    • Clegg R.A., Mullaney I., Robson N. A., Zammit V.A. Modulation of intracellular cyclic AMP content and rate of lipogenesis in mammary acini in vitro. Biochem. J. 240:1986;13-18.
    • (1986) Biochem. J. , vol.240 , pp. 13-18
    • Clegg, R.A.1    Mullaney, I.2    Robson, N.A.3    Zammit, V.A.4
  • 13
    • 0023088809 scopus 로고
    • Protein phosphorylation in rat mammary acinin and in cytosol preparations in vitro: Phosphorylation of acetyl-CoA carboxylase is unaffected by cyclic AMP
    • Clegg R.A., West D.W., Aitchison R.E.D. Protein phosphorylation in rat mammary acinin and in cytosol preparations in vitro: phosphorylation of acetyl-CoA carboxylase is unaffected by cyclic AMP. Biochem. J. 241:1987;447-454.
    • (1987) Biochem. J. , vol.241 , pp. 447-454
    • Clegg, R.A.1    West, D.W.2    Aitchison, R.E.D.3
  • 14
    • 0027408422 scopus 로고
    • Transport of casein submicelles and formation of secretion granules in the Golgi apparatus of epithelial cells of the lactating mammary gland of the rat
    • Clermont Y., Xia L., Rambourg A., Turner J.D., Hermo L. Transport of casein submicelles and formation of secretion granules in the Golgi apparatus of epithelial cells of the lactating mammary gland of the rat. Anat. Rec. 235:1993;363-373.
    • (1993) Anat. Rec. , vol.235 , pp. 363-373
    • Clermont, Y.1    Xia, L.2    Rambourg, A.3    Turner, J.D.4    Hermo, L.5
  • 15
    • 0026522343 scopus 로고
    • Evidence for the regulation of exocytic transport by protein phosphorylation
    • Davidson H.W., McGowan C.H., Balch W.E. Evidence for the regulation of exocytic transport by protein phosphorylation. J. Cell Biol. 116:1992;1343-1355.
    • (1992) J. Cell Biol. , vol.116 , pp. 1343-1355
    • Davidson, H.W.1    McGowan, C.H.2    Balch, W.E.3
  • 17
    • 0030219389 scopus 로고    scopus 로고
    • More on target with protein phosphorylation: Conferring specificity by location
    • Faux M.C., Scott J.D. More on target with protein phosphorylation: conferring specificity by location. TIBS. 21:1996;312-315.
    • (1996) TIBS , vol.21 , pp. 312-315
    • Faux, M.C.1    Scott, J.D.2
  • 18
    • 0017225443 scopus 로고
    • Involvement of vesicle coat material in casein secretion and surface regeneration
    • Franke W.W., Lüder M.R., Kartenbeck J., Zerbeu H., Keenan T.W. Involvement of vesicle coat material in casein secretion and surface regeneration. J. Cell Biol. 69:1976;173-195.
    • (1976) J. Cell Biol. , vol.69 , pp. 173-195
    • Franke, W.W.1    Lüder, M.R.2    Kartenbeck, J.3    Zerbeu, H.4    Keenan, T.W.5
  • 19
    • 0027969290 scopus 로고
    • Cyclic AMP-dependent protein kinase in rat mammary tissue: Expression of catalytic and regulatory subunits throughout pregnancy and lactation
    • Gardner R.A., Travers M.T., Barber M.C., Miller W.R., Clegg R.A. Cyclic AMP-dependent protein kinase in rat mammary tissue: expression of catalytic and regulatory subunits throughout pregnancy and lactation. Biochem. J. 301:1994;807-812.
    • (1994) Biochem. J. , vol.301 , pp. 807-812
    • Gardner, R.A.1    Travers, M.T.2    Barber, M.C.3    Miller, W.R.4    Clegg, R.A.5
  • 20
    • 0024996699 scopus 로고
    • Ultrastructural localization of the regulatory RII subunit of cyclic AMP-dependent protein kinase to subcellular compartments active in endocytosis and recycling of membrane receptors
    • Griffiths G., Hollinstead R., Hemmings B.A., Nigg E.A. Ultrastructural localization of the regulatory RII subunit of cyclic AMP-dependent protein kinase to subcellular compartments active in endocytosis and recycling of membrane receptors. J. Cell Sci. 96:1990;691-703.
    • (1990) J. Cell Sci. , vol.96 , pp. 691-703
    • Griffiths, G.1    Hollinstead, R.2    Hemmings, B.A.3    Nigg, E.A.4
  • 21
    • 0028167863 scopus 로고
    • sα stimulates trancytosis and apical secretion in MDCK cells through cAMP and protein kinase A
    • sα stimulates trancytosis and apical secretion in MDCK cells through cAMP and protein kinase A. J. Cell Biol. 126:1994;677-687.
    • (1994) J. Cell Biol. , vol.126 , pp. 677-687
    • Hansen, S.H.1    Casanova, J.E.2
  • 22
    • 0027527671 scopus 로고
    • Movement of the free catalytic subunit of cAMP-dependent protein kinase into and out of the nucleus can be explained by diffusion
    • Harootunian A.T., Adams S.R., Wen W., Meinkoth J.L., Taylor S.S., Tsien R.Y. Movement of the free catalytic subunit of cAMP-dependent protein kinase into and out of the nucleus can be explained by diffusion. Mol. Biol. Cell. 4:1993;993-1002.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 993-1002
    • Harootunian, A.T.1    Adams, S.R.2    Wen, W.3    Meinkoth, J.L.4    Taylor, S.S.5    Tsien, R.Y.6
  • 23
    • 0030029836 scopus 로고    scopus 로고
    • Cyclic AMP and chloride-dependent regulation of the apical constitutive secretory pathway in colonic epithelial cells
    • Jilling T., Kirk K.L. Cyclic AMP and chloride-dependent regulation of the apical constitutive secretory pathway in colonic epithelial cells. J. Biol. Chem. 271:1996;4381-4387.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4381-4387
    • Jilling, T.1    Kirk, K.L.2
  • 24
    • 0024060464 scopus 로고
    • Immunoelectron microscopic localization of catalytic and regulatory subunits of cAMP-dependent protein kinases in the parotid gland
    • Joachim S., Schwoch G. Immunoelectron microscopic localization of catalytic and regulatory subunits of cAMP-dependent protein kinases in the parotid gland. Eur. J. Cell Biol. 46:1988;491-498.
    • (1988) Eur. J. Cell Biol. , vol.46 , pp. 491-498
    • Joachim, S.1    Schwoch, G.2
  • 25
    • 0025034634 scopus 로고
    • Localisation of cAMP-dependent protein kinase subunits along the secretory pathway in pancreatic and parotid acinar cells and accumulation of the catalytic subunit in parotid secretory granules following β-adrenergic stimulation
    • Joachim S., Schwoch G. Localisation of cAMP-dependent protein kinase subunits along the secretory pathway in pancreatic and parotid acinar cells and accumulation of the catalytic subunit in parotid secretory granules following β-adrenergic stimulation. Eur. J. Cell. Biol. 51:1990;76-84.
    • (1990) Eur. J. Cell. Biol. , vol.51 , pp. 76-84
    • Joachim, S.1    Schwoch, G.2
  • 26
    • 0027240379 scopus 로고
    • A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network
    • Jones S.M., Crosby J.R., Salamero J., Howell K.E. A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans-Golgi network. J. Cell Biol. 122:1993;775-788.
    • (1993) J. Cell Biol. , vol.122 , pp. 775-788
    • Jones, S.M.1    Crosby, J.R.2    Salamero, J.3    Howell, K.E.4
  • 27
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4: I. DNA packaging events
    • Laemmli U.K., Favre M. Maturation of the head of bacteriophage T4: I. DNA packaging events. J. Mol. Biol. 80:1973;575-599.
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 28
    • 0024443061 scopus 로고
    • Forskolin: A specific stimulation of adenylyl cyclase or a diterpene with multiple sites of action?
    • Laurenza A., McHugh Sutkowski E., Seamon K.B. Forskolin: a specific stimulation of adenylyl cyclase or a diterpene with multiple sites of action? TIPS Reviews. 10:1989;442-447.
    • (1989) TIPS Reviews. , vol.10 , pp. 442-447
    • Laurenza, A.1    McHugh Sutkowski, E.2    Seamon, K.B.3
  • 29
    • 0027072502 scopus 로고
    • Multiple trimeric G-proteins on the Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation
    • Leyte A., Barr F.A., Kehlenbach R.H., Huttner W.B. Multiple trimeric G-proteins on the Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation. EMBO J. 11:1992;4795-4804.
    • (1992) EMBO J. , vol.11 , pp. 4795-4804
    • Leyte, A.1    Barr, F.A.2    Kehlenbach, R.H.3    Huttner, W.B.4
  • 30
    • 0018227745 scopus 로고
    • Ultrastructural changes in lactating guinea pig mammary gland slices associated with theophylline inhibition of lactose synthesis
    • Loizzi R.F., Amato P.A. Ultrastructural changes in lactating guinea pig mammary gland slices associated with theophylline inhibition of lactose synthesis. Cytobios. 22:1978;47-67.
    • (1978) Cytobios , vol.22 , pp. 47-67
    • Loizzi, R.F.1    Amato, P.A.2
  • 31
    • 0025117591 scopus 로고
    • β-adrenergic receptors in the rat mammary gland during pregnancy and lactation: Characterization, distribution and coupling to adenylate cyclase
    • Marchetti B., Fortier M.A., Poyet P., Follea N., Peletier G., Labrie F. β-adrenergic receptors in the rat mammary gland during pregnancy and lactation: characterization, distribution and coupling to adenylate cyclase. Endocrinology. 126:1990;565-574.
    • (1990) Endocrinology , vol.126 , pp. 565-574
    • Marchetti, B.1    Fortier, M.A.2    Poyet, P.3    Follea, N.4    Peletier, G.5    Labrie, F.6
  • 32
    • 0019400281 scopus 로고
    • Phosphorylation of caseins, present evidence for an amino acid triplet code post-translationally recognized by specific kinases
    • Mercier J.C. Phosphorylation of caseins, present evidence for an amino acid triplet code post-translationally recognized by specific kinases. Biochimie. 63:1981;1-17.
    • (1981) Biochimie , vol.63 , pp. 1-17
    • Mercier, J.C.1
  • 33
    • 0029843580 scopus 로고    scopus 로고
    • A regulatory role for cAMPdependent protein kinase in protein traffic along the exocytic route
    • Muñiz M., Alonso M., Hidalgo J., Velasco A. A regulatory role for cAMPdependent protein kinase in protein traffic along the exocytic route. J. Biol. Chem. 271:1996;30935-30941.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30935-30941
    • Muñiz, M.1    Alonso, M.2    Hidalgo, J.3    Velasco, A.4
  • 34
    • 0031474609 scopus 로고    scopus 로고
    • Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network
    • Muñiz M., Martín M.E., Hidalgo J., Velasco A. Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network. Proc. Natl. Acad. Sci. USA. 94:1997;14461-14466.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14461-14466
    • Muñiz, M.1    Martín, M.E.2    Hidalgo, J.3    Velasco, A.4
  • 35
    • 0022363913 scopus 로고
    • Cyclic-AMP-dependent protein kinase type II is associated with the Golgi complex and with centrosomes
    • Nigg E.A., Schäffer G., Hilz H., Eppenberger H.M. Cyclic-AMP-dependent protein kinase type II is associated with the Golgi complex and with centrosomes. Cell. 41:1985;1039-1051.
    • (1985) Cell , vol.41 , pp. 1039-1051
    • Nigg, E.A.1    Schäffer, G.2    Hilz, H.3    Eppenberger, H.M.4
  • 36
    • 0027938942 scopus 로고
    • Phosphorylation of rabphilin-3A, a putative target protein for Rab 3A, by cyclic AMP-dependent protein kinase
    • Numata S.I., Shirataki H., Hagi S., Yamamoto T., Takai Y. Phosphorylation of rabphilin-3A, a putative target protein for Rab 3A, by cyclic AMP-dependent protein kinase. Biochem. Biophys. Res. Com. 203:1994;1927-1934.
    • (1994) Biochem. Biophys. Res. Com. , vol.203 , pp. 1927-1934
    • Numata, S.I.1    Shirataki, H.2    Hagi, S.3    Yamamoto, T.4    Takai, Y.5
  • 37
    • 0028239912 scopus 로고
    • GTPases: Multifunctional molecular switches regulating vesicular traffic
    • Nuoffer C., Balch W.E. GTPases: multifunctional molecular switches regulating vesicular traffic. Annu. Rev. Biochem. 63:1994;949-990.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 949-990
    • Nuoffer, C.1    Balch, W.E.2
  • 38
    • 0016711037 scopus 로고
    • High resolution two-dimensional gel electrophoresis of proteins
    • O'Farrell P.H. High resolution two-dimensional gel electrophoresis of proteins. J. Biol. Chem. 250:1975;4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 39
    • 0028033742 scopus 로고
    • An elevation of cytosolic protein phosphorylation modulates trimeric G-protein regulation of secretory vesicle formation from the trans-Golgi network
    • Ohashi M., Huttner W.B. An elevation of cytosolic protein phosphorylation modulates trimeric G-protein regulation of secretory vesicle formation from the trans-Golgi network. J. Biol. Chem. 269:1994;24897-24905.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24897-24905
    • Ohashi, M.1    Huttner, W.B.2
  • 40
    • 0021356246 scopus 로고
    • Oxytocin-stimulated myosin phosphorylation in mammary myoepithelial cells: Roles of calcium ions and cyclic nucleotides
    • Olins G.M., Bremel R.D. Oxytocin-stimulated myosin phosphorylation in mammary myoepithelial cells: roles of calcium ions and cyclic nucleotides. Endocrinology. 114:1984;1617-1626.
    • (1984) Endocrinology , vol.114 , pp. 1617-1626
    • Olins, G.M.1    Bremel, R.D.2
  • 41
    • 0017305010 scopus 로고
    • Effet de l'ocytocine in vitro sur le transit intracellulaire et la secretion des proteines du lait
    • Ollivier-Bousquet M. Effet de l'ocytocine in vitro sur le transit intracellulaire et la secretion des proteines du lait. C.R. Acad. Sci. Paris. 282:1976;1433-1436.
    • (1976) C.R. Acad. Sci. Paris , vol.282 , pp. 1433-1436
    • Ollivier-Bousquet, M.1
  • 42
    • 0017872735 scopus 로고
    • Early effects of prolactin on lactating rabbit mammary gland
    • Ollivier-Bousquet M. Early effects of prolactin on lactating rabbit mammary gland. Cell Tissue Res. 187:1978;25-43.
    • (1978) Cell Tissue Res. , vol.187 , pp. 25-43
    • Ollivier-Bousquet, M.1
  • 43
    • 0024354773 scopus 로고
    • The actions of forskolin, cholera toxin and iloprost on casein secretion by lactating doe mammary glands
    • Ollivier-Bousquet M. The actions of forskolin, cholera toxin and iloprost on casein secretion by lactating doe mammary glands. Mol. Cell Endocrinol. 65:1989;27-33.
    • (1989) Mol. Cell Endocrinol. , vol.65 , pp. 27-33
    • Ollivier-Bousquet, M.1
  • 44
    • 0016747862 scopus 로고
    • Effet de l'état physiologique et du 3′ 5′ adenosine monophosphate cyclique sur le transit intracellulaire et l'excrétion des protéines du lait. Etude autoradiographique en microscopic électronique
    • Ollivier-Bousquet M., Denamur R. Effet de l'état physiologique et du 3′ 5′ adenosine monophosphate cyclique sur le transit intracellulaire et l'excrétion des protéines du lait. Etude autoradiographique en microscopic électronique. J. Microsc. Biol. Cell. 23:1975;63-82.
    • (1975) J. Microsc. Biol. Cell , vol.23 , pp. 63-82
    • Ollivier-Bousquet, M.1    Denamur, R.2
  • 45
    • 0000090018 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade G.E. Intracellular aspects of the process of protein synthesis. Science. 230:1975;25-32.
    • (1975) Science , vol.230 , pp. 25-32
    • Palade, G.E.1
  • 46
    • 0018666264 scopus 로고
    • Selected hormonal effects on protein secretion and amino acid uptake by acini from bovine mammary gland
    • Park C.S., Smith J.J., Eigel W.N., Keenan T.W. Selected hormonal effects on protein secretion and amino acid uptake by acini from bovine mammary gland. Int. J. Biochem. 10:1979;889-894.
    • (1979) Int. J. Biochem. , vol.10 , pp. 889-894
    • Park, C.S.1    Smith, J.J.2    Eigel, W.N.3    Keenan, T.W.4
  • 48
    • 0030896106 scopus 로고    scopus 로고
    • Brefeldin A differentially affects basal and prolactin-stimulated milk protein secretion in lactating rabbit mammary epithelial cells
    • Pauloin A., Delpal S., Chanat E., Lavialle F., Aubourg A., Ollivier-Bousquet M. Brefeldin A differentially affects basal and prolactin-stimulated milk protein secretion in lactating rabbit mammary epithelial cells. Eur. J. Cell. Biol. 72:1997;324-336.
    • (1997) Eur. J. Cell. Biol. , vol.72 , pp. 324-336
    • Pauloin, A.1    Delpal, S.2    Chanat, E.3    Lavialle, F.4    Aubourg, A.5    Ollivier-Bousquet, M.6
  • 49
    • 0027401264 scopus 로고
    • s class of heterotrimeric-G protein
    • s class of heterotrimeric-G protein. Nature. 362:1993;456-458.
    • (1993) Nature , vol.362 , pp. 456-458
    • Pimplikar, S.W.1    Simons, K.2
  • 50
    • 0028236891 scopus 로고
    • Activators of protein kinase A stimulate apical but not basolateral transport in Madin-Darby canine kidney cells
    • Pimplikar W., Simons K. Activators of protein kinase A stimulate apical but not basolateral transport in Madin-Darby canine kidney cells. J. Biol. Chem. 269:1994;19054-19059.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19054-19059
    • Pimplikar, W.1    Simons, K.2
  • 51
    • 0026577257 scopus 로고
    • Identification of a high affinity binding protein for the regulatory subunit RIIb of cAMP-dependent protein kinase in Golgi enriched membranes of human lymphoblasts
    • Rios R.M., Celati C., Lohmann S.M., Bornens M., Keryer G. Identification of a high affinity binding protein for the regulatory subunit RIIb of cAMP-dependent protein kinase in Golgi enriched membranes of human lymphoblasts. EMBO J. 11:1992;1723-1731.
    • (1992) EMBO J. , vol.11 , pp. 1723-1731
    • Rios, R.M.1    Celati, C.2    Lohmann, S.M.3    Bornens, M.4    Keryer, G.5
  • 52
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J.E. Mechanisms of intracellular protein transport. Nature. 372:1995;55-66.
    • (1995) Nature , vol.372 , pp. 55-66
    • Rothman, J.E.1
  • 53
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman J.E., Wieland F.T. Protein sorting by transport vesicles. Science. 272:1996;227-233.
    • (1996) Science , vol.272 , pp. 227-233
    • Rothman, J.E.1    Wieland, F.T.2
  • 54
    • 0031616441 scopus 로고    scopus 로고
    • The use of synthetic peptides in the dissection of protein-targeting interactions
    • R.A. Clegg. Totowa, NJ: Humana Press
    • Scott J.D., Faux M.C. The use of synthetic peptides in the dissection of protein-targeting interactions. Clegg R.A. Protein Targeting Protocols. 1998;161-185 Humana Press, Totowa, NJ.
    • (1998) Protein Targeting Protocols , pp. 161-185
    • Scott, J.D.1    Faux, M.C.2
  • 55
    • 0025864163 scopus 로고
    • Temperature dependence of prolactin endocytosis and casein exocytosis in epithelial mammary cells
    • Seddiki T., Ollivier-Bousquet M. Temperature dependence of prolactin endocytosis and casein exocytosis in epithelial mammary cells. Eur. J. Cell. Biol. 55:1991;60-70.
    • (1991) Eur. J. Cell. Biol. , vol.55 , pp. 60-70
    • Seddiki, T.1    Ollivier-Bousquet, M.2
  • 56
    • 0019938061 scopus 로고
    • Calcium and calcium ionophore A23187 alter protein synthesis and secretion by acini from rat mammary gland
    • Smith J.J., Park C.S., Keenan T.W. Calcium and calcium ionophore A23187 alter protein synthesis and secretion by acini from rat mammary gland. Int. J. Biochem. 14:1982;573-576.
    • (1982) Int. J. Biochem. , vol.14 , pp. 573-576
    • Smith, J.J.1    Park, C.S.2    Keenan, T.W.3
  • 58
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof T. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:1995;645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Sudhof, T.1
  • 59
    • 0025898668 scopus 로고
    • Cyclic AMP antagonist Rp-cAMPS inhibits amylase exocytosis form saponin-permeabilised parotid acini
    • Takuma T., Ichida T. Cyclic AMP antagonist Rp-cAMPS inhibits amylase exocytosis form saponin-permeabilised parotid acini. J. Biochem. 110:1991;292-294.
    • (1991) J. Biochem. , vol.110 , pp. 292-294
    • Takuma, T.1    Ichida, T.2
  • 60
    • 0028022771 scopus 로고
    • Catalytic subunit of protein kinase A induces amylase release from streptolysin O-permeabilized parotid acini
    • Takuma T., Ichida T. Catalytic subunit of protein kinase A induces amylase release from streptolysin O-permeabilized parotid acini. J. Biol. Chem. 269:1994;22124-22128.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22124-22128
    • Takuma, T.1    Ichida, T.2
  • 61
    • 0026519646 scopus 로고
    • Proteins are secreted by both constitutive and regulated secretory pathways in lactating mouse mammary epithelial cells
    • Turner M.D., Rennison M.E., Handel S.E., Wilde C.J., Burgoyne R.D. Proteins are secreted by both constitutive and regulated secretory pathways in lactating mouse mammary epithelial cells. J. Cell Biol. 117:1992;269-278.
    • (1992) J. Cell Biol. , vol.117 , pp. 269-278
    • Turner, M.D.1    Rennison, M.E.2    Handel, S.E.3    Wilde, C.J.4    Burgoyne, R.D.5
  • 62
    • 0027725135 scopus 로고
    • Differential effect of brefeldin A on phosphorylation of the caseins in lactating mouse mammary epithelial cells
    • Turner M.D., Handel S.E., Wilde C.J., Burgoyne R.D. Differential effect of brefeldin A on phosphorylation of the caseins in lactating mouse mammary epithelial cells. J. Cell Sci. 106:1993;1221-1226.
    • (1993) J. Cell Sci. , vol.106 , pp. 1221-1226
    • Turner, M.D.1    Handel, S.E.2    Wilde, C.J.3    Burgoyne, R.D.4
  • 63
    • 0029863203 scopus 로고    scopus 로고
    • Metabolism of Alzheimer β-amyloid precursor protein: Regulation by protein kinase A in intact cell and in a cell-free system
    • Xu H., Sweeney D., Greengard P., Gandy S. Metabolism of Alzheimer β-amyloid precursor protein: regulation by protein kinase A in intact cell and in a cell-free system. Proc. Natl. Acad. Sci. USA. 93:1996;4081-4084.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 4081-4084
    • Xu, H.1    Sweeney, D.2    Greengard, P.3    Gandy, S.4
  • 64
    • 0023375833 scopus 로고
    • 2 integral membrane proteins located in the cis-middle and trans-part of the Golgi system acquire sialylated N-linked carbohydrates and display different turnovers and sensitivity to cAMP-dependent phosphorylation
    • Yuan L., Barriocanal J.G., Bonifacio J.S., Sandoval I.V. 2 integral membrane proteins located in the cis-middle and trans-part of the Golgi system acquire sialylated N-linked carbohydrates and display different turnovers and sensitivity to cAMP-dependent phosphorylation. J. Cell Biol. 105:1987;215-227.
    • (1987) J. Cell Biol. , vol.105 , pp. 215-227
    • Yuan, L.1    Barriocanal, J.G.2    Bonifacio, J.S.3    Sandoval, I.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.