메뉴 건너뛰기




Volumn 183, Issue 2, 2000, Pages 228-237

Developmental expression and assembly of connexins into homomeric and heteromeric gap junction hemichannels in the mouse mammary gland

Author keywords

[No Author keywords available]

Indexed keywords

CONNEXIN 26; CONNEXIN 32; GAP JUNCTION PROTEIN;

EID: 0034115524     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(200005)183:2<228::AID-JCP9>3.0.CO;2-Y     Document Type: Article
Times cited : (71)

References (57)
  • 1
    • 0033560718 scopus 로고    scopus 로고
    • Synthesis and assembly of connexins in vitro into homomeric and heteromeric functional gap junction hemichannels
    • Ahmed S, Diez JA, George CH, Evans WH. 1999. Synthesis and assembly of connexins in vitro into homomeric and heteromeric functional gap junction hemichannels. Biochem J 339:247-253.
    • (1999) Biochem J , vol.339 , pp. 247-253
    • Ahmed, S.1    Diez, J.A.2    George, C.H.3    Evans, W.H.4
  • 2
    • 0021256942 scopus 로고
    • Electrical potentials and cell-to-cell dye movements in mouse mammary gland during lactation
    • Berga SE. 1984. Electrical potentials and cell-to-cell dye movements in mouse mammary gland during lactation. Am J Physiol 247:C20-C25.
    • (1984) Am J Physiol , vol.247
    • Berga, S.E.1
  • 4
    • 0032579554 scopus 로고    scopus 로고
    • Isoform composition of connexin channels determines selectivity among second messengers and uncharged molecules
    • Bevans CG, Kordel M, Rhee SK, Harris AL. 1998. Isoform composition of connexin channels determines selectivity among second messengers and uncharged molecules. J Biol Chem 273:2808-2816.
    • (1998) J Biol Chem , vol.273 , pp. 2808-2816
    • Bevans, C.G.1    Kordel, M.2    Rhee, S.K.3    Harris, A.L.4
  • 5
    • 0029060788 scopus 로고
    • Mutations of connexin43 gap junction gene in patients with heart malformations and aspects of laterality
    • Britz-Cunningham SH, Shah MM, Zuppan CW, Fletcher WH. 1995. Mutations of connexin43 gap junction gene in patients with heart malformations and aspects of laterality. New Engl J Med 332:1323-1329.
    • (1995) New Engl J Med , vol.332 , pp. 1323-1329
    • Britz-Cunningham, S.H.1    Shah, M.M.2    Zuppan, C.W.3    Fletcher, W.H.4
  • 6
    • 0029974655 scopus 로고    scopus 로고
    • Connections with connexins: The molecular basis of direct intercellular signalling
    • Bruzzone R, White TW, Paul DL. 1996. Connections with connexins: the molecular basis of direct intercellular signalling. Eur J Biochem 238:1-27.
    • (1996) Eur J Biochem , vol.238 , pp. 1-27
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 7
    • 0028923254 scopus 로고
    • Single channel behaviour of recombinant beta 2 gap junction connexons reconstituted into planar lipid bilayers
    • Buehler LK, Stauffer KA, Gilula NB, Kumar NM. 1995. Single channel behaviour of recombinant beta 2 gap junction connexons reconstituted into planar lipid bilayers. Biophys J 68:1767-1775.
    • (1995) Biophys J , vol.68 , pp. 1767-1775
    • Buehler, L.K.1    Stauffer, K.A.2    Gilula, N.B.3    Kumar, N.M.4
  • 8
    • 0030696315 scopus 로고    scopus 로고
    • Two different connexin 26 mutations in an inbred kindred segregating non-syndromic recessive deafness: Implications for genetic studies in isolated populations
    • Carrasquillo MM, Zlotogora J, Barges S, Chakravarti A. 1997. Two different connexin 26 mutations in an inbred kindred segregating non-syndromic recessive deafness: implications for genetic studies in isolated populations. Hum Mol Genet 6:2163-2172.
    • (1997) Hum Mol Genet , vol.6 , pp. 2163-2172
    • Carrasquillo, M.M.1    Zlotogora, J.2    Barges, S.3    Chakravarti, A.4
  • 9
    • 0030013824 scopus 로고    scopus 로고
    • Porcine aortic endothelial gap junctions: Identification and permeation by caged InsP3
    • Carter TD, Chen XY, Carlile G, Kalapothakis E, Ogden D, Evans WH. 1996. Porcine aortic endothelial gap junctions: identification and permeation by caged InsP3. J Cell Sci 109:1765-1773.
    • (1996) J Cell Sci , vol.109 , pp. 1765-1773
    • Carter, T.D.1    Chen, X.Y.2    Carlile, G.3    Kalapothakis, E.4    Ogden, D.5    Evans, W.H.6
  • 10
    • 0029096749 scopus 로고
    • Physical characterization of gap junction membrane connexons (hemi-channels) isolated from rat liver
    • Cascio M, Kumar NM, Safranik R, Gilula NB. 1995. Physical characterization of gap junction membrane connexons (hemi-channels) isolated from rat liver. J Biol Chem 270:18643-18648.
    • (1995) J Biol Chem , vol.270 , pp. 18643-18648
    • Cascio, M.1    Kumar, N.M.2    Safranik, R.3    Gilula, N.B.4
  • 12
    • 0023229231 scopus 로고
    • Expression of functional cell-cell channels from cloned rat liver gap junction complementary DNA
    • Dahl G, Miller T, Paul D, Voellmy R, Werner R. 1987. Expression of functional cell-cell channels from cloned rat liver gap junction complementary DNA. Science 236:1290-1293.
    • (1987) Science , vol.236 , pp. 1290-1293
    • Dahl, G.1    Miller, T.2    Paul, D.3    Voellmy, R.4    Werner, R.5
  • 13
    • 84965810273 scopus 로고
    • Development of mammary tumours from hyperplastic luminal nodules transplanted into gland-free mammary fat pads of female C3H mice
    • DeOme K, Faulkin K, Benn H, Blair P. 1959. Development of mammary tumours from hyperplastic luminal nodules transplanted into gland-free mammary fat pads of female C3H mice. Cancer Res 19:515-520.
    • (1959) Cancer Res , vol.19 , pp. 515-520
    • DeOme, K.1    Faulkin, K.2    Benn, H.3    Blair, P.4
  • 14
    • 0033563283 scopus 로고    scopus 로고
    • Assembly of heteromeric connexons in guinea pig liver en route to the Golgi apparatus, plasma membrane and gap junctions
    • Diez JA, Ahmed S, Evans WH. 1999. Assembly of heteromeric connexons in guinea pig liver en route to the Golgi apparatus, plasma membrane and gap junctions. Eur J Biochem 262:142-148.
    • (1999) Eur J Biochem , vol.262 , pp. 142-148
    • Diez, J.A.1    Ahmed, S.2    Evans, W.H.3
  • 16
    • 0014013791 scopus 로고
    • ++)-ATPase and 5′-nucleotidase activity of plasma membranes isolated from rat liver
    • ++)-ATPase and 5′-nucleotidase activity of plasma membranes isolated from rat liver. Biochim Biophys Acta 120:369.
    • (1966) Biochim Biophys Acta , vol.120 , pp. 369
    • Emmelot, P.1    Bos, C.2
  • 17
    • 0028077475 scopus 로고
    • Membrane insertion of gap junction connexins: Polytopic channel forming membrane proteins
    • Falk MM, Kumar NM, Gilula NB. 1994. Membrane insertion of gap junction connexins: polytopic channel forming membrane proteins. J Cell Biol 127:343-355.
    • (1994) J Cell Biol , vol.127 , pp. 343-355
    • Falk, M.M.1    Kumar, N.M.2    Gilula, N.B.3
  • 18
    • 0022423216 scopus 로고
    • Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family
    • Fort P, Marty L, Piechaczyk M, el-Sabrouty S, Dani C, Jeanteur P, Blanchard JM. 1985. Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family. Nucleic Acids Res 13:1431-1442.
    • (1985) Nucleic Acids Res , vol.13 , pp. 1431-1442
    • Fort, P.1    Marty, L.2    Piechaczyk, M.3    El-Sabrouty, S.4    Dani, C.5    Jeanteur, P.6    Blanchard, J.M.7
  • 20
    • 0032577887 scopus 로고    scopus 로고
    • Rapid determination of gap junction formation using HeLa cells microinjected with cDNAs encoding wild-type and chimeric connexins
    • George CH, Martin PE, Evans WH. 1998. Rapid determination of gap junction formation using HeLa cells microinjected with cDNAs encoding wild-type and chimeric connexins. Biochem Biophys Res Commun 247:785-789.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 785-789
    • George, C.H.1    Martin, P.E.2    Evans, W.H.3
  • 21
  • 22
    • 0017655195 scopus 로고
    • Hydrodynamic properties of the beta-adrenergic receptor and adenylate cyclase from wild type and variant S49 lymphoma cells
    • Haga T, Haga K, Gilman AG. 1977. Hydrodynamic properties of the beta-adrenergic receptor and adenylate cyclase from wild type and variant S49 lymphoma cells. J Biol Chem 252:5776-5582.
    • (1977) J Biol Chem , vol.252 , pp. 5776-15582
    • Haga, T.1    Haga, K.2    Gilman, A.G.3
  • 23
    • 0030052934 scopus 로고    scopus 로고
    • Heteromeric connexons in lens gap junction channels
    • Jiang JX, Goodenough DA. 1996. Heteromeric connexons in lens gap junction channels. Proc Natl Acad Sci USA 93:1287-1291.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1287-1291
    • Jiang, J.X.1    Goodenough, D.A.2
  • 25
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar NM, Gilula NB. 1996. The gap junction communication channel. Cell 84:381-388.
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 26
    • 0028882497 scopus 로고
    • Differential regulation of distinct types of gap junction channels by similar phosphorylating conditions
    • Kwak BR, Hermans MM, De-Jonge HR, Lohmann, SM, Jongsma HJ, Chanson M. 1995. Differential regulation of distinct types of gap junction channels by similar phosphorylating conditions. Mol Biol Cell 6:1707-1719.
    • (1995) Mol Biol Cell , vol.6 , pp. 1707-1719
    • Kwak, B.R.1    Hermans, M.M.2    De-Jonge, H.R.3    Lohmann, S.M.4    Jongsma, H.J.5    Chanson, M.6
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0031953118 scopus 로고    scopus 로고
    • Assembly of chimeric connexin-aequorin proteins into functional gap junction channels: Reporting intracellular and plasma membrane calcium environments
    • Martin PE, George CH, Castro C, Kendall JM, Capel JJ, Campbell AK, Revilla A, Barrio LC, Evans WH. 1998. Assembly of chimeric connexin-aequorin proteins into functional gap junction channels: reporting intracellular and plasma membrane calcium environments. J Biol Chem 273:1719-1726.
    • (1998) J Biol Chem , vol.273 , pp. 1719-1726
    • Martin, P.E.1    George, C.H.2    Castro, C.3    Kendall, J.M.4    Capel, J.J.5    Campbell, A.K.6    Revilla, A.7    Barrio, L.C.8    Evans, W.H.9
  • 30
    • 0029677184 scopus 로고    scopus 로고
    • The mammary gland: A unique organ for the study of development and tumourigenesis
    • Medina D. 1997. The mammary gland: a unique organ for the study of development and tumourigenesis. J Mamm Gland Biol Neoplasia 1:5-20.
    • (1997) J Mamm Gland Biol Neoplasia , vol.1 , pp. 5-20
    • Medina, D.1
  • 31
    • 0023917333 scopus 로고
    • Site-directed crosslinking; establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis
    • Milligan DL, Koshland Jr DE. 1988. Site-directed crosslinking; establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. J Biol Chem 263:6268-6275.
    • (1988) J Biol Chem , vol.263 , pp. 6268-6275
    • Milligan, D.L.1    Koshland D.E., Jr.2
  • 32
    • 0028239392 scopus 로고
    • Rapid modulation of gap junction expression in mouse mammary gland during pregnancy, lactation and involution
    • Monaghan P, Perusinghe N, Carlile G, Evans WH. 1994. Rapid modulation of gap junction expression in mouse mammary gland during pregnancy, lactation and involution. J Histochem Cytochem 42: 931-938.
    • (1994) J Histochem Cytochem , vol.42 , pp. 931-938
    • Monaghan, P.1    Perusinghe, N.2    Carlile, G.3    Evans, W.H.4
  • 33
    • 0032412495 scopus 로고    scopus 로고
    • High pressure freezing for immunocytochemistry
    • Monaghan P, Perusinghe N, Muller M. 1998. High pressure freezing for immunocytochemistry. J Microsc 192:248-258.
    • (1998) J Microsc , vol.192 , pp. 248-258
    • Monaghan, P.1    Perusinghe, N.2    Muller, M.3
  • 34
    • 0030050142 scopus 로고    scopus 로고
    • Intramolecular interactions mediate pH regulation of connexin43 channels
    • Morley GE, Taffet SM, Delmar M. 1996. Intramolecular interactions mediate pH regulation of connexin43 channels. Biophys J 70:1294-1302.
    • (1996) Biophys J , vol.70 , pp. 1294-1302
    • Morley, G.E.1    Taffet, S.M.2    Delmar, M.3
  • 35
    • 0027364529 scopus 로고
    • Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER
    • Musil LS, Goodenough DA. 1993. Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER. Cell 74:1065-1077.
    • (1993) Cell , vol.74 , pp. 1065-1077
    • Musil, L.S.1    Goodenough, D.A.2
  • 37
    • 0031172696 scopus 로고    scopus 로고
    • Gap junctions: Getting the message through
    • Nicholson SM, Bruzzone R. 1997. Gap junctions: getting the message through. Curr Biol 7:R340-R344.
    • (1997) Curr Biol , vol.7
    • Nicholson, S.M.1    Bruzzone, R.2
  • 38
    • 0028921640 scopus 로고
    • Expression of a dominant negative inhibitor of intercellular communication in the early Xenopus embryo causes delamination and extrusion of cells
    • Paul DL, Yu K, Bruzzone R, Gimlich RL, Goodenough DA. 1995. Expression of a dominant negative inhibitor of intercellular communication in the early Xenopus embryo causes delamination and extrusion of cells. Development 121:371-381.
    • (1995) Development , vol.121 , pp. 371-381
    • Paul, D.L.1    Yu, K.2    Bruzzone, R.3    Gimlich, R.L.4    Goodenough, D.A.5
  • 39
    • 0029102807 scopus 로고
    • Connexins 26, 32 and 43 are expressed in virgin, pregnant and lactating mammary glands
    • Perez-Armendariz E, Luna J, Aceves C, Tapia D. 1995. Connexins 26, 32 and 43 are expressed in virgin, pregnant and lactating mammary glands. Dev Growth Differ 37:421-431.
    • (1995) Dev Growth Differ , vol.37 , pp. 421-431
    • Perez-Armendariz, E.1    Luna, J.2    Aceves, C.3    Tapia, D.4
  • 41
    • 0023879414 scopus 로고
    • A novel method for producing anti-peptide antibodies
    • Posnett DN, McGrath H, Tam JP. 1988. A novel method for producing anti-peptide antibodies. J Biol Chem 263:1719-1725.
    • (1988) J Biol Chem , vol.263 , pp. 1719-1725
    • Posnett, D.N.1    McGrath, H.2    Tam, J.P.3
  • 42
    • 0029118539 scopus 로고
    • Analysis of multiple gap junction gene products in the rodent and human mammary gland
    • Pozzi A, Risek B, Kiang DT, Gilula NB, Kumar NM. 1995. Analysis of multiple gap junction gene products in the rodent and human mammary gland. Exp Cell Res 220:212-219.
    • (1995) Exp Cell Res , vol.220 , pp. 212-219
    • Pozzi, A.1    Risek, B.2    Kiang, D.T.3    Gilula, N.B.4    Kumar, N.M.5
  • 43
    • 0019876486 scopus 로고
    • Construction and preliminary characterisation of the rat casein and alpha-lactalbumin cDNA clones
    • Richards DA, Rodgers JR, Supowit SC, Rosen JM. 1981. Construction and preliminary characterisation of the rat casein and alpha-lactalbumin cDNA clones. J Biol Chem 256:526-532.
    • (1981) J Biol Chem , vol.256 , pp. 526-532
    • Richards, D.A.1    Rodgers, J.R.2    Supowit, S.C.3    Rosen, J.M.4
  • 44
    • 0029083742 scopus 로고
    • Gap junctions revealed by freeze-fracture electron microscopy
    • Shivers RR, McVicar LK. 1995. Gap junctions revealed by freeze-fracture electron microscopy. Microsc Res Tech 31:437-445.
    • (1995) Microsc Res Tech , vol.31 , pp. 437-445
    • Shivers, R.R.1    McVicar, L.K.2
  • 45
    • 0029045856 scopus 로고
    • Strain-dependent epithelial defects in mice lacking the EGF receptor
    • Sibilia M, Wagner EF. 1995. Strain-dependent epithelial defects in mice lacking the EGF receptor. Science 269:234-238.
    • (1995) Science , vol.269 , pp. 234-238
    • Sibilia, M.1    Wagner, E.F.2
  • 46
    • 0032932108 scopus 로고    scopus 로고
    • Gap junctions: More roles and structural data
    • Simon A. 1999. Gap junctions: more roles and structural data. Trends Cell Biol 9:169-170.
    • (1999) Trends Cell Biol , vol.9 , pp. 169-170
    • Simon, A.1
  • 47
    • 0029051717 scopus 로고
    • Mixing of connexins in gap junction membrane channels
    • Sosinsky G. 1995. Mixing of connexins in gap junction membrane channels. Proc Natl Acad Sci USA 92:9210-9214.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9210-9214
    • Sosinsky, G.1
  • 49
    • 0028964217 scopus 로고
    • The gap junction proteins beta 1-connexin (connexin-32) and beta 2-connexin (connexin-26) can form heteromeric hemichannels
    • Stauffer K. 1995. The gap junction proteins beta 1-connexin (connexin-32) and beta 2-connexin (connexin-26) can form heteromeric hemichannels. J Biol Chem 270:6768-6772.
    • (1995) J Biol Chem , vol.270 , pp. 6768-6772
    • Stauffer, K.1
  • 52
    • 0016218601 scopus 로고
    • Molecular characterization of proteins in detergent solutions
    • Tanford C, Nozaki Y, Reynolds JA, Makino S. 1974. Molecular characterization of proteins in detergent solutions. Biochemistry 13: 2369-2376.
    • (1974) Biochemistry , vol.13 , pp. 2369-2376
    • Tanford, C.1    Nozaki, Y.2    Reynolds, J.A.3    Makino, S.4
  • 53
    • 0031240077 scopus 로고    scopus 로고
    • High incidence of spontaneous and chemically induced liver tumours in mice deficient for Cx32
    • Temme A, Buchmann A, Gabriel HD, Nelles E, Schwarz M, Willecke K. 1997. High incidence of spontaneous and chemically induced liver tumours in mice deficient for Cx32. Curr Biol 7:713-716.
    • (1997) Curr Biol , vol.7 , pp. 713-716
    • Temme, A.1    Buchmann, A.2    Gabriel, H.D.3    Nelles, E.4    Schwarz, M.5    Willecke, K.6
  • 54
    • 0019074917 scopus 로고
    • Multiple hormone interactions in the developmental biology of the mammary gland
    • Topper YJ, Freeman CS. 1980. Multiple hormone interactions in the developmental biology of the mammary gland. Physiol Rev 60: 1049-1106.
    • (1980) Physiol Rev , vol.60 , pp. 1049-1106
    • Topper, Y.J.1    Freeman, C.S.2
  • 55
    • 0028145283 scopus 로고
    • Developmental and hormonal regulation of Wnt gene expression in the mouse mammary gland
    • Weber-Hall SJ, Phippard DJ, Niemeyer CC, Dale TC. 1994. Developmental and hormonal regulation of Wnt gene expression in the mouse mammary gland. Differentiation 57:205-214.
    • (1994) Differentiation , vol.57 , pp. 205-214
    • Weber-Hall, S.J.1    Phippard, D.J.2    Niemeyer, C.C.3    Dale, T.C.4
  • 56
    • 0028214204 scopus 로고
    • Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: The second extracellular domain is a determinant of compatibility between connexins
    • White TW, Bruzzone R, Wolfram S, Paul DL, Goodenough DA. 1995. Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: the second extracellular domain is a determinant of compatibility between connexins. J Cell Biol 125: 879-892.
    • (1995) J Cell Biol , vol.125 , pp. 879-892
    • White, T.W.1    Bruzzone, R.2    Wolfram, S.3    Paul, D.L.4    Goodenough, D.A.5
  • 57
    • 0026480797 scopus 로고
    • Subunit intercations of vesicular stomatitis virus envelope glycoprotein influenced by detergent micelles and lipid bilayers
    • Wilcox MD, MacKenzie MO, Parce JW, Lyles DS. 1992. Subunit intercations of vesicular stomatitis virus envelope glycoprotein influenced by detergent micelles and lipid bilayers. Biochemistry 31:10458-10464.
    • (1992) Biochemistry , vol.31 , pp. 10458-10464
    • Wilcox, M.D.1    MacKenzie, M.O.2    Parce, J.W.3    Lyles, D.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.