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Volumn 58, Issue 5, 1999, Pages 652-662

Calreticulin is transported to the surface of NG108-15 cells where it forms surface patches and is partially degraded in an acidic compartment

Author keywords

Calcium; Calreticulin; Cell surface; Degradation; KDEL proteins; NG108 15 cell

Indexed keywords

CALCIUM; CALRETICULIN; CELL PROTEIN;

EID: 0033485892     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4547(19991201)58:5<652::AID-JNR6>3.0.CO;2-H     Document Type: Article
Times cited : (30)

References (50)
  • 4
    • 0027530856 scopus 로고
    • Interactions of calreticulin with proteins of the endoplasmic and sarcoplasmic reticulum membranes
    • Burns K, Michalak M. 1993. Interactions of calreticulin with proteins of the endoplasmic and sarcoplasmic reticulum membranes. FEBS Lett 318:181-185.
    • (1993) FEBS Lett , vol.318 , pp. 181-185
    • Burns, K.1    Michalak, M.2
  • 6
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • Ciechanover A, Finley D, Varshavsky A. 1984. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 37:57-66.
    • (1984) Cell , vol.37 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 8
    • 0016277339 scopus 로고
    • The ultrastructure of neuroblastoma glioma somatic cell hybrids. Expression of neuronal characteristics stimulated by dibutyryl adenosine 3′, 5′ cyclic monophosphate
    • Daniels MP, Hamprecht B. 1974. The ultrastructure of neuroblastoma glioma somatic cell hybrids. Expression of neuronal characteristics stimulated by dibutyryl adenosine 3′, 5′ cyclic monophosphate. J Cell Biol 63:691-699.
    • (1974) J Cell Biol , vol.63 , pp. 691-699
    • Daniels, M.P.1    Hamprecht, B.2
  • 10
  • 12
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RAF, Michalak M. 1989. Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 264:21522-21528.
    • (1989) J Biol Chem , vol.264 , pp. 21522-21528
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.F.4    Michalak, M.5
  • 14
    • 0025818893 scopus 로고
    • The ubiquitin-activating enzyme, E1, is required for stress-induced lysosomal degradation of cellular proteins
    • Gropper R, Brandt RA, Elias S, Bearer CF, Mayer A, Schwartz AL, Ciechanover A. 1991. The ubiquitin-activating enzyme, E1, is required for stress-induced lysosomal degradation of cellular proteins. J Biol Chem 266:3602-3610.
    • (1991) J Biol Chem , vol.266 , pp. 3602-3610
    • Gropper, R.1    Brandt, R.A.2    Elias, S.3    Bearer, C.F.4    Mayer, A.5    Schwartz, A.L.6    Ciechanover, A.7
  • 15
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert DN, Foellmer B, Helenius A. 1996. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J 15:2961-2968.
    • (1996) EMBO J , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 16
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A, Ciechanover A. 1992. The ubiquitin system for protein degradation. Annu Rev Biochem 61:761-807.
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 17
    • 0030876616 scopus 로고    scopus 로고
    • Retrograde transport of KDEL-bearing B-fragment of shiga toxin
    • Johannes L, Tenza D, Antony C, Goud B. 1997. Retrograde transport of KDEL-bearing B-fragment of Shiga toxin. J Biol Chem 272: 19554-19561.
    • (1997) J Biol Chem , vol.272 , pp. 19554-19561
    • Johannes, L.1    Tenza, D.2    Antony, C.3    Goud, B.4
  • 18
    • 0031906941 scopus 로고    scopus 로고
    • Increased calreticulin stability in differentiated NG-108-15 cells correlates with resistance to apoptosis induced by antisense treatment
    • Johnson RJ, Liu N, Shanmugaratnam J, Fine RE. 1998. Increased calreticulin stability in differentiated NG-108-15 cells correlates with resistance to apoptosis induced by antisense treatment. Mol Brain Res 53:104-111.
    • (1998) Mol Brain Res , vol.53 , pp. 104-111
    • Johnson, R.J.1    Liu, N.2    Shanmugaratnam, J.3    Fine, R.E.4
  • 19
    • 0028214541 scopus 로고
    • Impact of ultraviolet radiation on the cellular expression of Ro/SS-A autoantigenic polypeotides
    • Kawashima T, Zappi EG, Lieu TS, Sontheimer RD. 1994. Impact of ultraviolet radiation on the cellular expression of Ro/SS-A autoantigenic polypeotides. Dermatology 189:6-10.
    • (1994) Dermatology , vol.189 , pp. 6-10
    • Kawashima, T.1    Zappi, E.G.2    Lieu, T.S.3    Sontheimer, R.D.4
  • 20
    • 0024206530 scopus 로고
    • Endocrine regulation of protein breakdown is skeletal muscle
    • Kettelhut IC, Wing SS, Goldberg AL. 1988. Endocrine regulation of protein breakdown is skeletal muscle. Diabetes Metab Rev 4:751-772.
    • (1988) Diabetes Metab Rev , vol.4 , pp. 751-772
    • Kettelhut, I.C.1    Wing, S.S.2    Goldberg, A.L.3
  • 22
    • 0026772733 scopus 로고
    • A novel di-leucine motif and a tyrosine-based motif independently mediated lysosomal targeting and endocytosis of CD3 chains
    • Letourneur F, Klausner RD. 1992. A novel di-leucine motif and a tyrosine-based motif independently mediated lysosomal targeting and endocytosis of CD3 chains. Cell 69:1143-1157.
    • (1992) Cell , vol.69 , pp. 1143-1157
    • Letourneur, F.1    Klausner, R.D.2
  • 23
    • 0028020123 scopus 로고
    • 2+ response to bradykinin and increases sensitivity to ionomycin in NG108-15 cells
    • 2+ response to bradykinin and increases sensitivity to ionomycin in NG108-15 cells. J Biol Chem 269:28635-28639.
    • (1994) J Biol Chem , vol.269 , pp. 28635-28639
    • Liu, N.1    Fine, R.E.2    Simons, E.3    Johnson, R.J.4
  • 24
    • 0024093903 scopus 로고
    • Cell lineage in the cerebral cortex of the mouse studied in vivo and in vitro with a recombinant retrovirus
    • Luskin MB, Pearlman AL, Sanes JR. 1988. Cell lineage in the cerebral cortex of the mouse studied in vivo and in vitro with a recombinant retrovirus. Neuron 1:635-647.
    • (1988) Neuron , vol.1 , pp. 635-647
    • Luskin, M.B.1    Pearlman, A.L.2    Sanes, J.R.3
  • 27
    • 0026041477 scopus 로고
    • Identification and immunolocation of calreticulin in pancreatic cells: No evidence for calcio-somes
    • Michalak M, Baksh S, Opas M. 1991. Identification and immunolocation of calreticulin in pancreatic cells: no evidence for "calcio-somes." Exp Cell Res 197:91-99.
    • (1991) Exp Cell Res , vol.197 , pp. 91-99
    • Michalak, M.1    Baksh, S.2    Opas, M.3
  • 29
    • 0029828912 scopus 로고    scopus 로고
    • Endoplasmic reticulum form of calreticulin modulates glucocorticoid-sensitive gene expression
    • Michalak M, Burns K, Andrin C, Mesaeli N, Jass GH, Busaan J, Opas M. 1996. Endoplasmic reticulum form of calreticulin modulates glucocorticoid-sensitive gene expression. J Biol Chem 271: 29436-29445.
    • (1996) J Biol Chem , vol.271 , pp. 29436-29445
    • Michalak, M.1    Burns, K.2    Andrin, C.3    Mesaeli, N.4    Jass, G.H.5    Busaan, J.6    Opas, M.7
  • 30
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S, Pelham HR. 1987. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48:899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 31
    • 0027982729 scopus 로고
    • Calreticulin, not just another calcium-binding protein
    • Nash PD, Opas M, Michalak M. 1994. Calreticulin, not just another calcium-binding protein. Mol Cell Biochem 135:71-78.
    • (1994) Mol Cell Biochem , vol.135 , pp. 71-78
    • Nash, P.D.1    Opas, M.2    Michalak, M.3
  • 32
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef WM, McCormick SJ, Clark RA. 1995. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J Biol Chem 270:4741-4747.
    • (1995) J Biol Chem , vol.270 , pp. 4741-4747
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 33
    • 0029941071 scopus 로고    scopus 로고
    • The glut 1 glucose transporter interacts with calnexin and calreticulin
    • Oliver JD, Hresko RC, Mueckler M, High S. 1996. The glut 1 glucose transporter interacts with calnexin and calreticulin. J Biol Chem 271:13691-13696.
    • (1996) J Biol Chem , vol.271 , pp. 13691-13696
    • Oliver, J.D.1    Hresko, R.C.2    Mueckler, M.3    High, S.4
  • 34
    • 0026072875 scopus 로고
    • Regulation of expression and intracellular distribution of calreticulin, a major calcium binding protein of nonmuscle cells
    • Opas M, Dziak E, Fliegel L, Michalak M. 1991. Regulation of expression and intracellular distribution of calreticulin, a major calcium binding protein of nonmuscle cells. J Cell Physiol 149:160-171.
    • (1991) J Cell Physiol , vol.149 , pp. 160-171
    • Opas, M.1    Dziak, E.2    Fliegel, L.3    Michalak, M.4
  • 35
    • 0015955240 scopus 로고
    • Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum
    • Ostwald TJ, MacLennan DH. 1974. Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. J Biol Chem 249:974-979.
    • (1974) J Biol Chem , vol.249 , pp. 974-979
    • Ostwald, T.J.1    Maclennan, D.H.2
  • 36
    • 0016172851 scopus 로고
    • Effects of cation binding on the conformation of calsequestrin and the high affinity calcium-binding protein of sarcoplasmic reticulum
    • Ostwald TJ, MacLennan DH, Dorrington KJ. 1974. Effects of cation binding on the conformation of calsequestrin and the high affinity calcium-binding protein of sarcoplasmic reticulum. J Biol Chem 249:5867-5871.
    • (1974) J Biol Chem , vol.249 , pp. 5867-5871
    • Ostwald, T.J.1    Maclennan, D.H.2    Dorrington, K.J.3
  • 37
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • Otteken A, Moss B. 1996. Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J Biol Chem 271:97-103.
    • (1996) J Biol Chem , vol.271 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 38
    • 0030333537 scopus 로고    scopus 로고
    • Extracellular matrix in early cortical development
    • Mize RR, Erzurumlu RS, editors. Amsterdam: Elsevier Science
    • Pearlman AL, Sheppard AM. 1996. Extracellular matrix in early cortical development. In: Mize RR, Erzurumlu RS, editors. Progress in brain research, Vol. 108. Amsterdam: Elsevier Science, p. 119-134.
    • (1996) Progress in Brain Research , vol.108 , pp. 119-134
    • Pearlman, A.L.1    Sheppard, A.M.2
  • 39
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson JR, Ora A, Van PN, Helenius A. 1995. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol Biol Cell 6:1173-1184.
    • (1995) Mol Biol Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 40
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart CM. 1997. Targeting of substrates to the 26S proteasome. FASEB J 11:1055-1066.
    • (1997) FASEB J , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 41
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan S, Xu Y, Brenner MB. 1994. Retention of unassembled components of integral membrane proteins by calnexin. Science 263:387-390.
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 42
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 43
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin a subunit
    • Rojian MV, Finlay BB, Gray V, Dedhar S. 1991. In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin a subunit. Biochemistry 30: 9859-9866.
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojian, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 44
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: Reverse protein flow of no return
    • Sommer T, Wolf DH. 1997. Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J 11:1227-1233.
    • (1997) FASEB J , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 45
    • 0026637858 scopus 로고
    • Widespread tissue distribution of rabbit calreticulin, a non-muscle functional analogue of calsequestrin
    • Tharin S, Dziak E, Michalak M, Opas M. 1992. Widespread tissue distribution of rabbit calreticulin, a non-muscle functional analogue of calsequestrin. Cell Tissue Res 269:29-37.
    • (1992) Cell Tissue Res , vol.269 , pp. 29-37
    • Tharin, S.1    Dziak, E.2    Michalak, M.3    Opas, M.4
  • 46
    • 0021990166 scopus 로고
    • Inhibition by lysosomotropic amines of dog thyroid secretion in vivo
    • Unger J, Ketelbant P, Dumont JE. 1985. Inhibition by lysosomotropic amines of dog thyroid secretion in vivo. Endocrinology 116:958-965.
    • (1985) Endocrinology , vol.116 , pp. 958-965
    • Unger, J.1    Ketelbant, P.2    Dumont, J.E.3
  • 47
    • 0029134004 scopus 로고
    • Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
    • Wada I, Imai S, Kai M, Sakanea F, Kanoh H. 1995. Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms. J Biol Chem 270:20298-20304.
    • (1995) J Biol Chem , vol.270 , pp. 20298-20304
    • Wada, I.1    Imai, S.2    Kai, M.3    Sakanea, F.4    Kanoh, H.5
  • 48
    • 0031055601 scopus 로고    scopus 로고
    • Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of ER-resident molecular chaperones
    • Weist DL, Bhandoola A, Punt J, Kreibich G, McKean D, Singer A. 1997. Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones. Proc Natl Acad Sci USA 94:1884-1889.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1884-1889
    • Weist, D.L.1    Bhandoola, A.2    Punt, J.3    Kreibich, G.4    McKean, D.5    Singer, A.6
  • 49
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White TK, Zhu Q, Tanzer ML. 1995. Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading. J Biol Chem 270:15926-15929.
    • (1995) J Biol Chem , vol.270 , pp. 15926-15929
    • White, T.K.1    Zhu, Q.2    Tanzer, M.L.3


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