메뉴 건너뛰기




Volumn 38, Issue 1, 2005, Pages 43-52

Anti-calreticulin antibody binds to a membrane protein in caveolae

Author keywords

Calcium; Calreticulin; Caveolae; Fibroblast; Immunocytochemistry

Indexed keywords

CALCIUM BINDING PROTEIN; CALRETICULIN; COMPLEMENTARY DNA; HEMAGGLUTININ; MEMBRANE PROTEIN; POLYCLONAL ANTIBODY;

EID: 17644411022     PISSN: 00445991     EISSN: None     Source Type: Journal    
DOI: 10.1267/ahc.38.43     Document Type: Article
Times cited : (3)

References (54)
  • 1
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson, R. G. W. (1998) The caveolae membrane system. Annu. Rev. Biochem. 67; 199-225.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 2
    • 0033546416 scopus 로고    scopus 로고
    • Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules
    • Arosa, F. A., de Jesus, O., Porto, G., Carmo, A. M. and de Sousa, M. (1999) Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules. J. Biol. Chem. 274; 16917-16922.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16917-16922
    • Arosa, F.A.1    De Jesus, O.2    Porto, G.3    Carmo, A.M.4    De Sousa, M.5
  • 3
    • 0026750513 scopus 로고
    • Calcium requirements for secretion in bovine chromaffin cells
    • Augustine, G. J. and Neher, E. (1992) Calcium requirements for secretion in bovine chromaffin cells. J. Physiol. 450; 247-271.
    • (1992) J. Physiol. , vol.450 , pp. 247-271
    • Augustine, G.J.1    Neher, E.2
  • 4
    • 0029128663 scopus 로고
    • Overexpression of calreticulin increases the Ca2+ capacity of rapidly exchanging Ca2+ stores and reveals aspects of their lumenal microenvironment and function
    • Bastianutto, C., Clementi, E., Codazzi, F., Podini, P., De Giorgi, F., Rizzuto, R., Meldolesi, J. and Pozzan, T. (1995) Overexpression of calreticulin increases the Ca2+ capacity of rapidly exchanging Ca2+ stores and reveals aspects of their lumenal microenvironment and function. J. Cell Biol. 130; 847-855.
    • (1995) J. Cell Biol. , vol.130 , pp. 847-855
    • Bastianutto, C.1    Clementi, E.2    Codazzi, F.3    Podini, P.4    De Giorgi, F.5    Rizzuto, R.6    Meldolesi, J.7    Pozzan, T.8
  • 5
    • 0023062987 scopus 로고
    • Inositol trisphosphate and diacylglycerol: Two interacting second messengers
    • Berridge, M. J. (1987) Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu. Rev. Biochem. 56; 159-193.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 159-193
    • Berridge, M.J.1
  • 8
    • 0029156597 scopus 로고
    • Calreticulin inhibits repetitive intracellular Ca2+ waves
    • Camacho, P. and Lechleiter, J. D. (1995) Calreticulin inhibits repetitive intracellular Ca2+ waves. Cell 82; 765-771.
    • (1995) Cell , vol.82 , pp. 765-771
    • Camacho, P.1    Lechleiter, J.D.2
  • 9
    • 0034537052 scopus 로고    scopus 로고
    • Caveolae from canine airway smooth muscle contain the necessary components for a role in Ca(2+) handling
    • Darby, P. J., Kwan, C. Y. and Daniel, E. E. (2000) Caveolae from canine airway smooth muscle contain the necessary components for a role in Ca(2+) handling. Am. J. Physiol. Lung Cell Mol. Physiol. 279; L1226-1235.
    • (2000) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.279
    • Darby, P.J.1    Kwan, C.Y.2    Daniel, E.E.3
  • 11
    • 0030910249 scopus 로고    scopus 로고
    • Calreticulin biosynthesis and processing in human myeloid cells: Demonstration of signal peptide cleavage and N-glycosylation
    • Denning, G. M., Leidal, K. G., Holst, V. A., Iyer, S. S., Pearson, D. W., Clark, J. R., Nauseef, W. M. and Clark, R. A. (1997) Calreticulin biosynthesis and processing in human myeloid cells: demonstration of signal peptide cleavage and N-glycosylation. Blood 90; 372-381.
    • (1997) Blood , vol.90 , pp. 372-381
    • Denning, G.M.1    Leidal, K.G.2    Holst, V.A.3    Iyer, S.S.4    Pearson, D.W.5    Clark, J.R.6    Nauseef, W.M.7    Clark, R.A.8
  • 12
    • 0033591411 scopus 로고    scopus 로고
    • Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion
    • Fadel, M. P., Dziak, E., Lo, C. M., Ferrier, J., Mesaeli, N., Michalak, M. and Opas, M. (1999) Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion. J. Biol. Chem. 274; 15085-15094.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15085-15094
    • Fadel, M.P.1    Dziak, E.2    Lo, C.M.3    Ferrier, J.4    Mesaeli, N.5    Michalak, M.6    Opas, M.7
  • 14
    • 0028828220 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes
    • Fujimoto, K. (1995) Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes. J. Cell Sci. 108; 3443-3449.
    • (1995) J. Cell Sci. , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 15
    • 0029969182 scopus 로고    scopus 로고
    • Transmembrane phospholipid distribution revealed by freeze-fracture replica labeling
    • Fujimoto, K., Umeda, M. and Fujimoto, T. (1996) Transmembrane phospholipid distribution revealed by freeze-fracture replica labeling. J. Cell Sci. 109; 2453-2460.
    • (1996) J. Cell Sci. , vol.109 , pp. 2453-2460
    • Fujimoto, K.1    Umeda, M.2    Fujimoto, T.3
  • 16
    • 0027102133 scopus 로고
    • Localization of inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae
    • Fujimoto, T., Nakade, S., Miyawaki, A., Mikoshiba, K. and Ogawa, K. (1992) Localization of inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae. J. Cell Biol. 119; 1507-1513.
    • (1992) J. Cell Biol. , vol.119 , pp. 1507-1513
    • Fujimoto, T.1    Nakade, S.2    Miyawaki, A.3    Mikoshiba, K.4    Ogawa, K.5
  • 17
    • 0027452708 scopus 로고
    • Calcium pump of the plasma membrane is localized in caveolae
    • Fujimoto, T. (1993) Calcium pump of the plasma membrane is localized in caveolae. J. Cell Biol. 120; 1147-1157.
    • (1993) J. Cell Biol. , vol.120 , pp. 1147-1157
    • Fujimoto, T.1
  • 18
    • 0028877917 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae is linked to actin filaments
    • Fujimoto, T., Miyawaki, A. and Mikoshiba, K. (1995) Inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae is linked to actin filaments. J. Cell Sci. 108; 7-15.
    • (1995) J. Cell Sci. , vol.108 , pp. 7-15
    • Fujimoto, T.1    Miyawaki, A.2    Mikoshiba, K.3
  • 19
    • 0029757511 scopus 로고    scopus 로고
    • GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking
    • Fujimoto, T. (1996) GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking. J. Histochem. Cytochem. 44; 929-941.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 929-941
    • Fujimoto, T.1
  • 20
    • 0030962443 scopus 로고    scopus 로고
    • Metal sandwich method to quick-freeze monolayer cultured cells for freeze-fracture
    • Fujimoto, T. and Fujimoto, K. (1997) Metal sandwich method to quick-freeze monolayer cultured cells for freeze-fracture. J. Histochem. Cytochem. 45; 595-598.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 595-598
    • Fujimoto, T.1    Fujimoto, K.2
  • 21
    • 4944254847 scopus 로고    scopus 로고
    • Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum
    • Gelebart, P., Opas, M. and Michalak, M. (2005) Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum. Int. J. Biochem. Cell Biol. 37; 260-266.
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 260-266
    • Gelebart, P.1    Opas, M.2    Michalak, M.3
  • 22
    • 0038756766 scopus 로고    scopus 로고
    • Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule
    • Ghiran, I., Klickstein, L. B. and Nicholson-Weller, A. (2003) Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule. J. Biol. Chem. 278; 21024-21031.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21024-21031
    • Ghiran, I.1    Klickstein, L.B.2    Nicholson-Weller, A.3
  • 24
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and Calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert, D. N., Foellmer, B. and 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
  • 25
    • 0024375480 scopus 로고
    • Mechanism of the calcium pump in the endoplasmic reticulum of liver: Phosphoproteins as reaction intermediates
    • Heilmann, C., Spamer, C. and Gerok, W. (1989) Mechanism of the calcium pump in the endoplasmic reticulum of liver: phosphoproteins as reaction intermediates. Cell Calcium 10; 275-287.
    • (1989) Cell Calcium , vol.10 , pp. 275-287
    • Heilmann, C.1    Spamer, C.2    Gerok, W.3
  • 26
    • 0032574603 scopus 로고    scopus 로고
    • Endothelial Ca2+ waves preferentially originate at specific loci in caveolin-rich cell edges. Proc
    • Isshiki, M., Ando, J., Korenaga, R., Kogo, H., Fujimoto, T., Fujita, T. and Kamiya, A. (1998) Endothelial Ca2+ waves preferentially originate at specific loci in caveolin-rich cell edges. Proc. Natl. Acad. Sci. USA 95; 5009-5014.
    • (1998) Natl. Acad. Sci. USA , vol.95 , pp. 5009-5014
    • Isshiki, M.1    Ando, J.2    Korenaga, R.3    Kogo, H.4    Fujimoto, T.5    Fujita, T.6    Kamiya, A.7
  • 27
    • 0036473056 scopus 로고    scopus 로고
    • Sites of Ca(2+) wave initiation move with caveolae to the trailing edge of migrating cells
    • Isshiki, M., Ando, J., Yamamoto, K., Fujita, T., Ying, Y. and Anderson, R. G. W. (2002) Sites of Ca(2+) wave initiation move with caveolae to the trailing edge of migrating cells. J. Cell Sci. 115; 475-484.
    • (2002) J. Cell Sci. , vol.115 , pp. 475-484
    • Isshiki, M.1    Ando, J.2    Yamamoto, K.3    Fujita, T.4    Ying, Y.5    Anderson, R.G.W.6
  • 28
    • 0037044751 scopus 로고    scopus 로고
    • A molecular sensor detects signal transduction from caveolae in living cells
    • Isshiki, M., Ying, Y. S., Fujita, T. and Anderson, R. G. W. (2002) A molecular sensor detects signal transduction from caveolae in living cells. J. Biol. Chem. 277; 43389-43398.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43389-43398
    • Isshiki, M.1    Ying, Y.S.2    Fujita, T.3    Anderson, R.G.W.4
  • 29
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of Calreticulin: From the ER lumen to the extracellular space
    • Johnson, S., Michalak, M., Opas, M. and Eggleton, P. (2001) The ins and outs of Calreticulin: from the ER lumen to the extracellular space. Trends Cell Biol. 11; 122-129.
    • (2001) Trends Cell Biol. , vol.11 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 30
    • 0028323266 scopus 로고
    • Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin alpha-subunit-binding protein
    • Leung-Hagesteijn, C. Y., Milankov, K., Michalak, M., Wilkins, J. and Dedhar, S. (1994) Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin alpha-subunit-binding protein. J. Cell Sci. 107; 589-600.
    • (1994) J. Cell Sci. , vol.107 , pp. 589-600
    • Leung-Hagesteijn, C.Y.1    Milankov, K.2    Michalak, M.3    Wilkins, J.4    Dedhar, S.5
  • 31
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • Liu, P., Rudick, M. and Anderson, R. G. W. (2002) Multiple functions of caveolin-1. J. Biol. Chem. 277; 41295-41298.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41295-41298
    • Liu, P.1    Rudick, M.2    Anderson, R.G.W.3
  • 32
    • 0019350409 scopus 로고
    • Relationship between presynaptic calcium current and postsynaptic potential in squid giant synapse
    • Llinas, R., Steinberg, I. Z. and Walton, K. (1981) Relationship between presynaptic calcium current and postsynaptic potential in squid giant synapse. Biophys. J. 33; 323-351.
    • (1981) Biophys. J. , vol.33 , pp. 323-351
    • Llinas, R.1    Steinberg, I.Z.2    Walton, K.3
  • 33
    • 0034697041 scopus 로고    scopus 로고
    • Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains
    • Lockwich, T. P., Liu, X., Singh, B. B., Jadlowiec, J., Weiland, S. and Ambudkar, I. S. (2000) Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains. J. Biol. Chem. 275; 11934-11942.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11934-11942
    • Lockwich, T.P.1    Liu, X.2    Singh, B.B.3    Jadlowiec, J.4    Weiland, S.5    Ambudkar, I.S.6
  • 34
    • 0020078629 scopus 로고
    • Antibodies to the Golgi complex and the rough endoplasmic reticulum
    • Louvard, D., Reggio, H. and Warren, G. (1982) Antibodies to the Golgi complex and the rough endoplasmic reticulum. J. Cell Biol. 92; 92-107.
    • (1982) J. Cell Biol. , vol.92 , pp. 92-107
    • Louvard, D.1    Reggio, H.2    Warren, G.3
  • 35
    • 0023749218 scopus 로고
    • Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum
    • Macer, D. R. and Koch, G. L. (1988) Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum. J. Cell Sci. 91; 61-70.
    • (1988) J. Cell Sci. , vol.91 , pp. 61-70
    • Macer, D.R.1    Koch, G.L.2
  • 37
    • 0029828912 scopus 로고    scopus 로고
    • Endoplasmic reticulum form of Calreticulin modulates glucocorticoid- sensitive gene expres-sion
    • Michalak, M., Burns, K., Andrin, C., Mesaeli, N., Jass, G. H., Busaan, J. L. and Opas, M. (1996) Endoplasmic reticulum form of Calreticulin modulates glucocorticoid-sensitive gene expres-sion. 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.L.6    Opas, M.7
  • 39
    • 0026690553 scopus 로고
    • Calcium binding proteins in the sarcoplasmic/endoplasmic reticulum of muscle and nonmuscle cells
    • Milner, R. E., Famulski, K. S. and Michalak, M. (1992) Calcium binding proteins in the sarcoplasmic/endoplasmic reticulum of muscle and nonmuscle cells. Mol. Cell. Biochem. 112; 1-13.
    • (1992) Mol. Cell. Biochem. , vol.112 , pp. 1-13
    • Milner, R.E.1    Famulski, K.S.2    Michalak, M.3
  • 40
    • 0037477628 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly
    • Orr, A. W., Pedraza, C. E., Pattern, M. A., Elzie, C. A., Goicoechea, S., Strickland, D. K. and Murphy-Ullrich, J. E. (2003) Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly. J. Cell Biol. 161; 1179-1189.
    • (2003) J. Cell Biol. , vol.161 , pp. 1179-1189
    • Orr, A.W.1    Pedraza, C.E.2    Pattern, M.A.3    Elzie, C.A.4    Goicoechea, S.5    Strickland, D.K.6    Murphy-Ullrich, J.E.7
  • 41
    • 0035965323 scopus 로고    scopus 로고
    • Cell biology. Life without caveolae
    • L Parton, R. G. (2001) Cell biology. Life without caveolae. Science 293; 2404-2405.
    • (2001) Science , vol.293 , pp. 2404-2405
    • Parton, R.G.1
  • 44
    • 0021757077 scopus 로고
    • Cell physiology: Cellular site of calcium regulation
    • Somlyo, A. P. (1984) Cell physiology: cellular site of calcium regulation. Nature 309; 516-517.
    • (1984) Nature , vol.309 , pp. 516-517
    • Somlyo, A.P.1
  • 46
    • 0024405953 scopus 로고
    • Evidence for extracellular localization of activator calcium in dog coronary artery smooth muscle as studied by the pyroantimonate method
    • Suzuki, S. and Sugi, H. (1989) Evidence for extracellular localization of activator calcium in dog coronary artery smooth muscle as studied by the pyroantimonate method. Cell Tissue Res. 257; 237-246.
    • (1989) Cell Tissue Res. , vol.257 , pp. 237-246
    • Suzuki, S.1    Sugi, H.2
  • 48
    • 0021748350 scopus 로고
    • Localization of endoplasmic reticulum in living and glut-araldehyde-fixed cells with fluorescent dyes
    • Terasaki, M., Song, J., Wong, J. R., Weiss, M. J. and Chen, L. B. (1984) Localization of endoplasmic reticulum in living and glut-araldehyde-fixed cells with fluorescent dyes. Cell 38; 101-108.
    • (1984) Cell , vol.38 , pp. 101-108
    • Terasaki, M.1    Song, J.2    Wong, J.R.3    Weiss, M.J.4    Chen, L.B.5
  • 49
    • 0019042936 scopus 로고
    • Immunochemistry on ultrathin frozen sections
    • Tokuyasu, K. T. (1980) Immunochemistry on ultrathin frozen sections. Histochem. J. 12; 381-403.
    • (1980) Histochem. J. , vol.12 , pp. 381-403
    • Tokuyasu, K.T.1
  • 50
    • 0037166343 scopus 로고    scopus 로고
    • Calcium oscillation linked to pacemaking of interstitial cells of Cajal: Requirement of calcium influx and localization of TRP4 in caveolae
    • Torihashi, S., Fujimoto, T., Trost, C. and Nakayama, S. (2002) Calcium oscillation linked to pacemaking of interstitial cells of Cajal: requirement of calcium influx and localization of TRP4 in caveolae. J. Biol. Chem. 277; 19191-19197.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19191-19197
    • Torihashi, S.1    Fujimoto, T.2    Trost, C.3    Nakayama, S.4
  • 51
    • 0035976822 scopus 로고    scopus 로고
    • Identification of mouse trp homologs and lipid rafts from spermatogenic cells and sperm
    • Trevino, C. L., Serrano, C. J., Beltran, C., Felix, R. and Darszon, A. (2001) Identification of mouse trp homologs and lipid rafts from spermatogenic cells and sperm. FEBS Lett. 509; 119-125.
    • (2001) FEBS Lett. , vol.509 , pp. 119-125
    • Trevino, C.L.1    Serrano, C.J.2    Beltran, C.3    Felix, R.4    Darszon, A.5
  • 52
    • 0030561979 scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein
    • Way, M. and Parton, R. G. (1995) M-caveolin, a muscle-specific caveolin-related protein. FEBS Lett. 376; 108-112.
    • (1995) FEBS Lett. , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.G.2
  • 53
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White, T. K., Zhu, Q. and Tanzer, M. L. (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
  • 54
    • 77049234363 scopus 로고
    • The fine structure of the gall bladder epitheli-um of the mouse
    • Yamada, E. (1955) The fine structure of the gall bladder epitheli-um of the mouse. J. Biophys. Biochem. Cytol. 1; 445-458.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 445-458
    • Yamada, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.