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Volumn 73, Issue 3, 1997, Pages 1607-1616

Phosphatidylserine liposomes can be tethered by caldesmon to actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

CALDESMON; CHYMOTRYPSIN A; LIPOSOME; PHOSPHATIDYLSERINE;

EID: 0030804034     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78192-X     Document Type: Article
Times cited : (11)

References (63)
  • 1
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • Aderem, A. 1992. The MARCKS brothers: a family of protein kinase C substrates. Cell. 71:713-716.
    • (1992) Cell , vol.71 , pp. 713-716
    • Aderem, A.1
  • 2
    • 0025961398 scopus 로고
    • Purification and characterization of a brain-specific protein kinase C substrate, neurogranin
    • Baudier, J., J. C. Deloulme, A. Van Dorsselaer, D. Black, and H. W. D. Matthes. 1991. Purification and characterization of a brain-specific protein kinase C substrate, neurogranin. J. Biol. Chem. 266:229-237.
    • (1991) J. Biol. Chem. , vol.266 , pp. 229-237
    • Baudier, J.1    Deloulme, J.C.2    Van Dorsselaer, A.3    Black, D.4    Matthes, H.W.D.5
  • 3
    • 0028927536 scopus 로고
    • Computer-assistant prediction of phospholipid binding sites of caldesmon and calponin
    • Bogatcheva, N. V., and N. B. Gusev. 1995. Computer-assistant prediction of phospholipid binding sites of caldesmon and calponin. FEBS Lett. 363:269-272.
    • (1995) FEBS Lett. , vol.363 , pp. 269-272
    • Bogatcheva, N.V.1    Gusev, N.B.2
  • 5
    • 0021686984 scopus 로고
    • Smooth muscle caldesmon
    • Bretscher, A. 1984. Smooth muscle caldesmon. J. Biol. Chem. 259: 12873-12880.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12873-12880
    • Bretscher, A.1
  • 6
    • 0021914106 scopus 로고
    • Identification and localization of immunoreactive forms of caldesmon in smooth and nonmuscle cells: A comparison with the distributions of tropomyosin and alpha-actinin
    • Bretscher, A., and W. Lynch. 1985. Identification and localization of immunoreactive forms of caldesmon in smooth and nonmuscle cells: a comparison with the distributions of tropomyosin and alpha-actinin. J. Cell Biol. 100:1656-1663.
    • (1985) J. Cell Biol. , vol.100 , pp. 1656-1663
    • Bretscher, A.1    Lynch, W.2
  • 9
    • 0022655813 scopus 로고
    • Identification of a secretory granule-binding protein as caldesmon
    • Burgoyne, R. D., T. R. Cheek, and K.-M. Norman. 1986. Identification of a secretory granule-binding protein as caldesmon. Nature. 319:68-70.
    • (1986) Nature , vol.319 , pp. 68-70
    • Burgoyne, R.D.1    Cheek, T.R.2    Norman, K.-M.3
  • 10
    • 0028113894 scopus 로고
    • Biogenesis: Plasma membrane calcium ATPase: 15 years of work on the purified enzyme
    • Carafoli, E. 1994. Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J. 8:993-1002.
    • (1994) FASEB J. , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 11
    • 0022998463 scopus 로고
    • Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes
    • Cohen, A. M., S.-C. Liu, L. H. Derick, and J. Palek. 1986. Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes. Blood. 68:920-926.
    • (1986) Blood , vol.68 , pp. 920-926
    • Cohen, A.M.1    Liu, S.-C.2    Derick, L.H.3    Palek, J.4
  • 12
    • 0025982039 scopus 로고
    • The role of actin polymerization in cell motility
    • Cooper, J. A. 1991. The role of actin polymerization in cell motility. Annu. Rev. Physiol. 53:585-605.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 585-605
    • Cooper, J.A.1
  • 13
    • 0027263171 scopus 로고
    • Interaction of caldesmon with phospholipids
    • Czurylo, E. A., J. Zborowski, and R. Dabrowska. 1993. Interaction of caldesmon with phospholipids. Biochem. J. 291:403-408.
    • (1993) Biochem. J. , vol.291 , pp. 403-408
    • Czurylo, E.A.1    Zborowski, J.2    Dabrowska, R.3
  • 15
    • 0021925951 scopus 로고
    • The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filaments
    • Dabrowska, R., A. Goch, B. Galazkiewicz, and H. Osinska. 1985. The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filaments. Biochim. Biophys. Acta. 842:70-75.
    • (1985) Biochim. Biophys. Acta. , vol.842 , pp. 70-75
    • Dabrowska, R.1    Goch, A.2    Galazkiewicz, B.3    Osinska, H.4
  • 17
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg, D., E. Schwartz, M. Komaromy, and R. Wall. 1984. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwartz, E.2    Komaromy, M.3    Wall, R.4
  • 18
    • 0024394509 scopus 로고
    • The effect of caldesmon on assembly and dynamic properties of actin
    • Galazkiewicz, B., J. Belagyi, and R. Dabrowska. 1989. The effect of caldesmon on assembly and dynamic properties of actin. Eur. J. Biochem. 181:607-614.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 607-614
    • Galazkiewicz, B.1    Belagyi, J.2    Dabrowska, R.3
  • 21
    • 0027437479 scopus 로고
    • Actin conformation is drastically altered by direct interaction with membrane lipids: A differential scanning calorimetry study
    • Gicquaud, C. 1993. Actin conformation is drastically altered by direct interaction with membrane lipids: a differential scanning calorimetry study. Biochemistry. 32:11873-11877.
    • (1993) Biochemistry , vol.32 , pp. 11873-11877
    • Gicquaud, C.1
  • 22
    • 0023801362 scopus 로고
    • Caldesmon: Molecular weight and subunit composition by analytical ultracentrifugation
    • Graceffa, P., C.-L. A. Wang, and W. F. Stafford. 1988. Caldesmon: molecular weight and subunit composition by analytical ultracentrifugation. J. Biol. Chem. 263:14196-14202.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14196-14202
    • Graceffa, P.1    Wang, C.-L.A.2    Stafford, W.F.3
  • 23
    • 0026513601 scopus 로고
    • MARCKS is an actin filament crosslinking protein regulated by protein kinase C, and calcium-calmodulin
    • Hartwig, J. H., M. Thelen, A. Rosen, P. A. Janmey, A. C. Nairn, and A. Aderem. 1992. MARCKS is an actin filament crosslinking protein regulated by protein kinase C, and calcium-calmodulin. Nature. 356: 618-622.
    • (1992) Nature , vol.356 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 24
    • 0025900411 scopus 로고
    • The interactions of the brain-specific calmodulin-binding protein kinase C substrate, neuromodulin (GAP 43), with membrane phospholipids
    • Houbre, D., G. Duporthail, J. C. Deloulme, and J. Baudier. 1991. The interactions of the brain-specific calmodulin-binding protein kinase C substrate, neuromodulin (GAP 43), with membrane phospholipids. J. Biol. Chem. 266:7121-7131.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7121-7131
    • Houbre, D.1    Duporthail, G.2    Deloulme, J.C.3    Baudier, J.4
  • 25
    • 0016294918 scopus 로고
    • The measurement of actin concentration in solution: A comparison of methods
    • Houk, T., and K. Ue. 1974. The measurement of actin concentration in solution: a comparison of methods. Anal. Biochem. 62:66-74.
    • (1974) Anal. Biochem. , vol.62 , pp. 66-74
    • Houk, T.1    Ue, K.2
  • 26
    • 0025728518 scopus 로고
    • Actin binding proteins-lipid interactions
    • Isenberg, G. 1991. Actin binding proteins-lipid interactions. J. Muscle Res. Cell Motil. 12:136-144.
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 136-144
    • Isenberg, G.1
  • 28
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin - Potentiation of protective ability of tropomyosin by 83-kDa nonmuscle caldesmon
    • Ishikawa, R., S. Yamashiro, and F. Matsumura. 1989b. Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin - potentiation of protective ability of tropomyosin by 83-kDa nonmuscle caldesmon. J. Biol. Chem. 264: 7490-7497.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 29
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey, P. A. 1994. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56:169-191.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Janmey, P.A.1
  • 30
    • 0028361026 scopus 로고
    • Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin
    • Kim, J., P. J. Blackshear, J. D. Johnson, and S. McLaughlin. 1994. Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin. Biophys. J. 67:227-237.
    • (1994) Biophys. J. , vol.67 , pp. 227-237
    • Kim, J.1    Blackshear, P.J.2    Johnson, J.D.3    McLaughlin, S.4
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 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
  • 33
    • 0007114441 scopus 로고
    • Overcoming barrier to exocytosis
    • Linstedt, A. D., and R. B. Kelly. 1987. Overcoming barrier to exocytosis. Trends Neurosci. 10:446-448.
    • (1987) Trends Neurosci. , vol.10 , pp. 446-448
    • Linstedt, A.D.1    Kelly, R.B.2
  • 35
    • 0025990355 scopus 로고
    • Heavy-meromyosin-decorated actin filaments: A simple method to preserve actin filaments for rotary shadowing
    • Mabuchi, K. 1991. Heavy-meromyosin-decorated actin filaments: a simple method to preserve actin filaments for rotary shadowing. J. Struct. Biol. 107:22-28.
    • (1991) J. Struct. Biol. , vol.107 , pp. 22-28
    • Mabuchi, K.1
  • 36
    • 0027478542 scopus 로고
    • Electron microscopic images suggest both ends of caldesmon interact with actin filaments
    • Mabuchi, K., J. J.-C. Lin, and C.-L. A. Wang. 1993. Electron microscopic images suggest both ends of caldesmon interact with actin filaments. J. Muscle Res. Cell Motil. 14:54-64.
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 54-64
    • Mabuchi, K.1    Lin, J.J.-C.2    Wang, C.-L.A.3
  • 37
    • 0025881953 scopus 로고
    • Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin
    • Mabuchi, K., and C.-L. A. Wang. 1991. Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin. J. Muscle Res. Cell Motil. 12:145-151.
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 145-151
    • Mabuchi, K.1    Wang, C.-L.A.2
  • 40
    • 0025799684 scopus 로고
    • The molecular anatomy of caldesmon
    • Marston, S. B., and C. S. Redwood. 1991. The molecular anatomy of caldesmon. Biochem. J. 279:1-16.
    • (1991) Biochem. J. , vol.279 , pp. 1-16
    • Marston, S.B.1    Redwood, C.S.2
  • 42
    • 0028270914 scopus 로고
    • Precise identification of the regulatory F-actin- and calmodulin-binding sequences in the 10-kDa carboxyl-terminal domain of caldesmon
    • Mezgueldi, M., J. Derancourt, B. Calas, R. Kassab, and A. Fattoum. 1994. Precise identification of the regulatory F-actin-and calmodulin-binding sequences in the 10-kDa carboxyl-terminal domain of caldesmon. J. Biol. Chem. 269:12824-12832.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12824-12832
    • Mezgueldi, M.1    Derancourt, J.2    Calas, B.3    Kassab, R.4    Fattoum, A.5
  • 43
    • 0023182782 scopus 로고
    • Redistribution of caldesmon and tropomyosin associated with concanavalin A receptor capping on splenic T-lymphocytes
    • Mizushima, Y., K. Kanda, T. Hamaoka, H. Fujiwara, and K. Sobue. 1987. Redistribution of caldesmon and tropomyosin associated with concanavalin A receptor capping on splenic T-lymphocytes. Biomed. Res. 8:73-78.
    • (1987) Biomed. Res. , vol.8 , pp. 73-78
    • Mizushima, Y.1    Kanda, K.2    Hamaoka, T.3    Fujiwara, H.4    Sobue, K.5
  • 44
    • 85030291935 scopus 로고
    • Colortation des lipoprotéines après electrophorèse en gel de polyacrylamide
    • Prat, J. P., J. N. Lamy, and J. D. Weill. 1969. Colortation des lipoprotéines après electrophorèse en gel de polyacrylamide. Bull. Soc. Chim. Biol. 51:136739.
    • (1969) Bull. Soc. Chim. Biol. , vol.51 , pp. 136739
    • Prat, J.P.1    Lamy, J.N.2    Weill, J.D.3
  • 45
    • 0014779155 scopus 로고
    • Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser, G., S. Fleischer, and A. Yamamoto. 1970. Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids. 5:494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleischer, S.2    Yamamoto, A.3
  • 46
    • 0025900837 scopus 로고
    • Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems
    • Sobue, K., and J. R. Sellers. 1991. Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems. J. Biol. Chem. 266:12115-12118.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12115-12118
    • Sobue, K.1    Sellers, J.R.2
  • 47
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction: Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction: biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 48
    • 0024385603 scopus 로고
    • Evidence of direct interaction between actin and membrane lipids
    • St-Onge, D., and C. Gicquaud. 1989. Evidence of direct interaction between actin and membrane lipids. Biochem. Cell Biol. 67:297-300.
    • (1989) Biochem. Cell Biol. , vol.67 , pp. 297-300
    • St-Onge, D.1    Gicquaud, C.2
  • 49
    • 0028881723 scopus 로고
    • Over-expression of smooth muscle caldesmon in mouse fibroblasts
    • Surgucheva, I., and J. Bryan. 1995. Over-expression of smooth muscle caldesmon in mouse fibroblasts. Cell Motil. Cytoskeleton. 32:233-243.
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 233-243
    • Surgucheva, I.1    Bryan, J.2
  • 50
    • 0026673876 scopus 로고
    • 2+-stimulated binding of myosin I to phosphatidylserine concerted with calmodulin dissociation
    • 2+-stimulated binding of myosin I to phosphatidylserine concerted with calmodulin dissociation. J. Biol. Chem. 267:3445-3454.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3445-3454
    • Swanljung-Collins, H.1    Collins, J.H.2
  • 51
    • 0018881828 scopus 로고
    • Comparative properties and methods of preparations of lipid vesicles (liposomes)
    • Szoka, F., and D. Papahadjoboulos. 1980. Comparative properties and methods of preparations of lipid vesicles (liposomes). Annu. Rev. Biophys. Bioeng. 9:467-4.
    • (1980) Annu. Rev. Biophys. Bioeng. , vol.9 , pp. 467-474
    • Szoka, F.1    Papahadjoboulos, D.2
  • 52
    • 0022454873 scopus 로고
    • Functional domain of caldesmon
    • Szpacenko, A., and R. Dabrowska. 1986. Functional domain of caldesmon. FEBS Lett. 202:182-186.
    • (1986) FEBS Lett. , vol.202 , pp. 182-186
    • Szpacenko, A.1    Dabrowska, R.2
  • 54
    • 0025696188 scopus 로고
    • Interaction of smooth muscle caldesmon with phospholipids
    • Vorotnikov, A. V., and N. B. Gusev. 1990. Interaction of smooth muscle caldesmon with phospholipids. FEBS Lett. 277:134-136.
    • (1990) FEBS Lett. , vol.277 , pp. 134-136
    • Vorotnikov, A.V.1    Gusev, N.B.2
  • 56
    • 0024587183 scopus 로고
    • The role of caldesmon in the regulation of receptor capping in mouse T-lymphoma cell
    • Walker, G., W. G. L. Kerrick, and L. Y. W. Bourguignon. 1989. The role of caldesmon in the regulation of receptor capping in mouse T-lymphoma cell. J. Biol. Chem. 264:496-500.
    • (1989) J. Biol. Chem. , vol.264 , pp. 496-500
    • Walker, G.1    Kerrick, W.G.L.2    Bourguignon, L.Y.W.3
  • 57
    • 0026289054 scopus 로고
    • Calcium-dependent mechanisms of smooth muscle contraction
    • Walsh, M. P. 1990. Calcium-dependent mechanisms of smooth muscle contraction. Biochem. Cell Biol. 69:771-800.
    • (1990) Biochem. Cell Biol. , vol.69 , pp. 771-800
    • Walsh, M.P.1
  • 59
    • 0028268574 scopus 로고
    • 2+/calmodulin-, and tropomyosin-binding domains stabilizes endogenous tropomyosin and microfilaments
    • 2+/calmodulin-, and tropomyosin-binding domains stabilizes endogenous tropomyosin and microfilaments. J. Cell Biol. 125: 359-368.
    • (1994) J. Cell Biol. , vol.125 , pp. 359-368
    • Warren, K.S.1    Lin, J.L.-J.2    Wamboldt, D.D.3    Lin, J.J.-C.4
  • 60
    • 0026078926 scopus 로고
    • Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis
    • Yamashiro, S., Y. Yamakita, H. Hosoya, and F. Matsumura. 1991. Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis. Nature. 349:169-172.
    • (1991) Nature , vol.349 , pp. 169-172
    • Yamashiro, S.1    Yamakita, Y.2    Hosoya, H.3    Matsumura, F.4
  • 61
    • 0025272184 scopus 로고
    • Mitosis-specific phosphorylation causes 83k non-muscle caldesmon to dissociate from microfilaments
    • Yamashiro, S., Y. Yamakita, R. Ishikawa, and F. Matsumura. 1990. Mitosis-specific phosphorylation causes 83k non-muscle caldesmon to dissociate from microfilaments. Nature. 344:675-678.
    • (1990) Nature , vol.344 , pp. 675-678
    • Yamashiro, S.1    Yamakita, Y.2    Ishikawa, R.3    Matsumura, F.4
  • 62
    • 0025837139 scopus 로고
    • A calmodulin-binding peptide of caldesmon
    • Zhan, Q., S. S. Wong, and C.-L. A. Wang. 1991. A calmodulin-binding peptide of caldesmon. J. Biol. Chem. 266:21810-21814.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21810-21814
    • Zhan, Q.1    Wong, S.S.2    Wang, C.-L.A.3
  • 63
    • 0029112618 scopus 로고
    • Identification of the functionally relevant calmodulin binding site in smooth muscle caldesmon
    • Zhuang, S., E. Wang, and C.-L. A. Wang. 1995. Identification of the functionally relevant calmodulin binding site in smooth muscle caldesmon. J. Biol. Chem. 270:19964-19968.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19964-19968
    • Zhuang, S.1    Wang, E.2    Wang, C.-L.A.3


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