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Volumn 270, Issue 4 14-4, 1996, Pages

Involvement of annexin II in exocytosis of lamellar bodies from alveolar epithelial type II cells

Author keywords

permeabilized type II cells; phosphatidylcholine secretion

Indexed keywords

ANNEXIN; LIPOSOME; LUNG SURFACTANT; PHOSPHATIDYLCHOLINE;

EID: 0029960934     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1996.270.4.l668     Document Type: Article
Times cited : (71)

References (34)
  • 1
    • 0024390672 scopus 로고
    • A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells
    • Ali, S. M., M. J. Geisow, and R. D. Burgoyne. A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells. Nature Lond. 340: 313-315, 1989.
    • (1989) Nature Lond. , vol.340 , pp. 313-315
    • Ali, S.M.1    Geisow, M.J.2    Burgoyne, R.D.3
  • 2
    • 0020136308 scopus 로고
    • A simple method for the accurate determination of free [Ca] in Ca-EGTA solutions
    • Cell Physiol. 11
    • Bers, D. M. A simple method for the accurate determination of free [Ca] in Ca-EGTA solutions. Am. J Physiol. 242 (Cell Physiol. 11): C404-C408, 1982.
    • (1982) Am. J Physiol. , vol.242
    • Bers, D.M.1
  • 3
    • 0025195030 scopus 로고
    • 2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexing
    • 2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexing. Biochem. J. 266: 195-200, 1990.
    • (1990) Biochem. J. , vol.266 , pp. 195-200
    • Blackwood, R.A.1    Ernst, J.D.2
  • 4
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37: 911-917, 1959.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing the principle of protein dye binding
    • Bradford, M. M. A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing the principle of protein dye binding. Anal. Biochem. 72: 248-254, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0020504618 scopus 로고
    • Isolation of lamellar bodies from rat granular pneumocytes in primary culture
    • Chander, A., C. Dodia, J. Gil, and A. B. Fisher. Isolation of lamellar bodies from rat granular pneumocytes in primary culture. Biochim. Biophys. Acta 753: 119-129, 1983.
    • (1983) Biochim. Biophys. Acta , vol.753 , pp. 119-129
    • Chander, A.1    Dodia, C.2    Gil, J.3    Fisher, A.B.4
  • 7
    • 0025328270 scopus 로고
    • Regulation of lung surfactant secretion
    • Lung Cell. Mol. Physiol. 2
    • Chander, A., and A. B. Fisher. Regulation of lung surfactant secretion. Am. J. Physiol. 258 (Lung Cell. Mol. Physiol. 2): L241-L253, 1990.
    • (1990) Am. J. Physiol. , vol.258
    • Chander, A.1    Fisher, A.B.2
  • 9
    • 0026055780 scopus 로고
    • In vitro fusion of lung lamellar bodies and plasma membranes is augmented by lung synexin
    • Chander, A., and R. D. Wu. In vitro fusion of lung lamellar bodies and plasma membranes is augmented by lung synexin. Biochim. Biophys. Acta 1086: 157-166, 1992.
    • (1992) Biochim. Biophys. Acta , vol.1086 , pp. 157-166
    • Chander, A.1    Wu, R.D.2
  • 10
    • 0026744180 scopus 로고
    • Identification of calcium-dependent phospholipid-binding proteins (annexins) from guinea pig alveolar type II cells
    • Das, S. K., P. Chakrabarti, F. H. C. Tsao, T. Nayyar, and S. Mukherjee. Identification of calcium-dependent phospholipid-binding proteins (annexins) from guinea pig alveolar type II cells. Mol. Cell. Biochem. 115: 79-84, 1992.
    • (1992) Mol. Cell. Biochem. , vol.115 , pp. 79-84
    • Das, S.K.1    Chakrabarti, P.2    Tsao, F.H.C.3    Nayyar, T.4    Mukherjee, S.5
  • 11
    • 0022527271 scopus 로고
    • An improved method of isolating type II pneumocytes in high yield and purity
    • Dobbs, L. G., R. Gonzalez, and M. C. Williams. An improved method of isolating type II pneumocytes in high yield and purity. Am Rev. Respir. Dis. 134: 141-145, 1986.
    • (1986) Am Rev. Respir. Dis. , vol.134 , pp. 141-145
    • Dobbs, L.G.1    Gonzalez, R.2    Williams, M.C.3
  • 12
    • 0023818448 scopus 로고
    • Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
    • Drust, D. S., and C. E. Creutz. Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature Lond. 331: 88-91, 1988.
    • (1988) Nature Lond. , vol.331 , pp. 88-91
    • Drust, D.S.1    Creutz, C.E.2
  • 13
    • 0021923858 scopus 로고
    • Nile red: A selective fluorescent stain for intracellular lipid droplets
    • Greenspan, P., E. P. Mayer, and S. D. Fowler. Nile red: a selective fluorescent stain for intracellular lipid droplets. J. Cell Biol. 100: 965-973, 1985.
    • (1985) J. Cell Biol. , vol.100 , pp. 965-973
    • Greenspan, P.1    Mayer, E.P.2    Fowler, S.D.3
  • 14
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure, characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • Hope, M. J., M. B. Bally, G. Webb, and P. R. Cullis. Production of large unilamellar vesicles by a rapid extrusion procedure, characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochim. Biophys. Acta 812: 55-65, 1985.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 15
    • 0027052218 scopus 로고
    • Phosphorylation of annexin II tetramer by PKC inhibits aggregation of lipid vesicles by the protein
    • Johnstone, S. A., I.Hubaishy, and D. M. Waisman. Phosphorylation of annexin II tetramer by PKC inhibits aggregation of lipid vesicles by the protein. J Biol. Chem. 267: 25976-25981, 1992
    • (1992) J Biol. Chem. , vol.267 , pp. 25976-25981
    • Johnstone, S.A.1    Hubaishy, I.2    Waisman, D.M.3
  • 16
    • 0028124991 scopus 로고
    • Salt dependency of chromaffin granule aggregation by annexin II tetramer
    • Jones, P. G., S. Fitzpatrick, and D. M. Waisman. Salt dependency of chromaffin granule aggregation by annexin II tetramer. Biochemistry 33: 13751-13760, 1994.
    • (1994) Biochemistry , vol.33 , pp. 13751-13760
    • Jones, P.G.1    Fitzpatrick, S.2    Waisman, D.M.3
  • 19
    • 0000883949 scopus 로고
    • Influence of thyroid hormones on L-α-glycerophosphate dehydrogenase and other dehyrogenases in various organs of rat
    • Lee, Y. P., and H. A. Lardy. Influence of thyroid hormones on L-α-glycerophosphate dehydrogenase and other dehyrogenases in various organs of rat. J. Biol. Chem. 240: 1427-1436, 1965.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1427-1436
    • Lee, Y.P.1    Lardy, H.A.2
  • 20
    • 0029556511 scopus 로고
    • Regulation of annexin I by proteolysis in rat epithelial type II cells
    • Liu, L., A. B. Fisher, and U.-J. P. Zimmerman. Regulation of annexin I by proteolysis in rat epithelial type II cells. Biochem. Mol. Biol. Int. 36: 373-381, 1995.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 373-381
    • Liu, L.1    Fisher, A.B.2    Zimmerman, U.-J.P.3
  • 21
    • 15844409252 scopus 로고
    • Annexin II enhances calcium-dependent secretion of lung surfactant from the permeabilized type II cells
    • Liu, L., M. Wang, A. B. Fisher, and U.-J. P. Zimmerman. Annexin II enhances calcium-dependent secretion of lung surfactant from the permeabilized type II cells. Am. J. Respir. Crit. Care Med. 151: A313, 1995.
    • (1995) Am. J. Respir. Crit. Care Med. , vol.151
    • Liu, L.1    Wang, M.2    Fisher, A.B.3    Zimmerman, U.-J.P.4
  • 22
    • 0029551202 scopus 로고
    • An intramolecular disulfide bond is essential for annexin I-mediated liposome aggregation
    • Liu, L., and U.-J. P. Zimmerman. An intramolecular disulfide bond is essential for annexin I-mediated liposome aggregation. Biochem. Mol. Biol. Int. 35: 345-350, 1995.
    • (1995) Biochem. Mol. Biol. Int. , vol.35 , pp. 345-350
    • Liu, L.1    Zimmerman, U.-J.P.2
  • 23
    • 0025117429 scopus 로고
    • Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry
    • Nakata, T., K. Sobue, and N. Hirokawa. Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry. J. Cell Biol. 111: 13-25, 1990.
    • (1990) J. Cell Biol. , vol.111 , pp. 13-25
    • Nakata, T.1    Sobue, K.2    Hirokawa, N.3
  • 24
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021, 1975.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 25
    • 0025784431 scopus 로고
    • Annexin-mediated membrane fusion of human neutrophil plasma membranes and phospholipid vesicles
    • Oshry, L., P. Meers, T. Mealy, and A. I. Tauber. Annexin-mediated membrane fusion of human neutrophil plasma membranes and phospholipid vesicles. Biochim. Biophys. Acta 1066: 239-244, 1991.
    • (1991) Biochim. Biophys. Acta , vol.1066 , pp. 239-244
    • Oshry, L.1    Meers, P.2    Mealy, T.3    Tauber, A.I.4
  • 26
    • 0028302648 scopus 로고
    • Activation of G proteins may inhibit or stimulate surfactant secretion in rat alveolar type II cells
    • Lung Cell. Mol. Physiol. 10
    • Pian, M. S., and L. G. Dobbs. Activation of G proteins may inhibit or stimulate surfactant secretion in rat alveolar type II cells. Am. J. Physiol. 266 (Lung Cell. Mol. Physiol. 10): L375-L381, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Pian, M.S.1    Dobbs, L.G.2
  • 27
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal, P., and H. B. Pollard. Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta 1197: 63-93, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 28
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J. E., and L. Orci. Molecular dissection of the secretory pathway. Nature Lond. 355: 409-415, 1992.
    • (1992) Nature Lond. , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 29
    • 0026063254 scopus 로고
    • The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C
    • Sarafian, T., L. A. Pradel, J. P. Herry, D. Aunis, and M. F. Bader. The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C. J. Cell Biol. 114: 1135-1147, 1991.
    • (1991) J. Cell Biol. , vol.114 , pp. 1135-1147
    • Sarafian, T.1    Pradel, L.A.2    Herry, J.P.3    Aunis, D.4    Bader, M.F.5
  • 30
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., D. Hoekstra, and R. E. Pagano. Use of resonance energy transfer to monitor membrane fusion. Biochemistry 20: 4093-4099, 1981.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 31
    • 0025366990 scopus 로고
    • Purification and characterization of two rabbit lung calcium-dependent phospholipid-binding proteins
    • Tsao, F. H. C. Purification and characterization of two rabbit lung calcium-dependent phospholipid-binding proteins. Biochim. Biophys. Acta 1045: 29-39, 1990.
    • (1990) Biochim. Biophys. Acta , vol.1045 , pp. 29-39
    • Tsao, F.H.C.1
  • 32
    • 0028282606 scopus 로고
    • Immunocharacterization and developmental regulation of rabbit lung calcium-dependent phospholipid-binding proteins
    • Tsao, F. H. C., X. R. Chen, X. M. Chen, and V. X. Vu. Immunocharacterization and developmental regulation of rabbit lung calcium-dependent phospholipid-binding proteins. Biochim. Biophys. Acta 1213: 91-99, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1213 , pp. 91-99
    • Tsao, F.H.C.1    Chen, X.R.2    Chen, X.M.3    Vu, V.X.4
  • 33
    • 0026808777 scopus 로고
    • Regulation of the chromaffin granule aggregating activity of annexin I by phosphorylation
    • Wang, W., and C. E. Creutz. Regulation of the chromaffin granule aggregating activity of annexin I by phosphorylation. Biochemistry 31: 9934-9939, 1992.
    • (1992) Biochemistry , vol.31 , pp. 9934-9939
    • Wang, W.1    Creutz, C.E.2
  • 34
    • 0023600206 scopus 로고
    • The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: Studies using monoclonal antibodies to calpactin subunits
    • Zokas, L., and J. R. Glenney, Jr. The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunits. J. Cell Biol. 105: 2111-2121, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 2111-2121
    • Zokas, L.1    Glenney Jr., J.R.2


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