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Volumn 48, Issue 4, 1999, Pages 453-458

Proteolysis of synaptobrevin, syntaxin, and snap-25 in alveolar epithelial type II cells

Author keywords

Calpain; Proteolysis; SNAP 25; Synaptobrevin; Syntaxin

Indexed keywords

CALCIUM IONOPHORE; CALPAIN; PHORBOL 12 ACETATE 13 MYRISTATE; SYNAPTOBREVIN; SYNTAXIN;

EID: 0032702266     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/713803537     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 0030992881 scopus 로고    scopus 로고
    • The roles of NSF. SNAPs and SNAREs during membrane fusion
    • Woodman, P. G. (1997) The roles of NSF. SNAPs and SNAREs during membrane fusion. Biochim. Biophys. Acta 1357, 155-172.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 155-172
    • Woodman, P.G.1
  • 3
    • 0028870106 scopus 로고
    • A role for soluble NSF attachment proteins (SNAPs) in regulated exocytosis in adrenal chromaffin cells
    • Morgan, A., and Burgoyne, R. D. (1995) A role for soluble NSF attachment proteins (SNAPs) in regulated exocytosis in adrenal chromaffin cells. EMBO J. 14, 232-239.
    • (1995) EMBO J. , vol.14 , pp. 232-239
    • Morgan, A.1    Burgoyne, R.D.2
  • 4
    • 0029835084 scopus 로고    scopus 로고
    • Patch-clamp capacitance analysis of the effects of α-SNAP on exocytosis in adrenal chromaffin cells
    • Kibble, A. V., Barnard, R. J. O., and Burgoyne, R. D. (1996) Patch-clamp capacitance analysis of the effects of α-SNAP on exocytosis in adrenal chromaffin cells. J. Cell Sci. 109, 2417-2422.
    • (1996) J. Cell Sci. , vol.109 , pp. 2417-2422
    • Kibble, A.V.1    Barnard, R.J.O.2    Burgoyne, R.D.3
  • 8
    • 0009517180 scopus 로고
    • Composition of surface active material
    • (Crystal, R.G., ed.), Marcel Dekker, New York
    • Clements, J. A., and King, R. J. (1976) Composition of surface active material. In The Biochemical Basis of Pulmonary Function (Crystal, R.G., ed.), pp. 363-387, Marcel Dekker, New York.
    • (1976) The Biochemical Basis of Pulmonary Function , pp. 363-387
    • Clements, J.A.1    King, R.J.2
  • 9
    • 0015894118 scopus 로고
    • Isolation and characterization of lamellar bodies and tubular myelin from rat lung homogenate
    • Gil, J., and Reiss, O. K. (1973) Isolation and characterization of lamellar bodies and tubular myelin from rat lung homogenate. J. Cell Biol. 58, 152-171.
    • (1973) J. Cell Biol. , vol.58 , pp. 152-171
    • Gil, J.1    Reiss, O.K.2
  • 10
    • 0025328270 scopus 로고
    • Regulation of lung surfactant secretion
    • Chander, A., and Fisher, A. B. (1990) Regulation of lung surfactant secretion. Am. J. Physiol. 258, L241-L253.
    • (1990) Am. J. Physiol. , vol.258
    • Chander, A.1    Fisher, A.B.2
  • 11
    • 0028049687 scopus 로고
    • Molecular and cellular processing of lung surfactant
    • Rooney, S. S., Young, S. L., and Medelson, C. R. (1994) Molecular and cellular processing of lung surfactant. FASEB J. 8, 957-967.
    • (1994) FASEB J. , vol.8 , pp. 957-967
    • Rooney, S.S.1    Young, S.L.2    Medelson, C.R.3
  • 12
    • 0026707599 scopus 로고
    • Secretagogue-induced proteolysis of lung spectrin in alveolar epithelial type II cells
    • Zimmerman, U.-J. P., Speicher, D. W., and Fisher, A. B. (1992) Secretagogue-induced proteolysis of lung spectrin in alveolar epithelial type II cells. Biochim. Biophys. Acta 1137, 127-134.
    • (1992) Biochim. Biophys. Acta , vol.1137 , pp. 127-134
    • Zimmerman, U.-J.P.1    Speicher, D.W.2    Fisher, A.B.3
  • 13
    • 0029115870 scopus 로고
    • Inhibition of secretion from isolated rat alveolar epithelial type II cells by the cell permeant calpain inhibitor II (N-acetyl-leucyl-leucyl-methioninal)
    • Zimmerman, U.-J. P., Wang, M., and Liu, L. (1995) Inhibition of secretion from isolated rat alveolar epithelial type II cells by the cell permeant calpain inhibitor II (N-acetyl-leucyl-leucyl-methioninal). Cell Calcium 18, 1-8.
    • (1995) Cell Calcium , vol.18 , pp. 1-8
    • Zimmerman, U.-J.P.1    Wang, M.2    Liu, L.3
  • 14
    • 0030892186 scopus 로고    scopus 로고
    • Calpain: A cytosolic proteinase active at the membranes
    • Molinari, M., and Carafoli, E. (1997) Calpain: a cytosolic proteinase active at the membranes. J. Membr. Biol. 156, 1-8.
    • (1997) J. Membr. Biol. , vol.156 , pp. 1-8
    • Molinari, M.1    Carafoli, E.2
  • 15
    • 0023229512 scopus 로고
    • Correlation between calpain-mediated cytoskeletal degradation and expression of platelet procoagulant activity. A role for the platelet membrane-skeleton in the regulation of membrane lipid asymmetry?
    • Verhallen, P. F. J., Bevers, E. M., Comfurius, P., and Zwaal, R. F. A. (1987) Correlation between calpain-mediated cytoskeletal degradation and expression of platelet procoagulant activity. A role for the platelet membrane-skeleton in the regulation of membrane lipid asymmetry? Biochim. Biophys. Acta 903, 206-217.
    • (1987) Biochim. Biophys. Acta , vol.903 , pp. 206-217
    • Verhallen, P.F.J.1    Bevers, E.M.2    Comfurius, P.3    Zwaal, R.F.A.4
  • 16
    • 0023239520 scopus 로고
    • Phosphorylation and proteolytic modification of specific cytoskeletal proteins in human neutrophils stimulated by phorbol 12-myristate 13-acetate
    • Pontremoli, S., Melloni, E., Michetti, M., Sparatore, M., Salamino, F., Sacco, O., and Horecker, B. L. (1987) Phosphorylation and proteolytic modification of specific cytoskeletal proteins in human neutrophils stimulated by phorbol 12-myristate 13-acetate. Proc. Natl. Acad. Sci. USA 84, 3604-3608.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3604-3608
    • Pontremoli, S.1    Melloni, E.2    Michetti, M.3    Sparatore, M.4    Salamino, F.5    Sacco, O.6    Horecker, B.L.7
  • 17
    • 0027280456 scopus 로고
    • Cell-penetrating inhibitors of calpain block both membrane fusion and filamin cleavage in chick embryonic myoblasts
    • Kwak, K. B., Kambayashi, J.-I., Kang, M. S., Ha, D. B., and Chung, C. H. (1993) Cell-penetrating inhibitors of calpain block both membrane fusion and filamin cleavage in chick embryonic myoblasts. FEBS Lett. 323, 152-154.
    • (1993) FEBS Lett. , vol.323 , pp. 152-154
    • Kwak, K.B.1    Kambayashi, J.-I.2    Kang, M.S.3    Ha, D.B.4    Chung, C.H.5
  • 20
    • 0022527271 scopus 로고
    • An improved method for isolating type II cells in high yield and purity
    • Dobbs, L. G., Gonsalesz, R., and Williams, M. C. (1986) An improved method for isolating type II cells in high yield and purity. Am. Rev. Respir. Dis. 134, 141-145.
    • (1986) Am. Rev. Respir. Dis. , vol.134 , pp. 141-145
    • Dobbs, L.G.1    Gonsalesz, R.2    Williams, M.C.3
  • 21
    • 0020504618 scopus 로고
    • Isolation of lamellar bodies from rat granular pneumocytes in primary culture
    • Chander, A., Dodia, C. R., Gil, J., and Fisher, A. B. (1983) Isolation of lamellar bodies from rat granular pneumocytes in primary culture. Biochim. Biophys. Acta 753, 119-129.
    • (1983) Biochim. Biophys. Acta , vol.753 , pp. 119-129
    • Chander, A.1    Dodia, C.R.2    Gil, J.3    Fisher, A.B.4
  • 22
    • 0021683468 scopus 로고
    • Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates
    • Sasaki, T., Kikuchi, T., Yumoto, N., Yoshimura, N., and Murachi, T. (1984) Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. J. Biol. Chem. 259, 12489-12494.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12489-12494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murachi, T.5
  • 23
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett, M. K., and Scheller, R. H. (1993) The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl. Acad. Sci. USA 90, 2559-2563.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 24
    • 0028245594 scopus 로고
    • A molecular description of synaptic vesicle membrane trafficking
    • Bennett, M. K., and Scheller, R. H. (1994) A molecular description of synaptic vesicle membrane trafficking. Annu. Rev. Biochem. 63, 63-100.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 63-100
    • Bennett, M.K.1    Scheller, R.H.2
  • 25
    • 0027248876 scopus 로고
    • Tetanus and botulism neurotoxins: New group of zinc proteases
    • Montecucco, C., and Schiavo, G. (1993) Tetanus and botulism neurotoxins: new group of zinc proteases. Trends Biochem. Sci. 18, 324-327.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 324-327
    • Montecucco, C.1    Schiavo, G.2
  • 26
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann, H., Blasi, J., and Jahn, R. (1994) Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 4, 179-185.
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 30
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological-pathological involvemnt
    • Saido, T., Sorimachi, H., and Suzuki, K. (1994) Calpain: new perspectives in molecular diversity and physiological-pathological involvemnt. FASEB J. 8, 814-822.
    • (1994) FASEB J. , vol.8 , pp. 814-822
    • Saido, T.1    Sorimachi, H.2    Suzuki, K.3
  • 31
    • 0027988820 scopus 로고
    • Calpain inhibition: An overview of its therapeutic potential
    • Wang, K. K. W., and Yuen. P.-W. (1994) Calpain inhibition: an overview of its therapeutic potential. Trends Pharmacol. Sci. 15, 412-419.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 412-419
    • Wang, K.K.W.1    Yuen, P.-W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.