메뉴 건너뛰기




Volumn 71, Issue 1, 1997, Pages 37-44

Botulinum neurotoxin F, a VAMP-specific endopeptidase, inhibits CA2+- stimulated GH secretion from rat pituitary cells

Author keywords

Cell culture; Exocytosis; Immunohistochemistry; Secretory granule; Synaptobrevin; Vesicle

Indexed keywords

BOTULINUM TOXIN; CALCIUM ION; GROWTH HORMONE; PROTEINASE;

EID: 0343118139     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-0115(97)01017-3     Document Type: Article
Times cited : (6)

References (55)
  • 1
    • 0028491306 scopus 로고
    • Clostridial neurotoxins as a tool to investigate the molecular events of neurotransmitter release
    • Schiavo G, Rossetto O, Montecucco C. Clostridial neurotoxins as a tool to investigate the molecular events of neurotransmitter release. Semin Cell Biol 1994;5:221-9.
    • (1994) Semin Cell Biol , vol.5 , pp. 221-229
    • Schiavo, G.1    Rossetto, O.2    Montecucco, C.3
  • 2
    • 0002151193 scopus 로고
    • Bacterial sources of clostridial neurotoxins
    • Simpson LL, editor. San Diego: Academic Press
    • Hatheway CL, Bacterial sources of clostridial neurotoxins. In: Simpson LL, editor. Botulinum neurotoxin and tetanus toxin, San Diego: Academic Press, 1989: 3-24.
    • (1989) Botulinum Neurotoxin and Tetanus Toxin , pp. 3-24
    • Hatheway, C.L.1
  • 3
    • 0023658427 scopus 로고
    • 2-terminus of the heavy subunit of Clostridium botulinum type a neurotoxin forms channels in lipid vesicles
    • 2-terminus of the heavy subunit of Clostridium botulinum type A neurotoxin forms channels in lipid vesicles. Eur J Biochem 1987;167:175-80.
    • (1987) Eur J Biochem , vol.167 , pp. 175-180
    • Shone, C.C.1    Hambleton, P.2    Melling, J.3
  • 5
    • 46149134882 scopus 로고
    • How do tetanus and botulinum toxins bind to neuronal membranes?
    • Montecucco C. How do tetanus and botulinum toxins bind to neuronal membranes?. Trends Biochem Sci 1986;11:314-7.
    • (1986) Trends Biochem Sci , vol.11 , pp. 314-317
    • Montecucco, C.1
  • 6
    • 0028341442 scopus 로고
    • Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes
    • Nishiki T, Kamata Y, Nemoto Y, Omori A, Ito T, Takahashi M, Kozaki S. Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J Biol Chem 1994;269:10498-503.
    • (1994) J Biol Chem , vol.269 , pp. 10498-10503
    • Nishiki, T.1    Kamata, Y.2    Nemoto, Y.3    Omori, A.4    Ito, T.5    Takahashi, M.6    Kozaki, S.7
  • 7
    • 0022556315 scopus 로고
    • 125I-labeled botulinum neurotoxins with nerve terminals. Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis
    • 125I-labeled botulinum neurotoxins with nerve terminals. Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis. J Cell Biol 1986;103:535-44.
    • (1986) J Cell Biol , vol.103 , pp. 535-544
    • Black, J.D.1    Dolly, J.O.2
  • 10
    • 0026673922 scopus 로고
    • Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc
    • Schiavo G, Poulain B, Rossetto O, Benfenati F, Taue L, Montecucco C. Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc. EMBO J 1992;11:3577-83.
    • (1992) EMBO J , vol.11 , pp. 3577-3583
    • Schiavo, G.1    Poulain, B.2    Rossetto, O.3    Benfenati, F.4    Taue, L.5    Montecucco, C.6
  • 12
    • 0027241009 scopus 로고
    • Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin
    • Schiavo G, Shone CC, Rossetto O, Alexander FCG, Montecucco C. Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J Biol Chem 1993;268:11516-9.
    • (1993) J Biol Chem , vol.268 , pp. 11516-11519
    • Schiavo, G.1    Shone, C.C.2    Rossetto, O.3    Alexander, F.C.G.4    Montecucco, C.5
  • 14
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof TC. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 1995;375:645-53.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 15
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
    • Baumert M, Maycox PR, Navone F, De Camilli P, Jahn R. Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO J 1989;8:379-84.
    • (1989) EMBO J , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De Camilli, P.4    Jahn, R.5
  • 16
    • 0006602702 scopus 로고
    • VAMP-1: A synaptic vesicle-associated integral membrane protein
    • Trimble WS, Cowan DM, Scheller RH. VAMP-1: A synaptic vesicle-associated integral membrane protein. Proc Natl Acad Sci USA 1988;85:4538-42.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 17
    • 0024308501 scopus 로고
    • Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system
    • Elferink LA, Trimble WS, Scheller RH. Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J Biol Chem 1989;264:11061-4.
    • (1989) J Biol Chem , vol.264 , pp. 11061-11064
    • Elferink, L.A.1    Trimble, W.S.2    Scheller, R.H.3
  • 21
    • 0027176523 scopus 로고
    • Snappy exocytoxins
    • Huttner WB. Snappy exocytoxins. Nature 1993;365:104-5.
    • (1993) Nature , vol.365 , pp. 104-105
    • Huttner, W.B.1
  • 24
    • 0027434988 scopus 로고
    • Botulinum a like type B and tetanus toxins fulfils criteria for being a zinc-dependent protease
    • de Paiva A, Ashton AC, Foran P, Schiavo G, Montecucco C, Dolly JO. Botulinum A like type B and tetanus toxins fulfils criteria for being a zinc-dependent protease. J Neurochem 1993;61:2338-41.
    • (1993) J Neurochem , vol.61 , pp. 2338-2341
    • De Paiva, A.1    Ashton, A.C.2    Foran, P.3    Schiavo, G.4    Montecucco, C.5    Dolly, J.O.6
  • 26
    • 0027432376 scopus 로고
    • Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin
    • Blasi J, Chapman ER, Yamasaki S, Binz T, Niemann H, Jahn R. Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J 1993;12:4821-8.
    • (1993) EMBO J , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamasaki, S.3    Binz, T.4    Niemann, H.5    Jahn, R.6
  • 29
    • 0030457774 scopus 로고    scopus 로고
    • Molecular components of the exocytotic machinery in the rat pituitary gland
    • Jacobsson G, Meister B. Molecular components of the exocytotic machinery in the rat pituitary gland. Endocrinology 1996;137:5344-56.
    • (1996) Endocrinology , vol.137 , pp. 5344-5356
    • Jacobsson, G.1    Meister, B.2
  • 30
    • 0017291095 scopus 로고
    • Enzymatic dissociation and short-term culture of isolated rat anterior pituitary cells for studies on the control of hormone secretion
    • Nakano H, Fawcett CP, McCann SM. Enzymatic dissociation and short-term culture of isolated rat anterior pituitary cells for studies on the control of hormone secretion. Endocrinology 1976;98:278-88.
    • (1976) Endocrinology , vol.98 , pp. 278-288
    • Nakano, H.1    Fawcett, C.P.2    McCann, S.M.3
  • 31
    • 0024368011 scopus 로고
    • Poration by alpha-toxin and streptolysin O: An approach to analyze intracellular processes
    • Ahnert-Hilger G, Mach W, Fohr KJ, Gratzl M. Poration by alpha-toxin and streptolysin O: an approach to analyze intracellular processes. Methods Cell Biol 1989;31:63-90.
    • (1989) Methods Cell Biol , vol.31 , pp. 63-90
    • Ahnert-Hilger, G.1    Mach, W.2    Fohr, K.J.3    Gratzl, M.4
  • 32
    • 0020319190 scopus 로고
    • Calcium-dependence of catecholamine release from bovine adrenal medullary cells after exposure to intense electric fields
    • Knight DE, Baker PF. Calcium-dependence of catecholamine release from bovine adrenal medullary cells after exposure to intense electric fields. J Membr Biol 1982;68:107-40.
    • (1982) J Membr Biol , vol.68 , pp. 107-140
    • Knight, D.E.1    Baker, P.F.2
  • 33
    • 0019038173 scopus 로고
    • Neutral carrier ion-selective microelectrodes for measurement of intracellular free calcium
    • Tsien RY, Rink TJ. Neutral carrier ion-selective microelectrodes for measurement of intracellular free calcium. Biochim Biophys Acta 1980;599:623-38.
    • (1980) Biochim Biophys Acta , vol.599 , pp. 623-638
    • Tsien, R.Y.1    Rink, T.J.2
  • 34
    • 0000191753 scopus 로고
    • UV-method with pyruvate and NADH
    • Bergmeyer HU editor. Weinheim (Germany): Verlag Chemie
    • Vassault A. UV-method with pyruvate and NADH. In: Bergmeyer HU editor. Methods of enzymatic analysis. Weinheim (Germany): Verlag Chemie, 1983: 118-126.
    • (1983) Methods of Enzymatic Analysis , pp. 118-126
    • Vassault, A.1
  • 35
    • 0001425238 scopus 로고
    • Buffered picric acid formaldehyde: A new rapid fixative for electron microscopy
    • Zamboni L, De Martino C. Buffered picric acid formaldehyde: a new rapid fixative for electron microscopy. J Cell Biol 1967;148:35.
    • (1967) J Cell Biol , vol.148 , pp. 35
    • Zamboni, L.1    De Martino, C.2
  • 36
    • 0018152376 scopus 로고
    • Plasma levels of growth hormone in female rats of different ages
    • Eden S, Albertsson-Wikland K, Isaksson O. Plasma levels of growth hormone in female rats of different ages. Acta Endocrinol 1978;88:676-90.
    • (1978) Acta Endocrinol , vol.88 , pp. 676-690
    • Eden, S.1    Albertsson-Wikland, K.2    Isaksson, O.3
  • 38
    • 0015146643 scopus 로고
    • Use of polyethylene glycol to separate free and antibody-bound peptide hormones in radioimmunoassays
    • Desbuquois B, Aurbach GD. Use of polyethylene glycol to separate free and antibody-bound peptide hormones in radioimmunoassays. J Clin Endocrinol 1971;33:732-8.
    • (1971) J Clin Endocrinol , vol.33 , pp. 732-738
    • Desbuquois, B.1    Aurbach, G.D.2
  • 39
    • 0023681320 scopus 로고
    • An ultrastructural and functional characterization of rat somatotrophs highly enriched on a continuous Percoll density gradient
    • Ohlsson L, Lindström P, Norlund P. An ultrastructural and functional characterization of rat somatotrophs highly enriched on a continuous Percoll density gradient. Mol Cell Endocrinol 1988;59:47-55.
    • (1988) Mol Cell Endocrinol , vol.59 , pp. 47-55
    • Ohlsson, L.1    Lindström, P.2    Norlund, P.3
  • 42
    • 0030023904 scopus 로고    scopus 로고
    • Vamp/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues
    • Rossetto O, Gorza L, Schiavo G, Schiavo N, Scheller RH, Montecucco C. Vamp/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues. J Cell Biol 1996;132:167-79.
    • (1996) J Cell Biol , vol.132 , pp. 167-179
    • Rossetto, O.1    Gorza, L.2    Schiavo, G.3    Schiavo, N.4    Scheller, R.H.5    Montecucco, C.6
  • 43
    • 0028861707 scopus 로고
    • Vesicle-associated membrane protein (VAMP)/synaptobrevin-2 is associated with dense core secretory granules in PC12 neuroendocrine cells
    • Papini E, Rossetto O, Cutler DF. Vesicle-associated membrane protein (VAMP)/synaptobrevin-2 is associated with dense core secretory granules in PC12 neuroendocrine cells. J Biol Chem 1995;270:1332-6.
    • (1995) J Biol Chem , vol.270 , pp. 1332-1336
    • Papini, E.1    Rossetto, O.2    Cutler, D.F.3
  • 44
    • 0027971368 scopus 로고
    • Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle
    • Calakos N, Scheller RH. Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle. J Biol Chem 1994;269:24543-7.
    • (1994) J Biol Chem , vol.269 , pp. 24543-24547
    • Calakos, N.1    Scheller, R.H.2
  • 46
  • 49
    • 0027416837 scopus 로고
    • Comparison of the intracellular effects of clostridial neurotoxins on exocytosis from streptolysin O-permeabilized rat pheochromocytoma (PC12) and bovine adrenal chromaffin cells
    • Ahnert-Hilger G, Weller U. Comparison of the intracellular effects of clostridial neurotoxins on exocytosis from streptolysin O-permeabilized rat pheochromocytoma (PC12) and bovine adrenal chromaffin cells. Neuroscience 1993;53:547-52.
    • (1993) Neuroscience , vol.53 , pp. 547-552
    • Ahnert-Hilger, G.1    Weller, U.2
  • 50
    • 0023775458 scopus 로고
    • Dissection of Semliki forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells
    • DeCurtis I, Simons K. Dissection of Semliki forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells. Proc Natl Acad Sci USA 1988;85:8052-6.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8052-8056
    • DeCurtis, I.1    Simons, K.2
  • 51
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the frans-cisternae of the Golgi complex to the plasma membrane
    • Griffiths G, Pfeffer S, Simons K, Matlin K. Exit of newly synthesized membrane proteins from the frans-cisternae of the Golgi complex to the plasma membrane. J Cell Biol 1985;101:949-64.
    • (1985) J Cell Biol , vol.101 , pp. 949-964
    • Griffiths, G.1    Pfeffer, S.2    Simons, K.3    Matlin, K.4
  • 52
    • 0023663868 scopus 로고
    • The trans-most cisternae of the Golgi complex: A compartment for sorting of secretory and plasma membrane proteins
    • Orci L, Ravazzola M, Amherdt M, Perrelet A, Powell S, Quinn D, Moore H-P. The trans-most cisternae of the Golgi complex: a compartment for sorting of secretory and plasma membrane proteins. Cell 1987;51:1039-51.
    • (1987) Cell , vol.51 , pp. 1039-1051
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Perrelet, A.4    Powell, S.5    Quinn, D.6    Moore, H.-P.7
  • 53
    • 0025961797 scopus 로고
    • Reconstitution of constitutive secretion using semi-intact cells: Regulation by GTP but not calcium
    • Miller SG, Moore H-PH. Reconstitution of constitutive secretion using semi-intact cells: regulation by GTP but not calcium. J Cell Biol 1991;112:39-54.
    • (1991) J Cell Biol , vol.112 , pp. 39-54
    • Miller, S.G.1    Moore, H.-P.H.2
  • 54
    • 0000719018 scopus 로고
    • The adenohypophysis
    • Kovacs K, Asa SL, editors. Boston: Blackwell Scientific Publications
    • Horvath E, Kovacs K, The adenohypophysis. In: Kovacs K, Asa SL, editors. Functional endocrine pathology. Boston: Blackwell Scientific Publications, 1991: 245-281.
    • (1991) Functional Endocrine Pathology , pp. 245-281
    • Horvath, E.1    Kovacs, K.2
  • 55
    • 0029011652 scopus 로고
    • Clinical features and differential diagnosis of pituitary tumours with emphasis on acromegaly
    • Hennessey JV, Jackson IMD. Clinical features and differential diagnosis of pituitary tumours with emphasis on acromegaly. Bailliere's Clin Endocrinol Metabol 1995;9:271-314.
    • (1995) Bailliere's Clin Endocrinol Metabol , vol.9 , pp. 271-314
    • Hennessey, J.V.1    Jackson, I.M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.