Anti-syntaxin Antibodies Inhibit Calcium-Dependent Catecholamine Secretion from Permeabilized Chromaffin Cells

Gutiérrez, Luis M.; Quintanar, J. Luis; Viniegra, Salvador; Salinas, Eva; Moya, Fernando; Reig, Juan A.

doi:10.1006/bbrc.1995.1001

Cited by 35 publications

(18 citation statements)

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“…permeabilized chromaffin cells Secreted [3H]noradrenaline was determined in digitonin-permeabilized cells as described [20]. Briefly, cells were incubated with [3H]noradrenaline (1/tCi/ml) in DMEM during 4 h. Thereafter, monolayers were washed 4 times with a Krebs/HEPES basal solution: 15 mM HEPES, pH 7.4, with 134 mM NaCI 4.7 mM KC1 1.2 mM KH2PO 4 1.2 mM MgC12 2.5 mM CaCI 2 0.56 mM ascorbic acid 11 mM Glucose.…”

Section: Determination Of Catecholamine Release From Detergent-mentioning

confidence: 99%

A peptide that mimics the carboxy‐terminal domain of SNAP‐25 blocks Ca²⁺‐dependent exocytosis in chromaffin cells

et al. 1995

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Section: Determination Of Catecholamine Release From Detergent-mentioning

confidence: 99%

A peptide that mimics the carboxy‐terminal domain of SNAP‐25 blocks Ca²⁺‐dependent exocytosis in chromaffin cells

et al. 1995

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“…In contrast to the wide distribution of synaptobrevins in non-neuronal cells, the mammalian syntaxin 1 (A or B forms) has been detected only in brain (Bennett et al, 1992) and neurosecretory tissues (Jacobsson et al, 1994;Gutierrez et al, 1995). However, it is conceivable that non-neuronal homologues of syntaxin 1 participate in intracellular traffic in mammalian cells, in particular in the docking/fusion of GLUT4 glucose transporter-containing vesicles of insulin-sensitive cells.…”

Section: Introductionmentioning

confidence: 99%

Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport.

Volchuk

Wang

Ewart

et al. 1996

MBoC

136

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Syntaxins are thought to be membrane receptors that bind proteins of the synaptobrevin/ vesicle-associated membrane protein (VAMP) family found on transport vesicles. Recently, we detected synaptobrevin II and cellubrevin on immunopurified vesicles containing the glucose transporter 4 (GLUT4) in insulin-responsive cells. In an effort to identify the plasma membrane receptors for these vesicles, we now examine the expression of syntaxins in the 3T3-L1 adipocyte cell line. Neither syntaxin 1A nor 1B was found, in keeping with the neuronal restriction of these isoforms. In contrast, syntaxins 2 and 4 were readily detectable. By subcellular fractionation and estimation of protein yields, 67% of syntaxin 4 was localized to the plasma membrane, 24% to the low-density microsomes, and 9% to the high-density microsomes. Interestingly, acute insulin treatment decreased the content of syntaxin 4 in low-density microsomes and caused a corresponding gain in the plasma membrane fraction, reminiscent of the recruitment of GLUT4 glucose transporters. In contrast, there was no change in the distribution of syntaxin 2, which was mostly associated in the plasma membrane. A fraction of the intracellular syntaxin 4 was recovered with immunopurified GLUT4-containing vesicles. Moreover, anti-syntaxin 4 antibodies introduced into permeabilized 3T3-L1 adipocytes significantly reduced the insulin-dependent stimulation of glucose transport, in contrast to the introduction of irrelevant immunoglobulin G, which was without consequence. We propose that either the plasma membrane and/or the vesicular syntaxin 4 are involved in docking and/or fusion of GLUT4 vesicles at the cell surface of 3T3-L1 adipocytes.INTRODUCTION Molecules presumed to be involved in docking and fusion of synaptic vesicles with the plasma membrane of presynaptic nerve terminals have been identified recently. These are the vesicular synaptobrevin II/

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“…SNARE hypothesis predicts that the docking of vesicles with target membranes is mediated by the specific interaction between t-and v-SNAREs [7]. Although the involvement of NSF-SNAPs-SNAREs in various fusion events including exocytosis in chromaffin cells [17][18][19][20], recent studies revealed that t-SNAREs are localized not only on the plasma membrane but also on synaptic vesicles [21][22][23]. These results raised the question of whether or not syntaxin 1 and SNAP-25 act as t-SNAREs.…”

Section: Introductionmentioning

confidence: 99%

SNAP‐25 is present on chromaffin granules and acts as a SNAP receptor

et al. 1996

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SNAP-25 is located on the plasma membrane and essential for exocytosis of neurotransmitters. It was suggested that SNAP-25 and syntaxin 1 via the interaction with VAMP-2 located on synaptic vesicles mediate the docking of the vesicles with the plasma membrane. In the present study, by means of biochemical and morphological analyses, we showed that SNAP-25 is present on chromaffin granules as well as on the plasma membrane. Reconstitution and immunoprecipitation analyses revealed that SNAP-25 on chromaffin granules has essentially the same properties as does SNAP-25 on the plasma membrane.

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Anti-syntaxin Antibodies Inhibit Calcium-Dependent Catecholamine Secretion from Permeabilized Chromaffin Cells

Cited by 35 publications

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A peptide that mimics the carboxy‐terminal domain of SNAP‐25 blocks Ca²⁺‐dependent exocytosis in chromaffin cells

A peptide that mimics the carboxy‐terminal domain of SNAP‐25 blocks Ca²⁺‐dependent exocytosis in chromaffin cells

Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport.

SNAP‐25 is present on chromaffin granules and acts as a SNAP receptor

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Anti-syntaxin Antibodies Inhibit Calcium-Dependent Catecholamine Secretion from Permeabilized Chromaffin Cells

Cited by 35 publications

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A peptide that mimics the carboxy‐terminal domain of SNAP‐25 blocks Ca2+‐dependent exocytosis in chromaffin cells

A peptide that mimics the carboxy‐terminal domain of SNAP‐25 blocks Ca2+‐dependent exocytosis in chromaffin cells

Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport.

SNAP‐25 is present on chromaffin granules and acts as a SNAP receptor

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A peptide that mimics the carboxy‐terminal domain of SNAP‐25 blocks Ca²⁺‐dependent exocytosis in chromaffin cells

A peptide that mimics the carboxy‐terminal domain of SNAP‐25 blocks Ca²⁺‐dependent exocytosis in chromaffin cells