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Journal articles on the topic 'Vamps'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Rose, Adam J., Jacob Jeppesen, Bente Kiens, and Erik A. Richter. "Effects of contraction on localization of GLUT4 and v-SNARE isoforms in rat skeletal muscle." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 297, no. 5 (November 2009): R1228—R1237. http://dx.doi.org/10.1152/ajpregu.00258.2009.

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In skeletal muscle, contractions increase glucose uptake due to a translocation of GLUT4 glucose transporters from intracellular storage sites to the surface membrane. Vesicle-associated membrane proteins (VAMPs) are believed to play an important role in docking and fusion of the GLUT4 transporters at the surface membrane. However, knowledge about which VAMP isoforms colocalize with GLUT4 vesicles in mature skeletal muscle and whether they translocate during muscle contractions is incomplete. The aim of the present study was to further identify VAMP isoforms, which are associated with GLUT4 vesicles and examine which VAMP isoforms translocate to surface membranes in skeletal muscles undergoing contractions. VAMP2, VAMP3, VAMP5, and VAMP7 were enriched in immunoprecipitated GLUT4 vesicles. In response to 20 min of in situ contractions, there was a redistribution of GLUT4 (+64 ± 13%), transferrin receptor (TfR; +75 ± 22%), and insulin-regulated aminopeptidase (IRAP; +70 ± 13%) to fractions enriched in heavy membranes away from low-density membranes (−32 ± 7%; −18 ± 12%; −33 ± 9%; respectively), when compared with the resting contralateral muscle. Similarly, there was a redistribution of VAMP2 (+240 ± 40%), VAMP5 (+79 ± 9%), and VAMP7 (+79 ± 29%), but not VAMP3, to fractions enriched in heavy membranes away from low-density membranes (−49 ± 10%, −54 ± 9%, −14 ± 11%, respectively) in contracted vs. resting muscle. In summary, VAMP2, VAMP3, VAMP5, and VAMP7 coimmunoprecipitate with intracellular GLUT4 vesicles in muscle, and VAMP2, VAMP5, VAMP7, but not VAMP3, translocate to the cell surface membranes similar to GLUT4, TfR, and IRAP in response to muscle contractions. These findings suggest that VAMP2, VAMP5, and VAMP7 may be involved in translocation of GLUT4 during muscle contractions.

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2

Sadler, Jessica B. A., Nia J. Bryant, and Gwyn W. Gould. "Characterization of VAMP isoforms in 3T3-L1 adipocytes: implications for GLUT4 trafficking." Molecular Biology of the Cell 26, no. 3 (February 2015): 530–36. http://dx.doi.org/10.1091/mbc.e14-09-1368.

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The fusion of GLUT4-containing vesicles with the plasma membrane of adipocytes is a key facet of insulin action. This process is mediated by the formation of functional soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complexes between the plasma membrane t-SNARE complex and the vesicle v-SNARE or VAMP. The t-SNARE complex consists of Syntaxin4 and SNAP23, and whereas many studies identify VAMP2 as the v-SNARE, others suggest that either VAMP3 or VAMP8 may also fulfil this role. Here we characterized the levels of expression, distribution, and association of all the VAMPs expressed in 3T3-L1 adipocytes to provide the first systematic analysis of all members of this protein family for any cell type. Despite our finding that all VAMP isoforms form SDS-resistant SNARE complexes with Syntaxin4/SNAP23 in vitro, a combination of levels of expression (which vary by >30-fold), subcellular distribution, and coimmunoprecipitation analyses lead us to propose that VAMP2 is the major v-SNARE involved in GLUT4 trafficking to the surface of 3T3-L1 adipocytes.

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3

Jeff Bursey. "Estonian Vamps." American Book Review 31, no. 2 (2010): 15. http://dx.doi.org/10.1353/abr.0.0026.

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4

TIMMERS, Kim I., Avril E. CLARK, Mariko OMATSU-KANBE, Sidney W. WHITEHEART, Mark K. BENNETT, Geoffrey D. HOLMAN, and Samuel W. CUSHMAN. "Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein." Biochemical Journal 320, no. 2 (December 1, 1996): 429–36. http://dx.doi.org/10.1042/bj3200429.

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The vesicle-associated membrane proteins [VAMPs; vesicle SNAP receptors (v-SNAREs)] present on GLUT4-enriched vesicles prepared from rat adipose cells [Cain, Trimble and Lienhard (1992) J. Biol. Chem. 267, 11681–11684] have been identified as synaptobrevin 2 (VAMP 2) and cellubrevin (VAMP 3) by using isoform-specific antisera. Additional antisera identify syntaxins 2 and 4 as the predominant target membrane SNAP receptors (t-SNAREs) in the plasma membranes (PM), with syntaxin 3 at one-twentieth the level. Syntaxins 2 and 4 are enriched 5–10-fold in PM compared with low-density microsomes (LDM). Insulin treatment results in an 11-fold increase in immunodetectable GLUT4 in PM and smaller (approx. 2-fold) increases in VAMP 2 and VAMP 3, whereas the subcellular distributions of the syntaxins are not altered by insulin treatment. To determine which of the SNAP receptors (SNAREs) in PM might participate in SNARE complexes with proteins from GLUT4 vesicles, complexes were immunoprecipitated with anti-myc antibody from solubilized membranes after the addition of myc-epitope-tagged N-ethylmaleimide-sensitive fusion protein (NSF) and recombinant α-soluble NSF attachment protein (α-SNAP). These complexes contain VAMPs 2 and 3 and syntaxin 4, but not syntaxins 2 or 3. Complex formation requires ATP and is disrupted by ATP hydrolysis. When all membrane fractions are prepared from basal cells, few or no VAMPs and no syntaxin 4 are immunoprecipitated in SNARE complexes obtained from LDM alone (or from immunoisolated GLUT4 vesicles). The content of syntaxin 4 depends on the presence of PM, and participation of VAMPs 2 and 3 is enhanced 4–6-fold by the addition of solubilized GLUT4 vesicles to PM. The latter increase is greater than can be explained by the 2-fold higher levels of VAMPs added to the reaction mixture. When all membrane fractions are prepared from insulin-stimulated cells, SNARE complexes formed from PM alone contain similar levels of syntaxin 4 but 5–6-fold higher levels of VAMPs 2 and 3 compared with PM alone from basal cells. Addition of GLUT4 vesicle proteins to PM from insulin-treated cells results in a further 2-fold increase in VAMP 2 recovered in SNARE complexes. Therefore the VAMPs in PM of insulin-treated but not basal cells, and in GLUT4-vesicles from cells in either condition, are in a form that readily forms a SNARE complex with PM t-SNAREs and NSF. Insulin seems to activate PM and/or GLUT4 vesicles so as to increase the efficiency of SNARE complex formation.

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5

Zeng, Qi, V. Nathan Subramaniam, Siew Heng Wong, Bor Luen Tang, Robert G. Parton, Shane Rea, David E. James, and Wanjin Hong. "A Novel Synaptobrevin/VAMP Homologous Protein (VAMP5) Is Increased during In Vitro Myogenesis and Present in the Plasma Membrane." Molecular Biology of the Cell 9, no. 9 (September 1998): 2423–37. http://dx.doi.org/10.1091/mbc.9.9.2423.

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cDNA clones encoding a novel protein (VAMP5) homologous to synaptobrevins/VAMPs are detected during database searches. The predicted 102–amino acid VAMP5 harbors a 23-residue hydrophobic region near the carboxyl terminus and exhibits an overall amino acid identity of 33% with synaptobrevin/VAMP1 and 2 and cellubrevin. Northern blot analysis reveals that the mRNA for VAMP5 is preferentially expressed in the skeletal muscle and heart, whereas significantly lower levels are detected in several other tissues but not in the brain. During in vitro differentiation (myogenesis) of C2C12 myoblasts into myotubes, the mRNA level for VAMP5 is increased ∼8- to 10-fold. Immunoblot analysis using antibodies specific for VAMP5 shows that the protein levels are also elevated ∼6-fold during in vitro myogenesis of C2C12 cells. Indirect immunofluorescence microscopy and immunoelectron microscopy reveal that VAMP5 is associated with the plasma membrane as well as intracellular perinuclear and peripheral vesicular structures of myotubes. Epitope-tagged versions of VAMP5 are similarly targeted to the plasma membrane.

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6

Garcia, Edwin A., Giampaolo Trivellin, Elena D. Aflorei, Michael Powell, Joana Grieve, Ghassan Alusi, Luis Pobereskin, et al. "Characterization of SNARE Proteins in Human Pituitary Adenomas: Targeted Secretion Inhibitors as a New Strategy for the Treatment of Acromegaly?" Journal of Clinical Endocrinology & Metabolism 98, no. 12 (December 1, 2013): E1918—E1926. http://dx.doi.org/10.1210/jc.2013-2602.

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Context: Targeted secretion inhibitors (TSIs), a new class of recombinant biotherapeutic proteins engineered from botulinum toxin, represent a novel approach for treating diseases with excess secretion. They inhibit hormone secretion from targeted cell types through cleavage of SNARE (soluble N-ethylmaleimide-sensitive factor-activating protein receptor) proteins. qGHRH-LHN/D is a TSI targeting pituitary somatotroph through binding to the GHRH-receptor and cleavage of the vesicle-associated membrane protein (VAMP) family of SNARE proteins. Objective: Our objective was to study SNARE protein expression in pituitary adenomas and to inhibit GH secretion from somatotropinomas using qGHRH-LHN/D. Design: We analyzed human pituitary adenoma analysis for SNARE expression and response to qGHRH-LHN/D treatment. Setting: The study was conducted in University Hospitals. Patients: We used pituitary adenoma samples from 25 acromegaly and 47 nonfunctioning pituitary adenoma patients. Outcome: Vesicle-SNARE (VAMP1–3), target-SNARE (syntaxin1, SNAP-23, and SNAP-25), and GHRH-receptor detection with RT-qPCR, immunocytochemistry, and immunoblotting. Assessment of TSI catalytic activity on VAMPs and release of GH from adenoma cells. Results: SNARE proteins were variably expressed in pituitary samples. In vitro evidence using recombinant GFP-VAMP2&3 or pituitary adenoma lysates suggested sufficient catalytic activity of qGHRH-LHN/D to degrade VAMPs, but was unable to inhibit GH secretion in somatotropinoma cell cultures. Conclusions: SNARE proteins are present in human pituitary somatotroph adenomas that can be targeted by TSIs to inhibit GH secretion. qGHRH-LHN/D was unable to inhibit GH secretion from human somatotroph adenoma cells. Further studies are required to understand how the SNARE proteins drive GH secretion in human somatotrophs to allow the development of novel TSIs with a potential therapeutic benefit.

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7

d'Hugues, Philippe. "Le temps des vamps." Commentaire Numéro 84, no. 4 (October 1, 1998): 1167–68. http://dx.doi.org/10.3917/comm.084.1167.

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8

Williams, Dumaine, and Jeffrey E. Pessin. "Mapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes." Journal of Cell Biology 180, no. 2 (January 28, 2008): 375–87. http://dx.doi.org/10.1083/jcb.200709108.

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The functional trafficking steps used by soluble NSF attachment protein receptor (SNARE) proteins have been difficult to establish because of substantial overlap in subcellular localization and because in vitro SNARE-dependent binding and fusion reactions can be promiscuous. Therefore, to functionally identify the site of action of the vesicle-associated membrane protein (VAMP) family of R-SNAREs, we have taken advantage of the temporal requirements of adipocyte biosynthetic sorting of a dual-tagged GLUT4 reporter (myc-GLUT4-GFP) coupled with small interfering RNA gene silencing. Using this approach, we confirm the requirement of VAMP2 and VAMP7 for insulin and osmotic shock trafficking from the vesicle storage sites, respectively, and fusion with the plasma membrane. Moreover, we identify a requirement for VAMP4 for the initial biosynthetic entry of GLUT4 from the Golgi apparatus into the insulin-responsive vesicle compartment, VAMP8, for plasma membrane endocytosis and VAMP2 for sorting to the specialized insulin-responsive compartment after plasma membrane endocytosis.

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9

Peters, Christian G., and Robert Flaumenhaft. "Localization of VAMP Isoforms In Platelets Reveals Separate Granule Populations with Distinct Functions." Blood 116, no. 21 (November 19, 2010): 2015. http://dx.doi.org/10.1182/blood.v116.21.2015.2015.

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Abstract Abstract 2015 Secretion of granules from platelets is essential for normal platelet activity in hemostasis and thrombosis. Platelet granules have different morphologies and different granule subpopulations contain distinct cargos. Platelet granules not only participate in the release of granule contents, but also appear to function to increase plasma membrane surface area during platelet spreading, morphogenesis, tether formation, and membrane repair. Whether different granule subpopulations mediate these distinct functions of the granule is currently not known. To judge whether specific subpopulations of granules are involved in different granule functions, we evaluated the subcellular localization of vesicle-associated membrane proteins (VAMPs) in resting and spread platelets using immunofluorescence confocal microscopy. Imaging showed that VAMP 3- and VAMP 8-containing granules segregate from one another into distinct granule populations (Pearson (R) correlation values (R = 0.143 ± .039, n=25). Fibrinogen and von Willebrand factor (vWF) also segregated from one another (R= 0.099 ± .027, n=15), but associated with granules containing either VAMP 3 or 8 (R = 0.447 ± 0.065 and R = 0.5485 ± 0.62, n=20, respectively). To visualize the granule contribution to membrane remodeling during spreading, granule membranes were selectively labeled using the membrane dye FM 1–43 followed by washout of external dye. Following platelet spreading, FM 1–43-labeled granules coalesced at the ends of pseudopodia and appeared as punctate areas of FM-1-43 staining on the plasma membrane. Quantitation of staining within spread platelets demonstrated that 92% of granules expressing VAMP 8 translocated with their associated cargo (vWF or fibrinogen) to the central granulomere. VAMP 3 also translocated with vWF and fibrinogen to the granulomere in spread platelets. In contrast, only 31% of granules expressing VAMP 5 localized to the granulomere of spread platelets, while 69% of VAMP 5 staining localized to pseudopodia and lamellipodia at the platelet periphery. Granules expressing VAMP 5 demonstrated little colocalization with vWF and fibrinogen in spread platelets. Similarly, VAMP 7 translocated to pseudopodia and lamellipodia during spreading, displaying punctuate staining at the leading edge of plasma membrane. Studies evaluating the expression of VAMP isoforms in nonpermeabilized platelets demonstrated that a portion of VAMP 5, but not VAMPs 3, 7, or 8, resides on the extracellular face of the plasma membrane. Flow cytometry confirmed the presence of VAMP 5 on the extracellular surface of platelets. These data demonstrate that different VAMP isoforms segregate to distinct platelet granule subpopulations and subcellular locals. The colocalization of VAMPs 3 and 8 with vWF and fibrinogen is consistent with previous data demonstrating a role for these VAMP isoforms in cargo release. In contrast, granules expressing VAMP 5 or VAMP 7, which contains an actin-binding login domain, translocate to areas of cytoskeletal remodeling and may contribute membrane to growing cytoskeletal structures as the platelet spreads. These studies indicate that separate granule populations defined by expression of distinct VAMP isoforms perform different functions in platelets. Disclosures: No relevant conflicts of interest to declare.

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10

Schemenauer, Ellie. "Victims and Vamps, Madonnas and Whores." International Feminist Journal of Politics 14, no. 1 (March 2012): 83–102. http://dx.doi.org/10.1080/14616742.2011.631277.

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11

Jiwa, Fazeela. "Vamps, Heroines, Otherwise: Diasporic Women Resisting Essentialism." TOPIA: Canadian Journal of Cultural Studies 26 (November 2011): 127–44. http://dx.doi.org/10.3138/topia.26.127.

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12

Kelly-Worden, Marie, Fatimah Albrekkan, Michael Dugan, KyLeigh Harnish, Laura Gomez-Jaramillo, and Antonio Campos-Caro. "The Identification of VAMPs in B-Lymphocytes." Biophysical Journal 108, no. 2 (January 2015): 103a. http://dx.doi.org/10.1016/j.bpj.2014.11.587.

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13

Marshall, Misty R., Varsha Pattu, Mahantappa Halimani, Monika Maier-Peuschel, Martha-Lena Müller, Ute Becherer, Wanjin Hong, et al. "VAMP8-dependent fusion of recycling endosomes with the plasma membrane facilitates T lymphocyte cytotoxicity." Journal of Cell Biology 210, no. 1 (June 29, 2015): 135–51. http://dx.doi.org/10.1083/jcb.201411093.

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Cytotoxic T lymphocytes (CTLs) eliminate infected and neoplastic cells through directed release of cytotoxic granule contents. Although multiple SNARE proteins have been implicated in cytotoxic granule exocytosis, the role of vesicular SNARE proteins, i.e., vesicle-associated membrane proteins (VAMPs), remains enigmatic. VAMP8 was posited to represent the cytotoxic granule vesicular SNARE protein mediating exocytosis in mice. In primary human CTLs, however, VAMP8 colocalized with Rab11a-positive recycling endosomes. Upon stimulation, these endosomes rapidly trafficked to and fused with the plasma membrane, preceding fusion of cytotoxic granules. Knockdown of VAMP8 blocked both recycling endosome and cytotoxic granule fusion at immune synapses, without affecting activating signaling. Mechanistically, VAMP8-dependent recycling endosomes deposited syntaxin-11 at immune synapses, facilitating assembly of plasma membrane SNARE complexes for cytotoxic granule fusion. Hence, cytotoxic granule exocytosis is a sequential, multivesicle fusion process requiring VAMP8-mediated recycling endosome fusion before cytotoxic granule fusion. Our findings imply that secretory granule exocytosis pathways in other cell types may also be more complex than previously appreciated.

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14

Ren, Qiansheng, Holly Kalani Barber, Garland L. Crawford, Zubair A. Karim, Chunxia Zhao, Wangsun Choi, Cheng-Chun Wang, Wanjin Hong, and Sidney W. Whiteheart. "Endobrevin/VAMP-8 Is the Primary v-SNARE for the Platelet Release Reaction." Molecular Biology of the Cell 18, no. 1 (January 2007): 24–33. http://dx.doi.org/10.1091/mbc.e06-09-0785.

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Platelet secretion is critical to hemostasis. Release of granular cargo is mediated by soluble NSF attachment protein receptors (SNAREs), but despite consensus on t-SNAREs usage, it is unclear which Vesicle Associated Membrane Protein (VAMPs: synaptobrevin/VAMP-2, cellubrevin/VAMP-3, TI-VAMP/VAMP-7, and endobrevin/VAMP-8) is required. We demonstrate that VAMP-8 is required for release from dense core granules, alpha granules, and lysosomes. Platelets from VAMP-8−/−mice have a significant defect in agonist-induced secretion, though signaling, morphology, and cargo levels appear normal. In contrast, VAMP-2+/−, VAMP-3−/−, and VAMP-2+/−/VAMP-3−/−platelets showed no defect. Consistently, tetanus toxin had no effect on secretion from permeabilized mouse VAMP-3−/−platelets or human platelets, despite cleavage of VAMP-2 and/or -3. Tetanus toxin does block the residual release from permeabilized VAMP-8−/−platelets, suggesting a secondary role for VAMP-2 and/or -3. These data imply a ranked redundancy of v-SNARE usage in platelets and suggest that VAMP-8−/−mice will be a useful in vivo model to study platelet exocytosis in hemostasis and vascular inflammation.

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Hasan, Nazarul, Deborah Corbin, and Chuan Hu. "Fusogenic Pairings of Vesicle-Associated Membrane Proteins (VAMPs) and Plasma Membrane t-SNAREs – VAMP5 as the Exception." PLoS ONE 5, no. 12 (December 6, 2010): e14238. http://dx.doi.org/10.1371/journal.pone.0014238.

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16

De Tender, C., C. Schlundt, L. I. Devriese, T. J. Mincer, E. R. Zettler, and L. A. Amaral-Zettler. "A review of microscopy and comparative molecular-based methods to characterize “Plastisphere” communities." Analytical Methods 9, no. 14 (2017): 2132–43. http://dx.doi.org/10.1039/c7ay00260b.

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17

Che, Yong Ho, Toshihide Yamashita, and Masaya Tohyama. "Changes in mRNA for VAMPs following facial nerve transection." Journal of Chemical Neuroanatomy 24, no. 2 (July 2002): 147–52. http://dx.doi.org/10.1016/s0891-0618(02)00056-x.

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18

Wheelwright, Julie. "Revamping the vamps: When a female spy speaks out." Women: A Cultural Review 2, no. 2 (June 1991): 117–23. http://dx.doi.org/10.1080/09574049108578071.

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19

Fee, E. "Vamps Virgins and Victims: How Can Women Fight AIDS?" BMJ 313, no. 7071 (December 14, 1996): 1563. http://dx.doi.org/10.1136/bmj.313.7071.1563a.

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20

Koseoglu, Secil, Jennifer L. Fitch-Tewfik, Christian G. Peters, Lydia Danglot, Thierry Galli, and Robert C. Flaumenhaft. "VAMP-7 Interacts With The Actin Cytoskeleton To Control Platelet Spreading and Mediate α-Granule Exocytosis During Thrombus Formation." Blood 122, no. 21 (November 15, 2013): 1058. http://dx.doi.org/10.1182/blood.v122.21.1058.1058.

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Abstract Platelet granule secretion is important not only for hemostasis and thrombosis, but also for a variety of physiological processes including inflammation, angiogenesis and malignancy. Vesicle Associated Membrane Proteins (VAMPs) are a group of v-SNARE proteins resident on the platelet granule surface that participate in granule secretion. Platelets contain several VAMP isoforms including VAMP-2, VAMP-3, VAMP-7, and VAMP-8. VAMP-7 is unique in that it contains an N-terminal profilin-like longin domain. Previous work by our group demonstrated spatial segregation of granules expressing different VAMPs during platelet spreading. Granules expressing VAMP-3 and VAMP-8 localized to the granulomere of spreading platelets, while those expressing VAMP-7 moved towards the periphery. Based on this observation, we proposed that VAMP-7+ granules move to the periphery of the spreading platelet to add membrane to growing actin structures. To assess this hypothesis, platelets from VAMP-7 null mice were used to analyze the role of VAMP-7 in platelet spreading, aggregation and secretion. VAMP-7 null platelets were normal in size, shape, and number. When compared to wild-type platelets, VAMP-7 null platelets did not show any defects in aggregation upon exposure to increasing doses of the PAR4 agonist peptide, AYPGKF, or collagen. In contrast, the surface area of VAMP-7 null platelets following 15 min of spreading on poly-L-lysine was only 51% that of wild-type of platelets (P < 0.05). To assess mechanisms of the movement of VAMP-7 to the platelet periphery, the association of VAMP-7 to the Triton X-100-insoluble platelet cytoskeleton was evaluated and results showed that VAMP-7 associated with the actin cytoskeleton. Moreover, VAMP-7 null platelets showed impaired P-selectin surface expression and PF4 secretion at low concentrations of AYPGKF. TIMP-2 and VEGF localize to VAMP-7 expressing granules in the periphery of spread platelets. We therefore evaluated the secretion of TIMP-2 and VEGF from VAMP-7 null platelets. Secretion of TIMP-2 and VEGF was reduced even at saturating doses of agonist (300 mM AYPGKF). To examine the role of VAMP-7 in a-granule exocytosis during platelet activation in vivo, PF4 release was monitored following laser-induced injury of cremaster arterioles. Platelet accumulation at sites of laser injury was identical in wild-type and VAMP-7 null mice. In wild-type mice, PF4 was secreted by activated platelets and bound back to activated endothelium and platelets producing a localized concentration of PF4 that accumulated over 15 min following injury. PF4 release from platelets lacking VAMP-7 was decreased to 47% of that of control. These results demonstrate that VAMP-7 interacts with the actin cytoskeleton and functions selectively in a-granule exocytosis. VAMP-7 associates with the actin cytoskeleton and functions during platelet spreading, adding further support to the premise that membrane fusion occurring during granule secretion is an essential component of normal platelet spreading. This VAMP-7 mediated, actin-dependent mechanism of secretion is not important for platelet thrombus formation, but rather functions in the release of particular granular contents, such as PF4, at sites of vascular injury. Disclosures: No relevant conflicts of interest to declare.

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Wong, Siew Heng, Tao Zhang, Yue Xu, V. Nathan Subramaniam, Gareth Griffiths, and Wanjin Hong. "Endobrevin, a Novel Synaptobrevin/VAMP-Like Protein Preferentially Associated with the Early Endosome." Molecular Biology of the Cell 9, no. 6 (June 1998): 1549–63. http://dx.doi.org/10.1091/mbc.9.6.1549.

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Synaptobrevins/vesicle-associated membrane proteins (VAMPs) together with syntaxins and a synaptosome-associated protein of 25 kDa (SNAP-25) are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. We report here the molecular, biochemical, and cell biological characterization of a novel member of the synaptobrevin/VAMP family. The amino acid sequence of endobrevin has 32, 33, and 31% identity to those of synaptobrevin/VAMP-1, synaptobrevin/VAMP-2, and cellubrevin, respectively. Membrane fractionation studies demonstrate that endobrevin is enriched in membrane fractions that are also enriched in the asialoglycoprotein receptor. Indirect immunofluorescence microscopy establishes that endobrevin is primarily associated with the perinuclear vesicular structures of the early endocytic compartment. The preferential association of endobrevin with the early endosome was further established by electron microscopy (EM) immunogold labeling. In vitro binding assays show that endobrevin interacts with immobilized recombinant α-SNAP fused to glutathioneS-transferase (GST). Our results highlight the general importance of members of the synaptobrevin/VAMP protein family in membrane traffic and provide new avenues for future functional and mechanistic studies of this protein as well as the endocytotic pathway.

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Peters, Christian G., Alan D. Michelson, and Robert Flaumenhaft. "Granule exocytosis is required for platelet spreading: differential sorting of α-granules expressing VAMP-7." Blood 120, no. 1 (July 5, 2012): 199–206. http://dx.doi.org/10.1182/blood-2011-10-389247.

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Abstract There has been recent controversy as to whether platelet α-granules represent a single granule population or are composed of different subpopulations that serve discrete functions. To address this question, we evaluated the localization of vesicle-associated membrane proteins (VAMPs) in spread platelets to determine whether platelets actively sort a specific subpopulation of α-granules to the periphery during spreading. Immunofluorescence microscopy demonstrated that granules expressing VAMP-3 and VAMP-8 localized to the central granulomere of spread platelets along with the granule cargos von Willebrand factor and serotonin. In contrast, α-granules expressing VAMP-7 translocated to the periphery of spread platelets along with the granule cargos TIMP2 and VEFG. Time-lapse microscopy demonstrated that α-granules expressing VAMP-7 actively moved from the granulomere to the periphery during spreading. Platelets from a patient with gray platelet syndrome lacked α-granules and demonstrated only minimal spreading. Similarly, spreading was impaired in platelets obtained from Unc13dJinx mice, which are deficient in Munc13-4 and have an exocytosis defect. These studies identify a new α-granule subtype expressing VAMP-7 that moves to the periphery during spreading, supporting the premise that α-granules are heterogeneous and demonstrating that granule exocytosis is required for platelet spreading.

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23

Kuldova, Tereza. "Fashionable erotic masquerades: Of brides, gods and vamps in India." Critical Studies in Fashion & Beauty 3, no. 1 (December 1, 2012): 69–86. http://dx.doi.org/10.1386/csfb.3.1-2.69_1.

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24

Rosado, Juan A., Pedro C. Redondo, Ginés M. Salido, Stewart O. Sage, and Jose A. Pariente. "Cleavage of SNAP-25 and VAMP-2 impairs store-operated Ca2+entry in mouse pancreatic acinar cells." American Journal of Physiology-Cell Physiology 288, no. 1 (January 2005): C214—C221. http://dx.doi.org/10.1152/ajpcell.00241.2004.

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We recently reported that store-operated Ca2+entry (SOCE) in nonexcitable cells is likely to be mediated by a reversible interaction between Ca2+channels in the plasma membrane and the endoplasmic reticulum, a mechanism known as “secretion-like coupling.” As for secretion, in this model the actin cytoskeleton plays a key regulatory role. In the present study we have explored the involvement of the secretory proteins synaptosome-associated protein (SNAP-25) and vesicle-associated membrane protein (VAMP) in SOCE in pancreatic acinar cells. Cleavage of SNAP-25 and VAMPs by treatment with botulinum toxin A (BoNT A) and tetanus toxin (TeTx), respectively, effectively inhibited amylase secretion stimulated by the physiological agonist CCK-8. BoNT A significantly reduced Ca2+entry induced by store depletion using thapsigargin or CCK-8. In addition, treatment with BoNT A once SOCE had been activated reduced Ca2+influx, indicating that SNAP-25 is needed for both the activation and maintenance of SOCE in pancreatic acinar cells. VAMP-2 and VAMP-3 are expressed in mouse pancreatic acinar cells. Both proteins associate with the cytoskeleton upon Ca2+store depletion, although only VAMP-2 seems to be sensitive to TeTx. Treatment of pancreatic acinar cells with TeTx reduced the activation of SOCE without affecting its maintenance. These findings support a role for SNAP-25 and VAMP-2 in the activation of SOCE in pancreatic acinar cells and show parallels between this process and secretion in a specialized secretory cell type.

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Renard, H. F., M. D. Garcia-Castillo, V. Chambon, C. Lamaze, and L. Johannes. "Shiga toxin stimulates clathrin-independent endocytosis of the VAMP2, VAMP3 and VAMP8 SNARE proteins." Journal of Cell Science 128, no. 15 (June 12, 2015): 2891–902. http://dx.doi.org/10.1242/jcs.171116.

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Rapf, Joanna E. "DOING NOTHING: Harry Langdon and the Performance of Absence." Film Quarterly 59, no. 1 (2005): 27–35. http://dx.doi.org/10.1525/fq.2005.59.1.27.

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ABSTRACT Doing Nothing: Harry Langdon and The Performance of Absence. Where most comedians of the silent era did things, Harry Langdon's trick was to do nothing. His is a comedy of absence, surreal in its exploration of repressed desire that is perversely shown in his relationship with vamps. With long, slow takes he enacts a dark, subtle humor with contemporary resonance.

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Olson, A. L., J. B. Knight, and J. E. Pessin. "Syntaxin 4, VAMP2, and/or VAMP3/cellubrevin are functional target membrane and vesicle SNAP receptors for insulin-stimulated GLUT4 translocation in adipocytes." Molecular and Cellular Biology 17, no. 5 (May 1997): 2425–35. http://dx.doi.org/10.1128/mcb.17.5.2425.

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Introduction of the cytoplasmic domain of syntaxin 4, using either recombinant vaccinia virus or single-cell microinjection, resulted in an inhibition of insulin-stimulated GLUT4 but not GLUT1 translocation to the plasma membrane. This was specific for syntaxin 4, since neither the expression of syntaxin 3 nor the expression of a syntaxin 4 mutant in which the vesicle-associated membrane protein (VAMP) binding site was deleted had any significant effect. Consistent with the requirement for a functional VAMP binding site, expression of the cytoplasmic domains of VAMP2 or VAMP3/cellubrevin also resulted in an inhibition of insulin-stimulated GLUT4 translocation. In addition, immunoprecipitation of the expressed syntaxin 4 cytoplasmic domain resulted in an insulin-stimulated increase in the coimmunoprecipitation of GLUT4-containing vesicles. Together, these data demonstrate that syntaxin 4, VAMP2, and/or VAMP3/cellubrevin can function as target membrane and vesicle SNAP receptors, respectively, for insulin-responsive GLUT4 translocation to the plasma membrane.

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Pennuto, Maria, Dario Bonanomi, Fabio Benfenati, and Flavia Valtorta. "Synaptophysin I Controls the Targeting of VAMP2/Synaptobrevin II to Synaptic Vesicles." Molecular Biology of the Cell 14, no. 12 (December 2003): 4909–19. http://dx.doi.org/10.1091/mbc.e03-06-0380.

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Synaptic vesicle (SV) proteins are synthesized at the level of the cell body and transported down the axon in membrane precursors of SVs. To investigate the mechanisms underlying sorting of proteins to SVs, fluorescent chimeras of vesicle-associated membrane protein (VAMP) 2, its highly homologous isoform VAMP1 and synaptotagmin I (SytI) were expressed in hippocampal neurons in culture. Interestingly, the proteins displayed a diffuse component of distribution along the axon. In addition, VAMP2 was found to travel in vesicles that constitutively fuse with the plasma membrane. Coexpression of VAMP2 with synaptophysin I (SypI), a major resident of SVs, restored the correct sorting of VAMP2 to SVs. The effect of SypI on VAMP2 sorting was dose dependent, being reversed by increasing VAMP2 expression levels, and highly specific, because the sorting of the SV proteins VAMP1 and SytI was not affected by SypI. The cytoplasmic domain of VAMP2 was found to be necessary for both the formation of VAMP2-SypI hetero-dimers and for VAMP2 sorting to SVs. These data support a role for SypI in directing the correct sorting of VAMP2 in neurons and demonstrate that a direct interaction between the two proteins is required for SypI in order to exert its effect.

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MACAULAY, S. Lance, Dean R. HEWISH, Keith H. GOUGH, Violet STOICHEVSKA, Susan F. MACPHERSON, Mittur JAGADISH, and Colin W. WARD. "Functional studies in 3T3L1 cells support a role for SNARE proteins in insulin stimulation of GLUT4 translocation." Biochemical Journal 324, no. 1 (May 15, 1997): 217–24. http://dx.doi.org/10.1042/bj3240217.

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Insulin stimulation of glucose transport in the major insulin-responsive tissues results predominantly from the translocation to the cell surface of a particular glucose transporter isoform, GLUT4, residing normally under basal conditions in intracellular vesicular structures. Recent studies have identified the presence of vesicle-associated membrane protein (VAMP) 2, a protein involved in vesicular trafficking in secretory cell types, in the vesicles of insulin-sensitive cells that contain GLUT4. The plasma membranes of insulin-responsive cells have also been shown to contain syntaxin 4 and the 25 kDa synaptosome-associated protein (SNAP-25), two proteins that form a complex with VAMP 2. The potential functional involvement of VAMP 2, SNAP-25 and syntaxin 4 in the trafficking of GLUT4 was assessed in the present study by determining the effect on GLUT4 translocation of microinjection of toxins that specifically cleave VAMPs or SNAP-25, or microinjection of specific peptides from VAMP 2 and syntaxin 4. Microinjection of tetanus toxin light chain or botulinum D toxin light chain resulted in an 80 and 61% inhibition respectively of insulin stimulation of GLUT4 translocation in 3T3L1 cells assessed using the plasma-membrane lawn assay. Botulinum A toxin light chain, which cleaves SNAP-25, was without effect. Microinjection of an N-terminal VAMP 2 peptide (residues 1–26) inhibited insulin stimulation of GLUT4 translocation by 54%. A syntaxin 4 peptide (residues 106–122) inhibited insulin stimulation of GLUT4 translocation by 40% whereas a syntaxin 1c peptide (residues 226–260) was without effect. These data taken together strongly suggest a role for VAMP 2 in GLUT4 trafficking and also for syntaxin 4. They further indicate that the isoforms of SNAP-25 isolated to date that are sensitive to cleavage by botulinum A toxin light chain do not appear to be involved in GLUT4 translocation.

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Somerville, Kristine. "Enemy of Men: The Vamps, Ice Princesses and Flappers of the Silent Screens." Missouri Review 37, no. 2 (2014): 77–94. http://dx.doi.org/10.1353/mis.2014.0032.

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Kokkola, Lydia. "Virtuous Vampires and Voluptuous Vamps: Romance Conventions Reconsidered in Stephenie Meyer’s “Twilight” Series." Children's Literature in Education 42, no. 2 (December 18, 2010): 165–79. http://dx.doi.org/10.1007/s10583-010-9125-9.

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Volchuk, A., Y. Mitsumoto, L. He, Z. Liu, E. Habermann, W. Trimble, and A. Klip. "Expression of vesicle-associated membrane protein 2 (VAMP-2)/synaptobrevin II and cellubrevin in rat skeletal muscle and in a muscle cell line." Biochemical Journal 304, no. 1 (November 15, 1994): 139–45. http://dx.doi.org/10.1042/bj3040139.

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Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and cellubrevin, in skeletal muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal muscle and the muscle cell line also expressed cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain cells. Both VAMP-2 and cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature muscle or muscle cells in culture. Interestingly, both VAMP-2 and cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated muscle cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and cellubrevin, but not of VAMP-1, in both skeletal muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and cellubrevin are expressed in skeletal muscle cells and may each participate in specific processes of intracellular membrane traffic.

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Randhawa, Varinder K., Farah S. L. Thong, Dawn Y. Lim, Dailin Li, Rami R. Garg, Rachel Rudge, Thierry Galli, Assaf Rudich, and Amira Klip. "Insulin and Hypertonicity Recruit GLUT4 to the Plasma Membrane of Muscle Cells by Using N-Ethylmaleimide-sensitive Factor-dependent SNARE Mechanisms but Different v-SNAREs: Role of TI-VAMP." Molecular Biology of the Cell 15, no. 12 (December 2004): 5565–73. http://dx.doi.org/10.1091/mbc.e04-03-0266.

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Insulin and hypertonicity each increase the content of GLUT4 glucose transporters at the surface of muscle cells. Insulin enhances GLUT4 exocytosis without diminishing its endocytosis. The insulin but not the hypertonicity response is reduced by tetanus neurotoxin, which cleaves vesicle-associated membrane protein (VAMP)2 and VAMP3, and is rescued upon introducing tetanus neurotoxin-resistant VAMP2. Here, we show that hypertonicity enhances GLUT4 recycling, compounding its previously shown ability to reduce GLUT4 endocytosis. To examine whether the canonical soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) mechanism is required for the plasma membrane fusion of the tetanus neurotoxin-insensitive GLUT4 vesicles, L6 myoblasts stably expressing myc-tagged GLUT4 (GLUT4myc) were transiently transfected with dominant negative N-ethylmaleimide-sensitive factor (NSF) (DN-NSF) or small-interfering RNA to tetanus neurotoxin-insensitive VAMP (TI-VAMP siRNA). Both strategies markedly reduced the basal level of surface GLUT4myc and the surface gain of GLUT4myc in response to hypertonicity. The insulin effect was abolished by DN-NSF, but only partly reduced by TI-VAMP siRNA. We propose that insulin and hypertonicity recruit GLUT4myc from partly overlapping, but distinct sources defined by VAMP2 and TI-VAMP, respectively.

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de Paola, Matilde, Facundo Garrido, María N. Zanetti, and Marcela Alejandra Michaut. "VAMPs sensitive to tetanus toxin are required for cortical granule exocytosis in mouse oocytes." Experimental Cell Research 405, no. 1 (August 2021): 112629. http://dx.doi.org/10.1016/j.yexcr.2021.112629.

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35

Garipova Castellano, Nailya. "Women in Nabokov’s Russian novels." Revista Alicantina de Estudios Ingleses, no. 27 (November 15, 2014): 61. http://dx.doi.org/10.14198/raei.2014.27.04.

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This article examines the presence of female characters in the Nabokov’s novels of the Russian period (1925-1939). There is a pattern in the use of female characters that illuminates the novels studied. It clarifies our understanding of Nabokov’s literary techniques and contributes to the comprehension of two major themes seen in all his works: the passionate yearning for his beloved Russia and the satiric perception of an imperfect world. Thus, two categories of Nabokov’s women can be distinguished: the bearers of the Russian culture and the unfaithful vamps. The so called bearers of the Russian culture, presented and described in a positive way, function as guiding stars for their lovers: they help them to survive in the hostile surroundings of their exile. These characters represent the nature of the Russian womanhood; they are kind, tender, pure and supportive, and at the same time they are strong and powerful. Their descriptions allude to the heroines of the Russian literature and they share the author’s passion for the Russian literature and culture. The so called unfaithful vamps represent the world of the poshlost’, vulgarity and deceit. These female characters have common characteristics that make them unpleasant: they are ignorant in the world of art and literature, and they are greedy owners representing passion and lust. After this classification of Nabokov’s women we see that his two main modes of presenting female characters reflect his two major themes: they function as the personification of the lost paradise of the past Russia and as an embodiment of human fallibility and weakness.

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36

de Lerma, Dominique-Rene, Noel Da Costa, Per Brevig, Max Pollikoff, Evalyn Steinbock, Wanda Maximilien, and David Garvey. "Four Preludes for Trombone and Piano, 1973. Jes' Grew, 1973. Five Verses with Vamps, 1969." Black Perspective in Music 13, no. 2 (1985): 234. http://dx.doi.org/10.2307/1214590.

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37

Ralston, E., S. Beushausen, and T. Ploug. "Expression of the synaptic vesicle proteins VAMPs/synaptobrevins 1 and 2 in non-neural tissues." Journal of Biological Chemistry 269, no. 22 (June 1994): 15403–6. http://dx.doi.org/10.1016/s0021-9258(17)40690-9.

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38

Rothe, Eugenio. "Vampires and Vamps: The Use of a Popular Metaphor in the Psychodynamic Understanding of Adolescent Conflict." Adolescent Psychiatry 3, no. 3 (August 1, 2013): 260–68. http://dx.doi.org/10.2174/2210676611303030007.

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39

Redondo, Pedro C., Alan G. S. Harper, Ginés M. Salido, Jose A. Pariente, Stewart O. Sage, and Juan A. Rosado. "A role for SNAP-25 but not VAMPs in store-mediated Ca2+entry in human platelets." Journal of Physiology 558, no. 1 (June 24, 2004): 99–109. http://dx.doi.org/10.1113/jphysiol.2004.064899.

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40

Randhawa, Varinder K., Philip J. Bilan, Zayna A. Khayat, Nicholas Daneman, Zhi Liu, Toolsie Ramlal, Allen Volchuk, et al. "VAMP2, but Not VAMP3/Cellubrevin, Mediates Insulin-dependent Incorporation of GLUT4 into the Plasma Membrane of L6 Myoblasts." Molecular Biology of the Cell 11, no. 7 (July 2000): 2403–17. http://dx.doi.org/10.1091/mbc.11.7.2403.

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Like neuronal synaptic vesicles, intracellular GLUT4-containing vesicles must dock and fuse with the plasma membrane, thereby facilitating insulin-regulated glucose uptake into muscle and fat cells. GLUT4 colocalizes in part with the vesicle SNAREs VAMP2 and VAMP3. In this study, we used a single-cell fluorescence-based assay to compare the functional involvement of VAMP2 and VAMP3 in GLUT4 translocation. Transient transfection of proteolytically active tetanus toxin light chain cleaved both VAMP2 and VAMP3 proteins in L6 myoblasts stably expressing exofacially myc-tagged GLUT4 protein and inhibited insulin-stimulated GLUT4 translocation. Tetanus toxin also caused accumulation of the remaining C-terminal VAMP2 and VAMP3 portions in Golgi elements. This behavior was exclusive to these proteins, because the localization of intracellular myc-tagged GLUT4 protein was not affected by the toxin. Upon cotransfection of tetanus toxin with individual vesicle SNARE constructs, only toxin-resistant VAMP2 rescued the inhibition of insulin-dependent GLUT4 translocation by tetanus toxin. Moreover, insulin caused a cortical actin filament reorganization in which GLUT4 and VAMP2, but not VAMP3, were clustered. We propose that VAMP2 is a resident protein of the insulin-sensitive GLUT4 compartment and that the integrity of this protein is required for GLUT4 vesicle incorporation into the cell surface in response to insulin.

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Prekeris, Rytis, Bin Yang, Viola Oorschot, Judith Klumperman, and Richard H. Scheller. "Differential Roles of Syntaxin 7 and Syntaxin 8 in Endosomal Trafficking." Molecular Biology of the Cell 10, no. 11 (November 1999): 3891–908. http://dx.doi.org/10.1091/mbc.10.11.3891.

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To understand molecular mechanisms that regulate the intricate and dynamic organization of the endosomal compartment, it is important to establish the morphology, molecular composition, and functions of the different organelles involved in endosomal trafficking. Syntaxins and vesicle-associated membrane protein (VAMP) families, also known as soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptors (SNAREs), have been implicated in mediating membrane fusion and may play a role in determining the specificity of vesicular trafficking. Although several SNAREs, including VAMP3/cellubrevin, VAMP8/endobrevin, syntaxin 13, and syntaxin 7, have been localized to the endosomal membranes, their precise localization, biochemical interactions, and function remain unclear. Furthermore, little is known about SNAREs involved in lysosomal trafficking. So far, only one SNARE, VAMP7, has been localized to late endosomes (LEs), where it is proposed to mediate trafficking of epidermal growth factor receptor to LEs and lysosomes. Here we characterize the localization and function of two additional endosomal syntaxins, syntaxins 7 and 8, and propose that they mediate distinct steps of endosomal protein trafficking. Both syntaxins are found in SNARE complexes that are dissociated by α-soluble NSF attachment protein and NSF. Syntaxin 7 is mainly localized to vacuolar early endosomes (EEs) and may be involved in protein trafficking from the plasma membrane to the EE as well as in homotypic fusion of endocytic organelles. In contrast, syntaxin 8 is likely to function in clathrin-independent vesicular transport and membrane fusion events necessary for protein transport from EEs to LEs.

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Pegrum, Mark. "Virgins, Vixens, Vamps and Victims: François Ozon's 8 Femmes and the sexual (sub-)texts of French popular culture." Australian Journal of French Studies 42, no. 1 (January 2005): 76–93. http://dx.doi.org/10.3828/ajfs.42.1.76.

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43

Rapport, Evan. "Hearing punk as blues." Popular Music 33, no. 1 (January 2014): 39–67. http://dx.doi.org/10.1017/s0261143013000524.

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AbstractPunk is an extreme manifestation of the rock project, meaning that it depends on an association of raw and authentic expression with blackness, musically represented by particular approaches to the blues, combined with processes of white appropriation, transformation and obfuscation of those blues resources. Punk's powerful affect largely derives from the tension between punk's blues foundations and strategies that obscure its roots. Punk treatments and transformations of the blues include: (1) moving from multi-part, three-chord harmonic schemes to riffs and one- and two-chord vamps; (2) taking a new approach to vocal performance styles; and (3) retaining certain melodic approaches, such as the use of pentatonic scales and monophonic textures. Punk's complex relationship to the blues, including the history of negation and erasure, continues to be a central part of the punk aesthetic.

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Fader, Claudio Marcelo, Diego Germán Sánchez, María Belén Mestre, and María Isabel Colombo. "TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1793, no. 12 (December 2009): 1901–16. http://dx.doi.org/10.1016/j.bbamcr.2009.09.011.

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45

Grochala, Sarah. "Vamps, Vixens, and Feminists: Report on the Sphinx Conference held at the National Theatre, London, on 16 June 2009." New Theatre Quarterly 25, no. 3 (August 2009): 290. http://dx.doi.org/10.1017/s0266464x09000463.

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46

Flaumenhaft, Robert C., Alan D. Michelson, and Christian G. Peters. "Platelet Spreading Requires Exocytosis of a Subpopulation of α-Granules Expressing VAMP-7,." Blood 118, no. 21 (November 18, 2011): 3248. http://dx.doi.org/10.1182/blood.v118.21.3248.3248.

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Abstract Abstract 3248 There has been recent controversy as to whether platelet α-granules represent a single, homogenous granule population or are composed of different subpopulations that contain different cargos and serve discrete functions. To evaluate this question, we have studied granule movement in spreading platelets. During platelet spreading, the majority of dense and α-granules coalesce in the central granulomere. However, some granules are observed in the platelet periphery. We evaluated whether platelets actively sort a specific subpopulation of α-granules to the periphery during spreading. Granules in spread platelets were stained with antibodies directed at vesicle-associated membrane proteins (VAMPs) −3, −7, and −8. We and others have shown that VAMP-3 and −8 function in granule exocytosis. VAMP-7 contains a profilin-like N-terminal extension capable of interacting with Arp2/3. Samples were imaged using confocal microscopy. Quantitative evaluation of antibody staining in the granulomere vs. the periphery demonstrated that 93+/−7% of VAMP-8, 86+/−14% of von Willebrand factor (an α-granule cargo), and 93+/−7% of serotonin (a dense granule cargo) localized to the central granulomere. In contrast, 77+/−8% of VAMP-7 localized to the periphery. To determine whether a VAMP-7+ α-granule subpopulation actively moves from the granulomere to the platelet periphery during spreading, we loaded platelet α-granules with Qdot 565 nanocrystals and performed time-lapse video microscopy of single platelets. While the majority of endocytosed nanocrystals remained in the central granulomere during spreading, a subpopulation of labeled granules actively moved from the granulomere towards the growing edge at the platelet periphery. Colocalization studies demonstrated that 73% of peripheral Qdot 565 nanocrystals colocalized with VAMP-7. Furthermore, 82% of granules expressing VAMP-7 colocalized with P-selectin (specific for α-granules). These results indicate that a subpopulation of VAMP-7+ α-granules actively moves to the platelet periphery during spreading. To determine whether α-granules are required for spreading, we evaluated spreading in platelets from a patient with gray platelet syndrome (GPS, a congenital absence of α-granules). Platelet surface area increased 4-fold with spreading in normal controls. In contrast, the increase in surface area of GPS platelets following plating for 15 min was minimal – suggesting that α-granules are required for platelet spreading. We also evaluated spreading in murine Jinx platelets, which lack functional Munc13-4. These platelets demonstrate normal morphology and intact proximal signaling, but have a severe granule exocytosis defect. Total surface area of Munc13-4 deficient platelets spread for 15 min was 47+/−3% that of wild-type controls. Platelet spreading was also evaluated using a grated optical biosensor capable of detecting membrane contact with its surface in real time. This technique showed that spreading was decreased in Munc13-4 deficient platelets to 48+/−17% of controls. These results identify a new α-granule subtype that expresses VAMP-7 and is required for platelet spreading. This observation supports the premise that α-granules are heterogeneous and demonstrates that different VAMP isoforms localize to functionally discrete α-granule subpopulations. Disclosures: Michelson: GLSynthesis: Research Funding; Lilly/Daiichi Sankyo: Data Monitoring Committee for clinical trial, Research Funding; Takeda: Research Funding.

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BUXTON, Penelope, Xiang-Ming ZHANG, Bong WALSH, Absorn SRIRATANA, Irina SCHENBERG, Elizabeth MANICKAM, and Tony ROWE. "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells." Biochemical Journal 375, no. 2 (October 15, 2003): 433–40. http://dx.doi.org/10.1042/bj20030427.

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Members of the SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) superfamily [syntaxins, VAMPs (vesicle-associated membrane proteins) and SNAP25 (synaptosome-associated protein-25)-related proteins] are required for intracellular membrane-fusion events in eukaryotes. In neurons, assembly of SNARE core complexes comprising the presynaptic membrane-associated SNAREs syntaxin 1 and SNAP25, and the vesicle-associated SNARE VAMP2, is necessary for synaptic vesicle exocytosis. Several accessory factors have been described that associate with the synaptic SNAREs and modulate core complex assembly or mediate Ca2+ regulation. One such factor, Snapin, has been reported to be a brain-specific protein that interacts with SNAP25, and regulates association of the putative Ca2+-sensor synaptotagmin with the synaptic SNARE complex [Ilardi, Mochida and Sheng (1999) Nat. Neurosci. 2, 119–124]. Here we demonstrate that Snapin is expressed ubiquitously in neuronal and non-neuronal cells. Furthermore, using protein–protein-interaction assays we show that Snapin interacts with SNAP23, the widely expressed homologue of SNAP25, and that the predicted C-terminal helical domain of Snapin contains the SNAP23-binding site. Subcellular localization experiments revealed that Snapin is a soluble protein that exists in both cytosolic and peripheral membrane-bound pools in adipocytes. Moreover, association of Snapin with the plasma membrane was detected in cells overexpressing a Snapin–green fluorescent protein fusion protein. Finally, we show that Snapin is able to form a ternary complex with SNAP23 and syntaxin 4, suggesting that it is a component of non-neuronal SNARE complexes. An important implication of our results is that Snapin is likely to perform a general role in SNARE-mediated vesicle fusion events in non-neuronal cells in addition to its participation in Ca2+-regulated neurosecretion.

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Fox, Jesse, and Jeremy N. Bailenson. "Virtual Virgins and Vamps: The Effects of Exposure to Female Characters’ Sexualized Appearance and Gaze in an Immersive Virtual Environment." Sex Roles 61, no. 3-4 (June 12, 2009): 147–57. http://dx.doi.org/10.1007/s11199-009-9599-3.

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Clancy, Fiona. "Motherhood in crisis in Lucrecia Martel’s Salta Trilogy." Alphaville: Journal of Film and Screen Media, no. 10 (December 16, 2015): 64–75. http://dx.doi.org/10.33178/alpha.10.04.

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This article concerns the complex negotiation of ageing and femininity in Amy Heckerling’s two most recent films: I Could Never Be Your Woman (2007) and Vamps (2012). These films are positioned as part of the contemporary postfeminist media culture, (Gill, 2007) noting the scrutiny received by the ageing female body, and its changing status under the prevailing cultural norms of femininity. However, Heckerling’s films also demonstrate a sense of play with these gender norms, and so calls to be read also in terms of Judith Butler’s theorisation of performativity (1990; 1993; 2004). This article contends that Heckerling’s representation of liminality and indeterminacy—in her teen movies, and later work alike—provides a way for women to carve out an autonomous identity that humorously demonstrates the absurdity of mediatised constructions of femininity. Her work, then, is more complex than has hitherto been acknowledged, and the piece concludes by calling for the director and screenwriter to be repositioned as a significant female voice in 21st century screen media.

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50

Sebastian, Mrinalini. "Vamps and Villains or Citizen-Subjects? Converting a Third-Person Self-Conception of the Indian Christians into a First-Person Narrative." Studies in World Christianity 16, no. 2 (July 2010): 109–25. http://dx.doi.org/10.3366/swc.2010.0001.

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This article examines the historical factors that gave rise to stereotypes about Christians as aliens who are estranged from the ways of the dominant culture. On the basis of an analysis of the use of stereotypes about Christians in a renowned novel by the Kannada writer Kuvempu it argues that such articulations shape the persistent view that Christians represent Western culture and values. Internalisation of this third-person perspective by the Indian Christians has obstructed a clear articulation of their self-perception as a minority group in a multi-religious context. This article will argue that it is important for the Christian minority to develop a first-person narrative that is neither defensive nor passive.

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