Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion

Polgár, János; Chung, Sul Hee; Reed, Guy L.

doi:10.1182/blood.v100.3.1081

Cited by 146 publications

(154 citation statements)

References 14 publications

Supporting

Mentioning

149

Contrasting

Order By: Relevance

“…VAMP3 binds to plasma membrane t-SNAREs syntaxin1, syntaxin4, SNAP-23 and SNAP-25 [22,29,30,34]. Using the cell fusion assay in the current study, we examined the membrane fusion capacity of the ternary complexes formed by VAMP3 and the plasma membrane t-SNAREs.…”

Section: Resultsmentioning

confidence: 99%

“…It has been implicated in recycling of transferrin receptors to the plasma membrane [19], secretion of α-granules in platelets [21,22], recycling of T-cell receptors to the immunological synapses [23], and membrane trafficking during cell migration [24,25]. Using a cell fusion assay, we functionally examined the membrane fusion capacity of the ternary complexes formed by VAMP3 and plasma membrane t-SNAREs, syntaxin1, syntaxin4, SNAP-23 and SNAP-25.…”

Section: Discussionmentioning

confidence: 99%

“…VAMP3 forms complexes with syntaxin1, syntaxin4, SNAP-23 and SNAP-25 [29][30][31]. It has been reported that VAMP3 forms ternary complexes with syntaxin4/SNAP-25 [22] and syntaxin4/SNAP-23 [34]. Therefore, biochemically VAMP3 can form ternary complexes with t-SNARE complexes syntaxin1/SNAP-25, syntaxin1/SNAP-23, syntaxin4/SNAP-25 and syntaxin4/SNAP-23.…”

Section: Discussionmentioning

confidence: 99%

“…It colocalizes with endocytosed transferrin receptors [18] and the glucose transporter GLUT4 in adipocytes [20], and is also present in α-granules in platelets [21]. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane [19], secretion of α-granules in platelets [21,22], recycling of T-cell receptors to the immunological synapses [23], and membrane trafficking during cell migration [24,25]. Surprisingly, VAMP3 knockout mice have no obvious phenotype [26,27], which likely results from compensation by VAMP2 [28] and/or other v-SNARE proteins.…”

Section: Introductionmentioning

confidence: 99%

“…Syntaxin4 is a homologue of syntaxin1, whereas SNAP-23 is a homologue of SNAP-25 [32,33]. It has also been reported that VAMP3 forms ternary complexes with syntaxin4/SNAP-25 [22] and syntaxin4/SNAP-23 [34]. To fully understand VAMP3-mediated vesicle fusion, functional studies are needed to examine the membrane fusion capacity of the ternary complexes formed by VAMP3 and the plasma membrane t-SNAREs.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Membrane fusion by VAMP3 and plasma membrane t-SNAREs

Hardee

Minnear

2007

Experimental Cell Research

View full text Add to dashboard Cite

Pairing of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins on vesicles (v-SNAREs) and SNARE proteins on target membranes (t-SNAREs) mediates intracellular membrane fusion. VAMP3/cellubrevin is a v-SNARE that resides in recycling endosomes and endosome-derived transport vesicles. VAMP3 has been implicated in recycling of transferrin receptors, secretion of α-granules in platelets, and membrane trafficking during cell migration. Using a cell fusion assay, we examined membrane fusion capacity of the ternary complexes formed by VAMP3 and plasma membrane t-SNAREs syntaxin1, syntaxin4, SNAP-23 and SNAP-25. VAMP3 forms fusogenic pairing with t-SNARE complexes syntaxin1/SNAP-25, syntaxin1/SNAP-23 and syntaxin4/SNAP-25, but not with syntaxin4/SNAP-23. Deletion of the Nterminal domain of syntaxin4 enhanced membrane fusion more than two fold, indicating that the Nterminal domain negatively regulates membrane fusion. Differential membrane fusion capacities of the ternary v-/t-SNARE complexes suggest that transport vesicles containing VAMP3 have distinct membrane fusion kinetics with domains of the plasma membrane that present different t-SNARE proteins.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Membrane fusion by VAMP3 and plasma membrane t-SNAREs

Hardee

Minnear

2007

Experimental Cell Research

View full text Add to dashboard Cite

show abstract

Deletion of chromosome 1p36 is associated with periventricular nodular heterotopia

Neal

Apse

Şahin

et al. 2006

American J of Med Genetics Pt A

View full text Add to dashboard Cite

Use of chitosan for removal of bisphenol A and bisphenol derivatives through tyrosinase‐catalyzed quinone oxidation

Suzuki¹,

Sugiyama²,

Musashi³

et al. 2010

J of Applied Polymer Sci

View full text Add to dashboard Cite

In this study, the availability of chitosan was systematically investigated for removal of bisphenol A (BPA, 2,2-bis(hydroxyphenyl)propane) through the tyrosinase-catalyzed quinone oxidation and subsequent quinone adsorption on chitosan beads. In particular, the process parameters, such as the hydrogen peroxide (H 2 O 2 )-to-BPA ratio, pH value, temperature, and tyrosinase dose, were discussed in detail for the enzymatic quinone oxidation. Tyrosinase-catalyzed quinone oxidation of BPA was effectively enhanced by adding H 2 O 2 and the optimum conditions for BPA at 0.3 mM were determined to be pH 7.0 and 40 C in the presence of H 2 O 2 at 0.3 mM ([H 2 O 2 ]/[BPA] ¼ 1.0). Removal of BPA from aqueous solutions was accomplished by adsorption of enzymatically generated quinone derivatives on chitosan beads. The use of chitosan in the form of beads was found to be more effective because heterogeneous removal of BPA with chitosan beads was much faster than homogeneous removal of BPA with chitosan solutions, and the removal efficiency was enhanced by increasing the amount of chitosan beads dispersed in the BPA solutions and BPA was completely removed by quinone adsorption in the presence of chitosan beads more than 0.10 cm 3 /cm 3 . In addition, a variety of bisphenol derivatives were completely or effectively removed by the procedure constructed in this study, although the enzyme dose or the amount of chitosan beads was further increased as necessary for some of the bisphenol derivatives used.

show abstract

Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion

Abstract: Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion

Cited by 146 publications

References 14 publications

Membrane fusion by VAMP3 and plasma membrane t-SNAREs

Membrane fusion by VAMP3 and plasma membrane t-SNAREs

Deletion of chromosome 1p36 is associated with periventricular nodular heterotopia

Use of chitosan for removal of bisphenol A and bisphenol derivatives through tyrosinase‐catalyzed quinone oxidation

Contact Info

Product

Resources

About