Two Distinct Modes of Exocytotic Fusion Pore Expansion in Large Astrocytic Vesicles

Peng, Hong; Kang, Ning; Xu, Jun; Stanton, Patric K.; Kang, Jian

doi:10.1074/jbc.m113.468231

Cited by 4 publications

(5 citation statements)

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“…To confirm the effect of fendiline on endosomal vesicle formation and sorting, Panc1 cells were stained with FM1-43FX, a membrane probe for activity-dependent vesicle cycling [ 60 ]. Fluorescence microscopy of cells incubated with FM1-43FX and treated with fendiline for 6h showed a significant increase in the number and size of FM1-43 positive intracellular vesicles (Figure 7G and 7H ).…”

Section: Resultsmentioning

confidence: 99%

Fendiline inhibits proliferation and invasion of pancreatic cancer cells by interfering with ADAM10 activation and β-catenin signaling

et al. 2015

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Section: Resultsmentioning

confidence: 99%

Fendiline inhibits proliferation and invasion of pancreatic cancer cells by interfering with ADAM10 activation and β-catenin signaling

et al. 2015

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“…The current model of the platelet secretory process considers that a crucial step in exocytotic secretion is fusion of the membranes of secretory granules with the membranes of the open canalicular system (OCS)/plasma membrane (Lemons et al, 1997;Sudhof & Rothman, 2009;Fang & Lindau, 2014;Mellander et al, 2014). It is also recognized that in platelets, membrane fusion is mediated by the assembly of the SNARE (Soluble N-ethylmaleimide-sensitive factor Attachment protein REceptor) complex (Sudhof & Rothman, 2009;Peng et al, 2013). However, the central role of SNARE proteins in platelet secretion is still not certain (Golembiewska & Poole, 2015).…”

Section: Discussionmentioning

confidence: 99%

Aquaporins in human platelets: intracellular localization and possible role in granule and lysosome secretion

Misztal¹,

Rusak²,

Brańska-Januszewska³

et al. 2018

Acta Biochim Pol

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This study was undertaken to establish the presence and the role of aquaporins (AQPs) in human platelets. Immunodetection with polyclonal antibodies and fluorescent microscopy suggest the presence of AQP isoforms – 0–7 and 9–12 – localized (in resting platelets) in the plasma membrane and in the dense and alpha granules. In thrombin- or monensin-treated platelets, the granules’ AQPs become visible in the whole cell body, indicating the granules’ swelling. In our studies on the role of AQPs in platelet responses we used tetrachloroauric acid (HAuCl4), a classical water channel blocker. We found that 10–100 µM of Au(III) inhibited the hypotonicity-, monensin (simulating the action of Na+/H+ exchanger)-, and collagen-evoked platelet swelling and reduced tritiated water uptake by platelets treated by collagen or monensin, indicating its ability to block water channels in these cells. HAuCl4, at the concentrations reducing water influx, did not induce cell lysis, alter the plasma membrane shape or the –SH group content. The inhibitor also failed to affect Na+ and Cl--related osmotic gradient formation and protein kinase D2 phosphorylation. In platelets activated by threshold concentrations of collagen, the thrombin receptor activating peptide, ADP, calcium ionophore A23187, phorbol ester and arachidonic acid, HAuCl4 (100 µM) completely inhibited secretion of ATP from dense granules but failed to reduce platelet aggregation. In collagen-stimulated platelets, HAuCl4 (10–100 µM) reduced secretion from dense and alpha granules, as well as lysosomes, in a dose-dependent manner. We conclude that human platelets possess numerous AQPs subtypes localized in the plasma and granule membranes. AQP-mediated water fluxes may be crucial for platelet volume regulation as well as secretion from dense and alpha granules and lysosomes.

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“…From such studies in cultured astrocytes, the size of the vesicles is estimated to vary between ϳ30 -50 nm (43) and Ͼ300 nm (64,248). Even VGLUT-positive vesicles of several microns have been found in brain slice astrocytes, but these are produced by stimulating the astrocytes either mechanically or with high glutamate concentrations (184,326,445), suggesting that these vesicles are involved in release of gliotransmitters in pathological conditions. Moreover, localization studies have suggested that the three vesicular glutamate transporters, VGLUT1, VGLUT2, and VGLUT3, as well as the vesicular ATP transporter VNUT are all present in astrocytes.…”

Section: Vesicular Transportersmentioning

confidence: 99%

Neuroglial Transmission

Gundersen

Storm‐Mathisen

Bergersen

2015

Physiological Reviews

155

113

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Neuroglia, the "glue" that fills the space between neurons in the central nervous system, takes active part in nerve cell signaling. Neuroglial cells, astroglia, oligodendroglia, and microglia, are together about as numerous as neurons in the brain as a whole, and in the cerebral cortex grey matter, but the proportion varies widely among brain regions. Glial volume, however, is less than one-fifth of the tissue volume in grey matter. When stimulated by neurons or other cells, neuroglial cells release gliotransmitters by exocytosis, similar to neurotransmitter release from nerve endings, or by carrier-mediated transport or channel flux through the plasma membrane. Gliotransmitters include the common neurotransmitters glutamate and GABA, the nonstandard amino acid d-serine, the high-energy phosphate ATP, and l-lactate. The latter molecule is a "buffer" between glycolytic and oxidative metabolism as well as a signaling substance recently shown to act on specific lactate receptors in the brain. Complementing neurotransmission at a synapse, neuroglial transmission often implies diffusion of the transmitter over a longer distance and concurs with the concept of volume transmission. Transmission from glia modulates synaptic neurotransmission based on energetic and other local conditions in a volume of tissue surrounding the individual synapse. Neuroglial transmission appears to contribute significantly to brain functions such as memory, as well as to prevalent neuropathologies.

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Two Distinct Modes of Exocytotic Fusion Pore Expansion in Large Astrocytic Vesicles

Cited by 4 publications

References 50 publications

Fendiline inhibits proliferation and invasion of pancreatic cancer cells by interfering with ADAM10 activation and β-catenin signaling

Fendiline inhibits proliferation and invasion of pancreatic cancer cells by interfering with ADAM10 activation and β-catenin signaling

Aquaporins in human platelets: intracellular localization and possible role in granule and lysosome secretion

Neuroglial Transmission

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