scholarly journals Phospholipase D1 Production of Phosphatidic Acid at the Plasma Membrane Promotes Exocytosis of Large Dense-core Granules at a Late Stage

2007 ◽  
Vol 282 (30) ◽  
pp. 21746-21757 ◽  
Author(s):  
Maria Zeniou-Meyer ◽  
Naama Zabari ◽  
Uri Ashery ◽  
Sylvette Chasserot-Golaz ◽  
Anne-Marie Haeberlé ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Phosphatidic Acid ◽  
Late Stage ◽  
Dense Core ◽  
Phospholipase D1 ◽  
Dense Core Granules

scholarly journals Phospholipase D1‐induced phosphatidic acid at the plasma membrane promotes a late stage of large dense‐core

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Nicolas Vitale ◽  
Maria Zeniou‐Meyer ◽  
Sylvette Chasserot‐Golaz ◽  
Yannick Bailly ◽  
Marie‐France Bader
Keyword(s):  
Plasma Membrane ◽  
Phosphatidic Acid ◽  
Late Stage ◽  
Dense Core ◽  
Phospholipase D1

scholarly journals A Complex Web of Signal-dependent Trafficking Underlies the Triorganellar Distribution of P-Selectin in Neuroendocrine PC12 Cells

1999 ◽  
Vol 145 (7) ◽  
pp. 1419-1433 ◽  
Author(s):  
Anastasiya D. Blagoveshchenskaya ◽  
Eric W. Hewitt ◽  
Daniel F. Cutler
Keyword(s):  
Plasma Membrane ◽  
Horseradish Peroxidase ◽  
Pc12 Cells ◽  
Brefeldin A ◽  
Dense Core ◽  
Concomitant Increase ◽  
Targeting Signal ◽  
Lysosomal Targeting ◽  
Dense Core Granules ◽  
Lumenal Domain

By analyzing the trafficking of HRP–P-selectin chimeras in which the lumenal domain of P-selectin was replaced with horseradish peroxidase, we determined the sequences needed for targeting to synaptic-like microvesicles (SLMV), dense core granules (DCG), and lysosomes in neuroendocrine PC12 cells. Within the cytoplasmic domain of P-selectin, Tyr777 is needed for the appearance of P-selectin in immature and mature DCG, as well as for targeting to SLMV. The latter destination also requires additional sequences (Leu768 and 786DPSP789) which are responsible for movement through endosomes en route to the SLMV. Leu768 also mediates transfer from early transferrin (Trn)-positive endosomes to the lysosomes; i.e., operates as a lysosomal targeting signal. Furthermore, SLMV targeting of HRP–P-selectin chimeras, but not the endogenous SLMV protein synaptophysin/p38, previously shown to be delivered to SLMV directly from the plasma membrane, is a Brefeldin A–sensitive process. Together, these data are consistent with a model of SLMV biogenesis which involves an endosomal intermediate in PC12 cells. In addition, we have discovered that impairment of SLMV or DCG targeting results in a concomitant increase in lysosomal delivery, illustrating the entwined relationships between routes leading to regulated secretory organelles (RSO) and to lysosomes.

Requirements for the identification of dense-core granules

2004 ◽  
Vol 14 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Jacopo Meldolesi ◽  
Evelina Chieregatti ◽  
Maria Luisa Malosio
Keyword(s):  
Dense Core ◽  
Dense Core Granules

scholarly journals Synaptotagmin VII Is Targeted to Dense-core Vesicles and Regulates Their Ca2+-dependent Exocytosis in PC12 Cells

2004 ◽  
Vol 279 (50) ◽  
pp. 52677-52684 ◽  
Author(s):  
Mitsunori Fukuda ◽  
Eiko Kanno ◽  
Megumi Satoh ◽  
Chika Saegusa ◽  
Akitsugu Yamamoto
Keyword(s):  
Plasma Membrane ◽  
Neuropeptide Y ◽  
Cell Line ◽  
Pc12 Cells ◽  
Pc12 Cell ◽  
Small Interfering Rna ◽  
Dense Core ◽  
Dense Core Vesicles ◽  
Pc12 Cell Line ◽  
Interfering Rna

It has recently been proposed that synaptotagmin (Syt) VII functions as a plasma membrane Ca2+sensor for dense-core vesicle exocytosis in PC12 cells based on the results of transient overexpression studies using green fluorescent protein (GFP)-tagged Syt VII; however, the precise subcellular localization of Syt VII is still a matter of controversy (plasma membraneversussecretory granules). In this study we established a PC12 cell line “stably expressing” the Syt VII-GFP molecule and demonstrated by immunocytochemical and immunoelectron microscopic analyses that the Syt VII-GFP protein is localized on dense-core vesicles as well as in other intracellular membranous structures, such as thetrans-Golgi network and lysosomes. Syt VII-GFP forms a complex with endogenous Syts I and IX, but not with Syt IV, and it colocalize well with Syts I and IX in the cellular processes (where dense-core vesicles are accumulated) in the PC12 cell line. We further demonstrated by an N-terminal antibody-uptake experiment that Syt VII-GFP-containing dense-core vesicles undergo Ca2+-dependent exocytosis, the same as endogenous Syt IX-containing vesicles. Moreover, silencing of Syt VII-GFP with specific small interfering RNA dramatically reduced high KCl-dependent neuropeptide Y secretion from the stable PC12 cell line (∼60% of the control cells), whereas the same small interfering RNA had little effect on neuropeptide Y secretion from the wild-type PC12 cells (∼85–90% of the control cells), indicating that the level of endogenous expression of Syt VII molecules must be low. Our results indicate that the targeting of Syt VII-GFP molecules to specific membrane compartment(s) is affected by the transfection method (transient expressionversusstable expression) and suggested that Syt VII molecule on dense-core vesicles functions as a vesicular Ca2+sensor for exocytosis in endocrine cells.

scholarly journals The Small GTPase RalA Controls Exocytosis of Large Dense Core Secretory Granules by Interacting with ARF6-dependent Phospholipase D1

2005 ◽  
Vol 280 (33) ◽  
pp. 29921-29928 ◽  
Author(s):  
Nicolas Vitale ◽  
Jacques Mawet ◽  
Jacques Camonis ◽  
Romano Regazzi ◽  
Marie-France Bader ◽  
...  
Keyword(s):  
Secretory Granules ◽  
Small Gtpase ◽  
Dense Core ◽  
Phospholipase D1
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