Increased expression of two phospholipase D isoforms during experimentally induced hippocampal mossy fiber outgrowth

Zhang, Yan; Huang, Ping; Du, Guangwei; Kanaho, Yasunori; Frohman, Michael A.; Tsirka, Stella E.

doi:10.1002/glia.10322

Cited by 41 publications

(35 citation statements)

References 30 publications

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“…In bovine adrenal chromaffin cells and rat cerebellar granule cells, PLD1 is localized predominantly to the plasma membrane (28,62), whereas in rat liver homogenates PLD1 is detected in the both the Golgi apparatus and plasma membrane upon subcellular fractionation (49). In cell lines, PLD1 has been localized to intracellular membranes (Golgi, endosomes, lysosomes, and nucleus) as well as the plasma membrane (28,49,57,63). Transfection of chromophore-or epitope-tagged PLD1 has demonstrated a similar range of subcellular distributions, along with evidence of activation-associated translocation of PLD1 from secretory vesicles to the plasma membrane (58, 64 -66).…”

Section: Discussionmentioning

confidence: 99%

“…Subcellular fractionation of rat liver demonstrated predominant localization of endogenous PLD2 in the Golgi apparatus and light membranes (70). In cell lines, endogenous PLD2 has been demonstrated in the plasma membrane, Golgi apparatus, and nucleus (50,63,67). Overexpressed PLD2 has been demonstrated in the plasma membrane as well as intracellular vesicles and the nucleus (18,64,67).…”

Section: Discussionmentioning

confidence: 99%

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Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Barton¹,

Bourgoin²,

Kusner

2004

The Journal of Immunology

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Phagocytosis is a fundamental feature of the innate immune system, required for antimicrobial defense, resolution of inflammation, and tissue remodeling. Furthermore, phagocytosis is coupled to a diverse range of cytotoxic effector mechanisms, including the respiratory burst, secretion of inflammatory mediators and Ag presentation. Phospholipase D (PLD) has been linked to the regulation of phagocytosis and subsequent effector responses, but the identity of the PLD isoform(s) involved and the molecular mechanisms of activation are unknown. We used primary human macrophages and human THP-1 promonocytes to characterize the role of PLD in phagocytosis. Macrophages, THP-1 cells, and other human myelomonocytic cells expressed both PLD1 and PLD2 proteins. Phagocytosis of complement-opsonized zymosan was associated with stimulation of the activity of both PLD1 and PLD2, as demonstrated by a novel immunoprecipitation-in vitro PLD assay. Transfection of dominant-negative PLD1 or PLD2 each inhibited the extent of phagocytosis (by 55–65%), and their combined effects were additive (reduction of 91%). PLD1 and PLD2 exhibited distinct localizations in resting macrophages and those undergoing phagocytosis, and only PLD1 localized to the phagosome membrane. The COS-7 monkey fibroblast cell line, which has been used as a heterologous system for the analysis of receptor-mediated phagocytosis, expressed PLD2 but not PLD1. These data support a model in which macrophage phagocytosis is coordinately regulated by both PLD1 and PLD2, with isoform-specific localization. Human myelomonocytic cell lines accurately model PLD-dependent signal transduction events required for phagocytosis, but the heterologous COS cell system does not.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Barton¹,

Bourgoin²,

Kusner

2004

The Journal of Immunology

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“…The affinity-purified rabbit anti-PLD1 C-terminal antibody was described in Zhang et al (13). Anti-human GH, anti-SNAP25 antibodies, and secondary goat antibodies coupled to Alexa conjugates (555 or 647) have been described previously (14).…”

Section: Methodsmentioning

confidence: 99%

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

Zeniou-Meyer

Zabari

Ashery

et al. 2007

Journal of Biological Chemistry

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191

228

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Substantial efforts have recently been made to demonstrate the importance of lipids and lipid-modifying enzymes in various membrane trafficking processes, including calcium-regulated exocytosis of hormones and neurotransmitters. Among bioactive lipids, phosphatidic acid (PA) is an attractive candidate to promote membrane fusion through its ability to change membrane topology. To date, however, the biosynthetic pathway, the dynamic location, and actual function of PA in secretory cells remain unknown. Using a short interference RNA strategy on chromaffin and PC12 cells, we demonstrate here that phospholipase D1 is activated in secretagogue-stimulated cells and that it produces PA at the plasma membrane at the secretory granule docking sites. We show that phospholipase D1 activation and PA production represent key events in the exocytotic progression. Membrane capacitance measurements indicate that reduction of endogenous PA impairs the formation of fusion-competent granules. Finally, we show that the PLD1 short interference RNAmediated inhibition of exocytosis can be rescued by exogenous provision of a lipid that favors the transition of opposed bi-layer membranes to hemifused membranes having the outer leaflets fused. Our findings demonstrate that PA synthesis is required during exocytosis to facilitate a late event in the granule fusion pathway. We propose that the underlying mechanism is related to the ability of PA to alter membrane curvature and promote hemi-fusion. Phosphatidic acid (PA)2 is a pleiotropic bioactive lipid that has been proposed to activate selected enzymes (1), recruit proteins to membrane surfaces (2), and serve as a substrate for the formation of other signaling lipids (3). Most intriguingly, PA has also been shown to promote negative curvature in bi-layer membranes due to its small polar head-group in combination with two fatty-acyl side chains (4). The bulk of cellular PA is synthesized via two different acylation pathways, the glycerol 3-phosphate pathway and the dihydroxy acetone phosphate pathway, which are named according to their respective precursors. However, PA is also produced via hydrolysis of phosphatidylcholine by phospholipase D (PLD) (5) on a much faster time scale, and this latter source is thought to underlie the dynamic regulation of PA that allows it to function as a signaling lipid in agonist-stimulated cell biological responses such as secretion and changes in cellular morphology.In mammals, the classic PLD family is composed of a pair of membrane-associated proteins, PLD1 and PLD2. Both PLD isoforms require phosphatidylinositol 4,5-bisphosphate for their enzymatic activity. However, whereas PLD2 exhibits relatively high basal activity in isolation, full activation of PLD1 requires its stimulation by small GTPases of the ADP-ribosylation factor (ARF), Rho and Ral families, and protein kinase C (3, 6). PLD enzymes have been proposed to be involved in a number of cellular processes, including cell growth and survival, cell differentiation, and vesicular trafficking (3)....

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“…PLD isozymes, including PLD1 and PLD2, are present in many types of mammalian cells, including neurons (Meier et al, 1999). Recently, both PLD1 and PLD2 have been implicated in the regulation of neurite growth in neural cell lines (Hayakawa et al, 1999;Gibbs and Meier, 2000) and neural stem cells (Sung et al, 2001;Yoon et al, 2005) and the seizure-induced sprouting of mossy fibers (Zhang et al, 2004(Zhang et al, , 2005.…”

Section: Introductionmentioning

confidence: 99%

PLD1 Negatively Regulates Dendritic Branching

Zhu

Kang

Zhang

et al. 2012

Journal of Neuroscience

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Neurons have characteristic dendritic arborization patterns that contribute to information processing. One essential component of dendritic arborization is the formation of a specific number of branches. Although intracellular pathways promoting dendritic growth and branching are being elucidated, the mechanisms that negatively regulate the branching of dendrites remain enigmatic. In this study, using gain-of-function and loss-of-function studies, we show that phospholipase D1 (PLD1) acts as a negative regulator of dendritic branching in cultured hippocampal neurons from embryonic day 18 rat embryos. Overexpression of wild-type PLD1 (WT-PLD1) decreases the complexity of dendrites, whereas knockdown or inhibition of PLD1 increases dendritic branching. We further demonstrated that PLD1 acts downstream of RhoA, one of the small Rho GTPases, to suppress dendritic branching. The restriction of dendritic branching by constitutively active RhoA (V14-RhoA) can be partially rescued by knockdown of PLD1. Moreover, the inhibition of dendritic branching by V14-RhoA and WT-PLD1 can be partially ameliorated by reducing the level of phosphatidic acid (PA), which is the enzymatic product of PLD1. Together, these results suggest that RhoA-PLD1-PA may represent a novel signaling pathway in the restriction of dendritic branching and may thus provide insight into the mechanisms of dendritic morphogenesis.

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Increased expression of two phospholipase D isoforms during experimentally induced hippocampal mossy fiber outgrowth

Cited by 41 publications

References 30 publications

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

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

PLD1 Negatively Regulates Dendritic Branching

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