Regulation of Constitutive Protein Transit by Phospholipase D in HT29-cl19A Cells

Denmat-Ouisse, Lise Anne; Phebidias, Céline; Honkavaara, Päivi; Robin, Philippe; Geny, Blandine; Min, Do Sik; Bourgoin, Sylvain G.; Frohman, Michael A.; Raymond, Marie Noëlle

doi:10.1074/jbc.m104276200

Cited by 28 publications

(28 citation statements)

References 43 publications

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“…The cortical distribution is consistent with the plasma membrane localization proposed from biochemical studies of phagocytes (16, 32, 48, 56 -58). The intracellular PLD1 is likely vesicular in origin, in agreement with data from several cell types (28,49,58). PLD2 localized to intracellular vesicles (especially in the perinuclear region) and the nucleus in resting macrophages (Fig.…”

Section: Pld1 and Pld2 Exhibit Distinct Differences In Subcellular Losupporting

confidence: 75%

“…Western blotting of the IPs confirmed the specificity of the Abs, (Fig. 2B), as previously reported (28,49,50). No PLD1 protein was detected in the anti-PLD2 IPs, and only a minor amount of PLD2 was detected in the anti-PLD1 IPs.…”

Section: Phagocytic Particles Stimulated Increased Levels Of Pld1 Andsupporting

confidence: 57%

“…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%

“…Polyclonal Abs to PLD1 or PLD2 were raised by immunizing rabbits with specific peptides for each protein (four for PLD1, two for PLD2), as previously described (28). mAb to lysosome-associated membrane protein-1 (LAMP-1) was from the Developmental Studies Hybridoma Bank (University of Iowa, Iowa City, IA).…”

Section: Methodsmentioning

confidence: 99%

“…We have used improved anti-peptide Abs to PLD1 and PLD2 (28) to determine their distribution in primary human macrophage and several representative human myelomonocytic cell lines. Human macrophage and the human promonocytic cell lines, THP-1 and U937, express both PLD1 and PLD2 proteins with low levels of PLD2 detected in U937 cells (Fig.…”

Section: Primary Human Macrophages and Myelomonocytic Cell Lines Exprmentioning

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: Pld1 and Pld2 Exhibit Distinct Differences In Subcellular Losupporting

confidence: 75%

Section: Phagocytic Particles Stimulated Increased Levels Of Pld1 Andsupporting

confidence: 57%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Primary Human Macrophages and Myelomonocytic Cell Lines Exprmentioning

confidence: 99%

See 3 more Smart Citations

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Barton¹,

Bourgoin²,

Kusner

2004

The Journal of Immunology

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Regulation of Aldosterone Synthesis and Secretion

Bollag

2014

Comprehensive Physiology

150

110

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Aldosterone is a steroid hormone synthesized in and secreted from the outer layer of the adrenal cortex, the zona glomerulosa. Aldosterone is responsible for regulating sodium homeostasis, thereby helping to control blood volume and blood pressure. Insufficient aldosterone secretion can lead to hypotension and circulatory shock, particularly in infancy. On the other hand, excessive aldosterone levels, or those too high for sodium status, can cause hypertension and exacerbate the effects of high blood pressure on multiple organs, contributing to renal disease, stroke, visual loss, and congestive heart failure. Aldosterone is also thought to directly induce end-organ damage, including in the kidneys and heart. Because of the significance of aldosterone to the physiology and pathophysiology of the cardiovascular system, it is important to understand the regulation of its biosynthesis and secretion from the adrenal cortex. Herein, the mechanisms regulating aldosterone production in zona glomerulosa cells are discussed, with a particular emphasis on signaling pathways involved in the secretory response to the main controllers of aldosterone production, the renin-angiotensin II system, serum potassium levels and adrenocorticotrophic hormone. The signaling pathways involved include phospholipase C-mediated phosphoinositide hydrolysis, inositol 1,4,5-trisphosphate, cytosolic calcium levels, calcium influx pathways, calcium/calmodulin-dependent protein kinases, diacylglycerol, protein kinases C and D, 12-hydroxyeicostetraenoic acid, phospholipase D, mitogen-activated protein kinase pathways, tyrosine kinases, adenylate cyclase, and cAMP-dependent protein kinase. A complete understanding of the signaling events regulating aldosterone biosynthesis may allow the identification of novel targets for therapeutic interventions in hypertension, primary aldosteronism, congestive heart failure, renal disease, and other cardiovascular disorders.

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Phospholipase D

Bader¹,

Vitale²

Molecular Mechanisms of Exocytosis

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Regulation of Constitutive Protein Transit by Phospholipase D in HT29-cl19A Cells

Cited by 28 publications

References 43 publications

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Regulation of Aldosterone Synthesis and Secretion

Phospholipase D

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