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Book ; Online ; E-Book: Lipid signaling in human diseases

Gomez-Cambronero, Julian / Frohman, Michael A.

(Handbook of experimental pharmacology ; 259)

2020

Author's details	Julian Gomez-Cambronero, Michael A. Frohman editors
Series title	Handbook of experimental pharmacology ; 259
Collection
Keywords	Pharmacology ; Cancer research ; Medical biochemistry
Language	English
Size	1 Online-Ressource(xiv, 336 Seiten), Illustrationen
Publisher	Springer
Publishing place	Cham
Publishing country	Switzerland
Document type	Book ; Online ; E-Book
Remark	Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
HBZ-ID	HT020450766
ISBN	978-3-030-33668-4 ; 9783030336677 ; 3-030-33668-9 ; 3030336670
DOI	10.1007/978-3-030-33668-4
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article ; Online: Lack of effective translational regulation of PLD expression and exosome biogenesis in triple-negative breast cancer cells.

Gomez-Cambronero, Julian

Cancer metastasis reviews

2018 Volume 37, Issue 2-3, Page(s) 491–507

Abstract: Triple-negative breast cancer (TNBC) is an aggressive subtype of breast cancer that is difficult to treat since cells lack the three receptors (ES, PR, or HER) that the most effective treatments target. We have used a well-established TNBC cell line (MDA- ...

Abstract	Triple-negative breast cancer (TNBC) is an aggressive subtype of breast cancer that is difficult to treat since cells lack the three receptors (ES, PR, or HER) that the most effective treatments target. We have used a well-established TNBC cell line (MDA-MB-231) from which we found evidence in support for a phospholipase D (PLD)-mediated tumor growth and metastasis: high levels of expression of PLD, as well as the absence of inhibitory miRs (such as miR-203) and 3'-mRNA PARN deadenylase activity in these cells. Such findings are not present in a luminal B cell line, MCF-7, and we propose a new miR•PARN•PLD node that is not uniform across breast cancer molecular subtypes and as such TNBC could be pharmacologically targeted differentially. We review the participation of PLD and phosphatidic acid (PA), its enzymatic product, as new "players" in breast cancer biology, with the aspects of regulation of the tumor microenvironment, macrophage polarization, regulation of PLD transcripts by specific miRs and deadenylases, and PLD-regulated exosome biogenesis. A new signaling miR•PARN•PLD node could serve as new biomarkers for TNBC abnormal signaling and metastatic disease staging, potentially before metastases are able to be visualized using conventional imaging.
MeSH term(s)	Biomarkers, Tumor ; Disease Progression ; Exoribonucleases/metabolism ; Exosomes/metabolism ; Female ; Gene Expression Regulation, Neoplastic ; Humans ; MicroRNAs/genetics ; Phospholipase D/genetics ; Phospholipase D/metabolism ; Protein Biosynthesis ; RNA, Untranslated/genetics ; Triple Negative Breast Neoplasms/genetics ; Triple Negative Breast Neoplasms/metabolism ; Triple Negative Breast Neoplasms/pathology ; Tumor Microenvironment
Chemical Substances	Biomarkers, Tumor ; MicroRNAs ; RNA, Untranslated ; Exoribonucleases (EC 3.1.-) ; poly(A)-specific ribonuclease (EC 3.1.13.4) ; Phospholipase D (EC 3.1.4.4)
Language	English
Publishing date	2018-08-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	604857-2
ISSN	1573-7233 ; 0167-7659
ISSN (online)	1573-7233
ISSN	0167-7659
DOI	10.1007/s10555-018-9753-x
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Article ; Online: Targeting Phospholipase D Genetically and Pharmacologically for Studying Leukocyte Function.

Gomez-Cambronero, Julian / Ganesan, Ramya

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1835, Page(s) 297–314

Abstract: Phospholipase D (PLD), is a protein that breaks down phospholipids, maintaining structural integrity and remodeling of cellular or intracellular membranes, as well as mediating protein trafficking and cytoskeletal dynamics during cell motility. One of ... ...

Abstract	Phospholipase D (PLD), is a protein that breaks down phospholipids, maintaining structural integrity and remodeling of cellular or intracellular membranes, as well as mediating protein trafficking and cytoskeletal dynamics during cell motility. One of the reaction products of PLD action is phosphatidic acid (PA). PA is a mitogen involved in a large variety of physiological cellular functions, such as cell growth, cell cycle progression, and cell motility. We have chosen as cell models the leukocyte polymorphonuclear neutrophil and the macrophage as examples of cell motility. We provide a three-part method for targeting PLD genetically and pharmacologically to study its role in cell migration. In the first part, we begin with genetically deficient mice PLD1-KO and PLD2-KO. We describe bone marrow neutrophil (BMN) isolation; BMN is labeled fluorescently and can be used for studying tissue-damaging neutrophilia in ischemia-reperfusion injury (IRI). In the second part, we begin also with PLD1-KO and PLD2-KO and prepare bone marrow-derived macrophages (BMDM), first from monocytes and then inducing macrophage differentiation in culture with continuous incubation of cytokines. We use BMDM to find experimentally if PLD woul play a role in cholesterol phagocytosis, which is the first step in atherosclerosis progression. In the third part, we study PLD function in BMN and BMDM with PLD enzyme pharmacological inhibitors instead of genetically deficient mice, to ascertain the particular contributions of isoforms PLD1 and PLD2 on leukocyte function. By using the three-step thorough approach, we could understand the molecular underpinning of PLD in the pathological conditions indicated above, IRI-neutrophilia and atherosclerosis.
MeSH term(s)	Animals ; Cell Movement/drug effects ; Cell Movement/immunology ; Chemotaxis, Leukocyte/drug effects ; Chemotaxis, Leukocyte/immunology ; Enzyme Inhibitors/pharmacology ; Gene Targeting/methods ; Isoenzymes ; Leukocytes/drug effects ; Leukocytes/physiology ; Macrophages/drug effects ; Macrophages/physiology ; Mice ; Mice, Knockout ; Multigene Family ; Neutrophils/drug effects ; Neutrophils/physiology ; Phospholipase D/antagonists & inhibitors ; Phospholipase D/genetics ; Phospholipase D/metabolism ; RAW 264.7 Cells ; Signal Transduction
Chemical Substances	Enzyme Inhibitors ; Isoenzymes ; Phospholipase D (EC 3.1.4.4)
Language	English
Publishing date	2018-08-14
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-8672-9_16
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Article ; Online ; Conference proceedings: FASEB Science Research Conference on phospholipid cell signaling and metabolism in inflammation and cancer.

Gomez-Cambronero, Julian

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2014 Volume 29, Issue 1, Page(s) 5–10

MeSH term(s)	Animals ; Humans ; Inflammation/metabolism ; Neoplasms/metabolism ; Phospholipids/metabolism ; Signal Transduction
Chemical Substances	Phospholipids
Language	English
Publishing date	2014-12-18
Publishing country	United States
Document type	Congresses ; Research Support, N.I.H., Extramural
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.15-0102ufm
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Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Phospholipase D and the Mitogen Phosphatidic Acid in Human Disease: Inhibitors of PLD at the Crossroads of Phospholipid Biology and Cancer.

Gomez-Cambronero, Julian / Shah, Krushangi N

Handbook of experimental pharmacology

2019 Volume 259, Page(s) 89–113

Abstract: Lipids are key building blocks of biological membranes and are involved in complex signaling processes such as metabolism, proliferation, migration, and apoptosis. Extracellular signaling by growth factors, stress, and nutrients is transmitted through ... ...

Abstract	Lipids are key building blocks of biological membranes and are involved in complex signaling processes such as metabolism, proliferation, migration, and apoptosis. Extracellular signaling by growth factors, stress, and nutrients is transmitted through receptors that activate lipid-modifying enzymes such as the phospholipases, sphingosine kinase, or phosphoinositide 3-kinase, which then modify phospholipids, sphingolipids, and phosphoinositides. One such important enzyme is phospholipase D (PLD), which cleaves phosphatidylcholine to yield phosphatidic acid and choline. PLD isoforms have dual role in cells. The first involves maintaining cell membrane integrity and cell signaling, including cell proliferation, migration, cytoskeletal alterations, and invasion through the PLD product PA, and the second involves protein-protein interactions with a variety of binding partners. Increased evidence of elevated PLD expression and activity linked to many pathological conditions, including cancer, neurological and inflammatory diseases, and infection, has motivated the development of dual- and isoform-specific PLD inhibitors. Many of these inhibitors are reported to be efficacious and safe in cells and mouse disease models, suggesting the potential for PLD inhibitors as therapeutics for cancer and other diseases. Current knowledge and ongoing research of PLD signaling networks will help to evolve inhibitors with increased efficacy and safety for clinical studies.
MeSH term(s)	Animals ; Enzyme Inhibitors/pharmacology ; Humans ; Mice ; Neoplasms/enzymology ; Phosphatidic Acids ; Phospholipase D/antagonists & inhibitors ; Signal Transduction
Chemical Substances	Enzyme Inhibitors ; Phosphatidic Acids ; Phospholipase D (EC 3.1.4.4)
Language	English
Publishing date	2019-09-20
Publishing country	Germany
Document type	Journal Article
ISSN	0171-2004
ISSN	0171-2004
DOI	10.1007/164_2019_216
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Article ; Online: Phospholipase D in cell signaling: from a myriad of cell functions to cancer growth and metastasis.

Gomez-Cambronero, Julian

The Journal of biological chemistry

2014 Volume 289, Issue 33, Page(s) 22557–22566

Abstract: Phospholipase D (PLD) enzymes play a double vital role in cells: they maintain the integrity of cellular membranes and they participate in cell signaling including intracellular protein trafficking, cytoskeletal dynamics, cell migration, and cell ... ...

Abstract	Phospholipase D (PLD) enzymes play a double vital role in cells: they maintain the integrity of cellular membranes and they participate in cell signaling including intracellular protein trafficking, cytoskeletal dynamics, cell migration, and cell proliferation. The particular involvement of PLD in cell migration is accomplished: (a) through the actions of its enzymatic product of reaction, phosphatidic acid, and its unique shape-binding role on membrane geometry; (b) through a particular guanine nucleotide exchange factor (GEF) activity (the first of its class assigned to a phospholipase) in the case of the mammalian isoform PLD2; and (c) through protein-protein interactions with a wide network of molecules: Wiskott-Aldrich syndrome protein (WASp), Grb2, ribosomal S6 kinase (S6K), and Rac2. Further, PLD interacts with a variety of kinases (PKC, FES, EGF receptor (EGFR), and JAK3) that are activated by it, or PLD becomes the target substrate. Out of these myriads of functions, PLD is becoming recognized as a major player in cell migration, cell invasion, and cancer metastasis. This is the story of the evolution of PLD from being involved in a large number of seemingly unrelated cellular functions to its most recent role in cancer signaling, a subfield that is expected to grow exponentially.
MeSH term(s)	Animals ; Cell Membrane/enzymology ; Cell Membrane/genetics ; Cell Membrane/pathology ; Cell Movement ; GRB2 Adaptor Protein/genetics ; GRB2 Adaptor Protein/metabolism ; Humans ; Neoplasm Metastasis ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Neoplasms/enzymology ; Neoplasms/genetics ; Neoplasms/pathology ; Phosphatidic Acids/genetics ; Phosphatidic Acids/metabolism ; Phospholipase D/genetics ; Phospholipase D/metabolism ; Ribosomal Protein S6 Kinases/genetics ; Ribosomal Protein S6 Kinases/metabolism ; Signal Transduction ; Wiskott-Aldrich Syndrome Protein Family/genetics ; Wiskott-Aldrich Syndrome Protein Family/metabolism ; rac GTP-Binding Proteins/genetics ; rac GTP-Binding Proteins/metabolism ; RAC2 GTP-Binding Protein
Chemical Substances	GRB2 Adaptor Protein ; GRB2 protein, human ; Neoplasm Proteins ; Phosphatidic Acids ; Wiskott-Aldrich Syndrome Protein Family ; Ribosomal Protein S6 Kinases (EC 2.7.11.1) ; phospholipase D2 (EC 3.1.4.-) ; Phospholipase D (EC 3.1.4.4) ; rac GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2014-07-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.R114.574152
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Article ; Online: Phosphatidic acid, phospholipase D and tumorigenesis.

Gomez-Cambronero, Julian

Advances in biological regulation

2013 Volume 54, Page(s) 197–206

Abstract: Phospholipase D (PLD) is a membrane protein with a double role: maintenance of the structural integrity of cellular or intracellular membranes and involvement in cell signaling through the product of the catalytic reaction, PA, and through protein- ... ...

Abstract	Phospholipase D (PLD) is a membrane protein with a double role: maintenance of the structural integrity of cellular or intracellular membranes and involvement in cell signaling through the product of the catalytic reaction, PA, and through protein-protein interaction with a variety of partners. Cross-talk during PLD signaling occurs with other cancer regulators (Ras, PDGF, TGF and kinases). Elevation of either PLD1 or PLD2 (the two mammalian isoforms of PLD) is able to transform fibroblasts and contribute to cancer progression. Elevated total PLD activity, as well as overexpression, is present in a wide variety of cancers such as gastric, colorectal, renal, stomach, esophagus, lung and breast. PLD provides survival signals and is involved in migration, adhesion and invasion of cancer cells, and all are increased during PLD upregulation or, conversely, they are decreased during PLD loss of function. Eventhough the end results of PLD action as relates to downstream signaling mechanisms are still currently being elucidated, invasion, a pre-requisite for metastasis, is directly affected by PLD. This review will introduce the classical mammalian PLD's, PLD1 and PLD2, followed by the mechanisms of intracellular regulation and a status of current investigation in the crucial involvement of PLD in cancer, mostly through its role in cell migration, invasion and metastasis, that has grown exponentially in the last few years.
MeSH term(s)	Animals ; Carcinogenesis/genetics ; Carcinogenesis/metabolism ; Humans ; Neoplasms/enzymology ; Neoplasms/genetics ; Neoplasms/metabolism ; Phosphatidic Acids/metabolism ; Phospholipase D/genetics ; Phospholipase D/metabolism
Chemical Substances	Phosphatidic Acids ; phospholipase D2 (EC 3.1.4.-) ; Phospholipase D (EC 3.1.4.4) ; phospholipase D1 (EC 3.1.4.4)
Language	English
Publishing date	2013-09-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2667413-0
ISSN	2212-4934 ; 2212-4926
ISSN (online)	2212-4934
ISSN	2212-4926
DOI	10.1016/j.jbior.2013.08.006
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Article ; Online: Down-regulation of MicroRNAs (MiRs) 203, 887, 3619 and 182 Prevents Vimentin-triggered, Phospholipase D (PLD)-mediated Cancer Cell Invasion.

Fite, Kristen / Gomez-Cambronero, Julian

The Journal of biological chemistry

2015 Volume 291, Issue 2, Page(s) 719–730

Abstract: Breast cancer is a leading cause of morbidity and mortality among women. Metastasis is initiated after epithelial-mesenchymal-transition (EMT). We have found a connection between EMT markers and the expression of four microRNAs (miRs) mediated by the ... ...

Abstract	Breast cancer is a leading cause of morbidity and mortality among women. Metastasis is initiated after epithelial-mesenchymal-transition (EMT). We have found a connection between EMT markers and the expression of four microRNAs (miRs) mediated by the signaling enzyme phospholipase D (PLD). Low aggressive MCF-7 breast cancer cells have low endogenous PLD enzymatic activity and cell invasion, concomitant with high expression of miR-203, -887, and -3619 (that decrease PLD2 translation and a luciferase reporter) and miR-182 (targeting PLD1) that are, therefore, "tumor-suppressor-like" miRs. The combination miR-887+miR-3619 abolished >90% of PLD enzymatic activity. Conversely, post-EMT MDA-MB-231 cells have low miR expression, high levels of PLD1/2, and high aggressiveness. The latter was reversed by ectopically transfecting the miRs, which was negated by silencing miRs with specific siRNAs. We determined that the molecular mechanism is that E-cadherin triggers expression of the miRs in pre-EMT cells, whereas vimentin dampens expression of the miRs in post-EMT invasive cells. This novel work identifies for the first time a set of miRs that are activated by a major pre-EMT marker and deactivated by a post-EMT marker, boosting the transition from low invasion to high invasion, as mediated by the key phospholipid metabolism enzyme PLD.
MeSH term(s)	3' Untranslated Regions/genetics ; Base Sequence ; Binding Sites/genetics ; Biomarkers, Tumor/metabolism ; Breast Neoplasms/enzymology ; Breast Neoplasms/genetics ; Breast Neoplasms/pathology ; Conserved Sequence/genetics ; Down-Regulation/genetics ; Epithelial-Mesenchymal Transition/genetics ; Female ; Gene Expression Regulation, Neoplastic ; Humans ; MCF-7 Cells ; MicroRNAs/genetics ; MicroRNAs/metabolism ; Models, Biological ; Molecular Sequence Data ; Neoplasm Invasiveness ; Phenotype ; Phospholipase D/genetics ; Phospholipase D/metabolism ; Plasmids/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Vimentin/metabolism
Chemical Substances	3' Untranslated Regions ; Biomarkers, Tumor ; MicroRNAs ; RNA, Messenger ; Vimentin ; Phospholipase D (EC 3.1.4.4)
Language	English
Publishing date	2015-11-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M115.686006
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Article ; Online: Biochemical and cellular implications of a dual lipase-GEF function of phospholipase D2 (PLD2).

Gomez-Cambronero, Julian

Journal of leukocyte biology

2012 Volume 92, Issue 3, Page(s) 461–467

Abstract: PLD2 plays a key role in cell membrane lipid reorganization and as a key cell signaling protein in leukocyte chemotaxis and phagocytosis. Adding to the large role for a lipase in cellular functions, recently, our lab has identified a PLD2-Rac2 binding ... ...

Abstract	PLD2 plays a key role in cell membrane lipid reorganization and as a key cell signaling protein in leukocyte chemotaxis and phagocytosis. Adding to the large role for a lipase in cellular functions, recently, our lab has identified a PLD2-Rac2 binding through two CRIB domains in PLD2 and has defined PLD2 as having a new function, that of a GEF for Rac2. PLD2 joins other major GEFs, such as P-Rex1 and Vav, which operate mainly in leukocytes. We explain the biochemical and cellular implications of a lipase-GEF duality. Under normal conditions, GEFs are not constitutively active; instead, their activation is highly regulated. Activation of PLD2 leads to its localization at the plasma membrane, where it can access its substrate GTPases. We propose that PLD2 can act as a "scaffold" protein to increase efficiency of signaling and compartmentalization at a phagocytic cup or the leading edge of a leukocyte lamellipodium. This new concept will help our understanding of leukocyte crucial functions, such as cell migration and adhesion, and how their deregulation impacts chronic inflammation.
MeSH term(s)	Animals ; Chemotaxis, Leukocyte/physiology ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Leukocytes/metabolism ; Lipase/metabolism ; Phospholipase D/metabolism ; Signal Transduction/physiology
Chemical Substances	Guanine Nucleotide Exchange Factors ; Lipase (EC 3.1.1.3) ; phospholipase D2 (EC 3.1.4.-) ; Phospholipase D (EC 3.1.4.4)
Language	English
Publishing date	2012-07-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	605722-6
ISSN	1938-3673 ; 0741-5400
ISSN (online)	1938-3673
ISSN	0741-5400
DOI	10.1189/jlb.0212073
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Article ; Online: Structure analysis between the SWAP-70 RHO-GEF and the newly described PLD2-GEF.

Gomez-Cambronero, Julian

Small GTPases

2012 Volume 3, Issue 4, Page(s) 202–208

Abstract: Small GTPases like Rac2 are crucial regulators of many cell functions central to life itself. Our laboratory has recently found that phospholipase D2 (PLD2) can act as a guanine nucleotide exchange factor (GEF) for Rac2. PLD2 has a Pleckstrin Homology ( ... ...

Abstract	Small GTPases like Rac2 are crucial regulators of many cell functions central to life itself. Our laboratory has recently found that phospholipase D2 (PLD2) can act as a guanine nucleotide exchange factor (GEF) for Rac2. PLD2 has a Pleckstrin Homology (PH) domain but does not bear a Dbl homology (DH) or DOCK homology region (DHR) domain. It has, however, a Phox (PX) domain upstream of its PH domain. To better understand the novel finding of PLD2 as an enhancer of GDP/GTP exchange, we modeled the N-terminal portion of PLD2 (as the crystal structure of this protein has not as of yet been resolved), and studied the correlation with two known GEFs, SWAP-70 and the Leukemic Associated RhoGEF (LARG). Structural similarities between PLD2's PH and SWAP-70s or LARG's PH domain are very extensive, while similarities between PLD2's PX and SWAP-70s or LARG's DH domains are less evident. This indicates that PLD functions as a GEF utilizing its PH domain and part of its PX domain and possibly other regions. All this makes PLD unique, and an entirely new class of GEF. By bearing two enzymatic activities (break down of PC and GDP/GTP exchange), it is realistic to assume that PLD is an important signaling node for several intracellular pathways. Future experiments will ascertain how the newly described PLD2's GEF is regulated in the context of cell activation.
MeSH term(s)	DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Guanine Nucleotide Exchange Factors/chemistry ; Guanine Nucleotide Exchange Factors/metabolism ; Minor Histocompatibility Antigens ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Phospholipase D/chemistry ; Phospholipase D/metabolism ; Protein Structure, Tertiary ; Rho Guanine Nucleotide Exchange Factors ; rac GTP-Binding Proteins/metabolism ; RAC2 GTP-Binding Protein
Chemical Substances	DNA-Binding Proteins ; Guanine Nucleotide Exchange Factors ; Minor Histocompatibility Antigens ; Nuclear Proteins ; Rho Guanine Nucleotide Exchange Factors ; SWAP70 protein, human ; phospholipase D2 (EC 3.1.4.-) ; Phospholipase D (EC 3.1.4.4) ; rac GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2012-08-03
Publishing country	United States
Document type	Letter ; Research Support, N.I.H., Extramural
ZDB-ID	2682247-7
ISSN	2154-1256 ; 2154-1248
ISSN (online)	2154-1256
ISSN	2154-1248
DOI	10.4161/sgtp.20887
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