Cited by 225Protein Kinase Regulation and GTPase SignalingSphingolipid Metabolism and SignalingFatty Acid Research and Health

The DOI matches its Crossref record; 105 of the 105 references it cites were found in a registry or an index.

Arachidonic acid and free fatty acids as second messengers and the role of protein kinase C

Khan, Wasiuddin A., Blobe, Gerard C., Hannun, Yusuf A.·1995·Cellular Signalling

DOI 10.1016/0898-6568(94)00089-t

Open this paper in CoChat — free account

Abstract

In addition to serving as the precursor to a plethora of eicosanoids and other bioactive molecules, arachidonate may function as a bona fide second messenger. A number of studies have documented the ability of arachidonate to regulate the function of multiple targets in vitro systems. This has been particularly well established and studied with the activation of protein kinase C by arachidonate in a mechanism distinct from activation by diacylglycerol. In cells, arachidonate induces a number of activities, many of which may be independent of further metabolism to eicosanoids; suggesting possible direct action of arachidonate. This review summarizes the current state of knowledge on the possible second messenger function of arachidonate with specific emphasis on the regulation of protein kinase C.

Integrity signals

Registry

Crossref · 10.1016/0898-6568(94)00089-t

Cites

105 of 105 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Intracellular Signaling by Hydrolysis of Phospholipids and Activation of Protein Kinase C
Nishizuka, Y. (1992) · Science · doi:10.1126/science.1411571 · Cited by 4,472
cPLA2 is phosphorylated and activated by MAP kinase
Lin, L., Wartmann, M., Lin, A. Y., Knopf, J. L., Seth, A., & Davis, R. J. (1993) · Cell · doi:10.1016/0092-8674(93)90666-e · Cited by 1,851
A novel arachidonic acid-selective cytosolic PLA2 contains a Ca2+-dependent translocation domain with homology to PKC and GAP
Clark, J. D., Lin, L.-L., Kriz, R. W., Ramesha, C. S., Sultzman, L. A., Lin, A. Y., Milona, N., & Knopf, J. L. (1991) · Cell · doi:10.1016/0092-8674(91)90556-e · Cited by 1,688
Diversity of group types, regulation, and function of phospholipase A2.
Dennis, E. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36794-7 · Cited by 1,435
Biochemistry of Lipids, Lipoproteins and Membranes
(2021) · Elsevier eBooks · doi:10.1016/c2020-0-00089-7 · Cited by 1,402
Signaling through phosphatidylcholine breakdown.
Exton, J. H. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40184-1 · Cited by 1,358
Activation of calcium and phospholipid-dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover.
Kishimoto, A., Takai, Y., Terutoshi, M. O. R. I., Kikkawa, U., & Nishizuka, Y. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85886-6 · Cited by 1,303
Functions of Sphingolipids and Sphingolipid Breakdown Products in Cellular Regulation
Hannun, Y. A., & Bell, R. M. (1989) · Science · doi:10.1126/science.2643164 · Cited by 1,251
Self-citation
The sphingomyelin cycle and the second messenger function of ceramide.
Hannun, Y. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41834-5 · Cited by 1,229
Self-citation
How is the level of free arachidonic acid controlled in mammalian cells?
Irvine, R. F. (1982) · Biochemical Journal · doi:10.1042/bj2040003 · Cited by 1,187

Show all 105 references

Research works printed but not linked: 26

Graber, 1994, J. Lipid Med., 9, 91
Ono, 1989, 86, 4868
Hannun, 1986, J. biol. Chem., 261, 7148
Shinomura, 1991, 88, 5149
Chen, 1992, J. biol. Chem., 282, 33
Berry, 1990, 87, 2294
Aihara, 1991, 88, 11062
Yoshida, 1992, 89, 6443
Abumrad, 1991, 88, 6008
Werner, 1991, Mol. Pharmac., 39, 547
Butcher, 1993, Cancer Res., 53, 3405
Laposata, 1982, 79, 7654
Clark, 1990, 87, 7708
Lin, 1992, 89, 6147
Burch, 1986, 83, 7201
Bell, 1979, 76, 3238
Stemmel, 1985, 82, 4
Stemmel, 1985, J. clin. Invest., 75, 1026
Custer, 1984, 81, 6738
Bassuk, 1987, 84, 7547
Wolf, 1986, J. biol. Chem., 261, 3501, 10.1016/S0021-9258(17)35676-4 · DOI
Hwang, 1990, 87, 5706
Piomelli, 1989, 86, 8550
Waldman, 1987, Pharmac. Rev., 39, 163
Speizer, 1991, Am. J. Physiol., 261, E109
Lopez-Ruiz, 1992, Endocrinology, 130, 1122

Sorted by citations

Glutamate uptake
Danbolt, N. C. (2001) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00067-8 · Cited by 4,227
Antibacterial free fatty acids: activities, mechanisms of action and biotechnological potential
Desbois, A. P., & Smith, V. J. (2009) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-009-2355-3 · Cited by 1,551
Shotgun lipidomics: Electrospray ionization mass spectrometric analysis and quantitation of cellular lipidomes directly from crude extracts of biological samples
Han, X., & Gross, R. W. (2004) · Mass Spectrometry Reviews · doi:10.1002/mas.20023 · Cited by 1,126
Regulation of protein kinase C
Newton, A. C. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80058-0 · Cited by 914
Pharmacokinetics and pharmacodynamics of systemically administered glucocorticoids.
Czock, D., Keller, F., Rasche, F. M., & H??ussler, U. (2005) · Clinical Pharmacokinetics · doi:10.2165/00003088-200544010-00003 · Cited by 886
Pathogenesis of insulin resistance in skeletal muscle
Abdul-Ghani, M. A., & DeFronzo, R. A. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2010/476279 · Cited by 670
Apoptosis: A Functional Paradigm for Programmed Plant Cell Death Induced by a Host-Selective Phytotoxin and Invoked during Development
Wang, H., Li, J., Bostock, R. M., & Gilchrist, D. G. (1996) · The Plant Cell · doi:10.1105/tpc.8.3.375 · Cited by 584
The Sevenfold Way of PKC Regulation
Liu, W. S., & Heckman, C. A. (1998) · Cellular Signalling · doi:10.1016/s0898-6568(98)00012-6 · Cited by 487
Endocannabinoids
Mechoulam, R., Fride, E., & Marzo, V. D. (1998) · European Journal of Pharmacology · doi:10.1016/s0014-2999(98)00649-9 · Cited by 447
Green Fluorescent Protein (GFP)-tagged Cysteine-rich Domains from Protein Kinase C as Fluorescent Indicators for Diacylglycerol Signaling in Living Cells
Oancea, E., Teruel, M. N., Quest, A. F. G., & Meyer, T. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.3.485 · Cited by 323
Hydrogen Peroxide as a Cell-Survival Signaling Molecule
Groeger, G., Quiney, C., & Cotter, T. G. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2728 · Cited by 318
The Unique Molecular and Cellular Microenvironment of Ovarian Cancer
Worzfeld, T., von Strandmann, E. P., Huber, M., Adhikary, T., Wagner, U. A. G., Reinartz, S., & Müller, R. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00024 · Cited by 296
Arachidonic Acid Stimulates Prostate Cancer Cell Growth: Critical Role of 5-Lipoxygenase
Ghosh, J., & Myers, C. E. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6799 · Cited by 259
Novel Roles of Specific Isoforms of Protein Kinase C in Activation of the c-fosSerum Response Element
Soh, J., Lee, E. H., Prywes, R., & Weinstein, I. B. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1313 · Cited by 259
Pathogenesis of cerebral vasospasm following aneurysmal subarachnoid hemorrhage: Putative mechanisms and novel approaches
Kolias, A. G., Sen, J., & Belli, A. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21823 · Cited by 231
Solvent-free matrix dry-coating for MALDI imaging of phospholipids
Puolitaival, S. M., Burnum-Johnson, K., Cornett, D. S., & Caprioli, R. M. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.02.013 · Cited by 234
Fatty Acids and Immune Responses—A New Perspective in Searching for Clues to Mechanism
Hwang, D. H. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.431 · Cited by 205
Effects of fatty acid unsaturation numbers on membrane fluidity and α-secretase-dependent amyloid precursor protein processing
Yang, X., Sheng, W., Sun, G. Y., & Lee, J. C. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.004 · Cited by 215
Fumonisin-induced hepatocarcinogenesis: mechanisms related to cancer initiation and promotion.
Gelderblom, W. C. A., Abel, S., Smuts, C. M., Marnewick, J. L., Marasas, W. F. O., Lemmer, E. R., & Ramljak, D. (2001) · Environmental Health Perspectives · doi:10.1289/ehp.01109s2291 · Cited by 192
20-Hydroxyeicosatetraenoic Acid-induced Vasoconstriction and Inhibition of Potassium Current in Cerebral Vascular Smooth Muscle Is Dependent on Activation of Protein Kinase C
Lange, A. R., Gebremedhin, D., Narayanan, J., & Harder, D. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.43.27345 · Cited by 186
Interrelationships between astrocyte function, oxidative stress and antioxidant status within the central nervous system
Peuchen, S., Bolaños, J. P., Heales, S., Almeida, Á., Duchen, M. R., & Clark, J. B. (1997) · Progress in Neurobiology · doi:10.1016/s0301-0082(97)00010-5 · Cited by 160
Spatial and temporal alterations of phospholipids determined by mass spectrometry during mouse embryo implantation
Burnum-Johnson, K., Cornett, D. S., Puolitaival, S. M., Milne, S. B., Myers, D. S., Tranguch, S. L., Brown, H. A., Dey, S. K., & Caprioli, R. M. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m900100-jlr200 · Cited by 159
20-Hydroxyeicosa-tetraenoic acid (20 HETE) activates protein kinase C. Role in regulation of rat renal Na+,K+-ATPase.
Nowicki, S., Chen, S. L., Aizman, O., Cheng, X.-J., Li, D., Nowicki, C., Nairn, A. C., Greengard, P., & Aperia, A. C. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119279 · Cited by 153
Arachidonic Acid Promotes Phosphorylation of 5-Lipoxygenase at Ser-271 by MAPK-activated Protein Kinase 2 (MK2)
Werz, O., Szellas, D., Steinhilber, D., & Rådmark, O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111945200 · Cited by 130
Pharmacology of signaling induced by dopamine D1-like receptor activation
Undieh, A. S. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.05.003 · Cited by 137
Peroxisome Proliferator–Activated Receptors: A Critical Link among Fatty Acids, Gene Expression and Carcinogenesis
Heuvel, J. P. V. (1999) · Journal of Nutrition · doi:10.1093/jn/129.2.575s · Cited by 126
Protein kinase C: a physiological mediator of enhanced transmitter output
Majewski, H., & Iannazzo, L. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(98)00017-3 · Cited by 116
Imaging of Intact Tissue Sections: Moving beyond the Microscope
Seeley, E. H., Schwamborn, K., & Caprioli, R. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.225854 · Cited by 111
A transcriptome-based global map of signaling pathways in the ovarian cancer microenvironment associated with clinical outcome
Reinartz, S., Finkernagel, F., Adhikary, T., Rohnalter, V., Schumann, T., Schober, Y., Nockher, W. A., Nist, A., Stiewe, T., Jansen, J. M., et al. (2016) · Genome biology · doi:10.1186/s13059-016-0956-6 · Cited by 108
The molecular biology of the group VIA Ca2+-independent phospholipase A2
Ma, Z., & TURK, J. W. (2001) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(01)67023-5 · Cited by 106
Isoenzymes of protein kinase C: differential involvement in apoptosis and pathogenesis.
Deacon, E. M., Pongracz, J. E., Griffiths, G., & Lord, J. M. (1997) · Molecular Pathology · doi:10.1136/mp.50.3.124 · Cited by 104
Ca2+ influx through CRAC channels activates cytosolic phospholipase A 2 , leukotriene C 4 secretion, and expression of c‐fos through ERK‐dependent and independent pathways in mast cells
Chang, W., Nelson, C., & Parekh, A. B. (2006) · The FASEB Journal · doi:10.1096/fj.06-6016fje · Cited by 102
Assessment of the arachidonic acid content in foods commonly consumed in the American diet
Taber, L., Chiu, C., & Whelan, J. (1998) · Lipids · doi:10.1007/s11745-998-0317-4 · Cited by 101
Role of polyunsaturated fatty acids in the inhibitory effect of human adipocytes on osteoblastic proliferation
Maurin, A., Chavassieux, P., Véricel, E., & Meunier, P. J. (2002) · Bone · doi:10.1016/s8756-3282(02)00805-0 · Cited by 100
Novel, selective delta6 or delta5 fatty acid desaturase inhibitors as antiinflammatory agents in mice.
Obukowicz, M. G., Welsch, D., Salsgiver, W. J., Martin-Berger, C. L., Chinn, K. S., Duffin, K. L., Raz, A., & Needleman, P. (1998) · PubMed · Cited by 100
Regulation of Rat Hepatocyte Protein Kinase C β Isoenzymes by the Lipid Peroxidation Product 4–Hydroxy–2,3–Nonenal: A Signaling Pathway to Modulate Vesicular Transport of Glycoproteins
Chiarpotto, E., Domenicotti, C., Paola, D., Vitali, A., Nitti, M., Pronzato, M. A., Biasi, F., Cottalasso, D., Marinari, U. M., Dragonetti, A., et al. (1999) · Hepatology · doi:10.1002/hep.510290510 · Cited by 97
A New Phosphatidylinositol 4,5-Bisphosphate-binding Site Located in the C2 Domain of Protein Kinase Cα
Corbalán‐García, S., Garcı́a-Garcı́a, J., Rodrı́guez-Alfaro, J. A., & Gómez-Fernández, J. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209385200 · Cited by 98
Receptor-mediated signaling pathways: potential targets of modulation by dietary fatty acids
Hwang, D., & Rhee, S. H. (1999) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/70.4.545 · Cited by 95
Prostaglandin E2 regulation of cyclooxygenase expression in keratinocytes is mediated via cyclic nucleotide-linked prostaglandin receptors
Maldve, R. E., Kim, Y., Muga, S. J., & Fischer, S. M. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32029-0 · Cited by 96
A causal relationship between unscheduled eicosanoid signaling and tumor development: cancer chemoprevention by inhibitors of arachidonic acid metabolism
Marks, F., Müller‐Decker, K., & Fürstenberger, G. (2000) · Toxicology · doi:10.1016/s0300-483x(00)00301-2 · Cited by 95
Effects of partial substitution of dietary fish oil with blends of vegetable oils, on blood leucocyte fatty acid compositions, immune function and histology in European sea bass (Dicentrarchus labrax L.)
Mourente, G., Good, J. E., Thompson, K. D., & Bell, J. G. (2007) · British Journal Of Nutrition · doi:10.1017/s000711450773461x · Cited by 93
Carnitine inhibits arachidonic acid turnover, platelet function, and oxidative stress
Pignatelli, P., Lenti, L., Sanguigni, V., Frati, G., Simeoni, I., Gazzaniga, P. P., Pulcinelli, F. M., & Violi, F. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00249.2002 · Cited by 92
How lipids contribute to ion channel function, a fat perspective on direct and indirect interactions
Cordero-Morales, J. F., & Vásquez, V. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.03.015 · Cited by 86
Eicosapentaenoic acid reduces ABCA1 serine phosphorylation and impairs ABCA1-dependent cholesterol efflux through cyclic AMP/protein kinase A signaling pathway in THP-1 macrophage-derived foam cells
Hu, Y., Ma, X., Li, X., Liu, X., Xiao, J., Mo, Z., Xiang, J., Liao, D., & Tang, C. (2008) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2008.11.003 · Cited by 89
Close Functional Coupling between Ca2+ Release-activated Ca2+ Channels, Arachidonic Acid Release, and Leukotriene C4 Secretion
Chang, W., & Parekh, A. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403969200 · Cited by 86
Rapid quantitation of free fatty acids in human plasma by high-performance liquid chromatography
Mehta, A., Oeser, A. M., & Carlson, M. G. (1998) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(98)00403-4 · Cited by 83
Eicosapentaenoic Acid, a n-3 Polyunsaturated Fatty Acid Differentially Modulates TNF-α, IL-1α, IL-6 and PGE2 Expression in UVB-Irradiated Human Keratinocytes
Pupe, A., Haes, P. D., Rhodes, L. E., Garmyn, M., Moison, R. M. W., van Henegouwen, G. B., & Degreef, H. J. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.01615.x · Cited by 82
Cyclooxygenase-2 and prostaglandin signaling in cholangiocarcinoma
Wu, T. (2005) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2005.04.002 · Cited by 83
Regulation of plasma fatty acid metabolism
Saleh, J., Sniderman, A. D., & Cianflone, K. (1999) · Clinica Chimica Acta · doi:10.1016/s0009-8981(99)00099-6 · Cited by 81
Silencing the expression of mitochondrial acyl-CoA thioesterase I and acyl-CoA synthetase 4 inhibits hormone-induced steroidogenesis
Maloberti, P., Castilla, R., Castillo, F., Maciel, F. C., Mendez, C. F., Paz, C., & Podestá, E. J. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04616.x · Cited by 79
Arachidonic Acid Influences Proinflammatory Gene Induction by Stabilizing the Inhibitor-κBα/Nuclear Factor-κB (NF-κB) Complex, thus Suppressing the Nuclear Translocation of NF-κB
Stuhlmeier, K. M., Kao, J. J., & Bach, F. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24679 · Cited by 78
Activation of Epithelial Growth Factor Receptor Pathway by Unsaturated Fatty Acids
Vacaresse, N., Lajoie‐Mazenc, I., Augè, N., Suc, I., Frisach, M., Salvayre, R., & Nègre‐Salvayre, A. (1999) · Circulation Research · doi:10.1161/01.res.85.10.892 · Cited by 77
Cellular Regulation of Cytosolic Group IV Phospholipase A2 by Phosphatidylinositol Bisphosphate Levels
Balsinde, J., Balboa, M. A., Li, W.-H., Llopis, J. L., & Dennis, E. A. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.10.5398 · Cited by 77
Activation of neutral sphingomyelinase in human neutrophils by polyunsaturated‘qc fatty acids
Robinson, B. S., Hii, C. S. T., Poulos, A., & Ferrante, A. (1997) · Immunology · doi:10.1046/j.1365-2567.1997.d01-2227.x · Cited by 77
Putative neuroprotective actions of N-acyl-ethanolamines
Hansen, H. S., Moesgaard, B., Petersen, G. L., & Hansen, H. H. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00251-6 · Cited by 73
Phospholipases of Mineralization Competent Cells and Matrix Vesicles: Roles in Physiological and Pathological Mineralizations
Mebarek, S., Abousalham, A., Magne, D., Do, L.-D., Bandorowicz‐Pikuła, J., Pikuła, S., & Buchet, R. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14035036 · Cited by 73
The role of lipids and protein kinase Cs in the pathogenesis of diabetic retinopathy
Curtis, T. M., & Scholfield, C. N. (2004) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.431 · Cited by 70
Modulation of phosphoinositide–protein kinase C signal transduction by omega-3 fatty acids: Implications for the pathophysiology and treatment of recurrent neuropsychiatric illness
McNamara, R. K., Ostrander, M. M., Abplanalp, W. A., Richtand, N. M., Benoit, S. C., & Clegg, D. J. (2006) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2006.07.009 · Cited by 70
Long‐chain polyunsaturated fatty acids and eicosanoids in infants‐physiological and pathophysiological aspects and open questions
Sellmayer, A., & Koletzko, B. V. (1999) · Lipids · doi:10.1007/s11745-999-0354-z · Cited by 69
Changes in essential fatty acid patterns associated with normal liver regeneration and the progression of hepatocyte nodules in rat hepatocarcinogenesis
Abel, S. (2001) · Carcinogenesis · doi:10.1093/carcin/22.5.795 · Cited by 68
The heterodimer of the Ca2+‐binding proteins MRP8 and MRP14 binds arachidonic acid
Klempt, M., Melkonyan, H., Nacken, W. K. F., Wiesmann, D., Holtkemper, U., & Sorg, C. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00394-3 · Cited by 68
Stimulation of GLP-1 Secretion Downstream of the Ligand-Gated Ion Channel TRPA1
Emery, E. C., Diakogiannaki, E., Gentry, C., Psichas, A., Habib, A. M., Bevan, S., Fischer, M. J. M., Reimann, F. M., & Gribble, F. M. (2014) · Diabetes · doi:10.2337/db14-0737 · Cited by 63
Mitochondrial oxidative stress is modulated by oleic acid via an epidermal growth factor receptor-dependent activation of glutathione peroxidase
Duval, C., Augè, N., Frisach, M., Casteilla, L., Salvayre, R., & Nègre‐Salvayre, A. (2002) · Biochemical Journal · doi:10.1042/bj20020625 · Cited by 67
Protein Kinases C Translocation Responses to Low Concentrations of Arachidonic Acid
O’Flaherty, J. T., Chadwell, B. A., Kearns, M. W., Sergeant, S., & Daniel, L. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101093200 · Cited by 64
Functional food science and the cardiovascular system
Hornstra, G., Barth, C. A., Galli, C. L., Mensink, R. P., Mutanen, M. L., Riemersma, R. A., Roberfroid, M. B., Salminen, K. R., Vansant, G. A. A. M., & Verschuren, P. M. (1998) · British Journal Of Nutrition · doi:10.1079/bjn19980107 · Cited by 63
SIGNAL TRANSDUCTION IN ENVIRONMENTAL NEUROTOXICITY
Costa, L. G. (1998) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.38.1.21 · Cited by 62
Arachidonic acid protects neonatal rat cardiac myocytes from ischaemic injury through ε protein kinase C
Mackay, K. (2001) · Cardiovascular Research · doi:10.1016/s0008-6363(00)00322-9 · Cited by 61
Identification and Characterization of a Novel Δ6/Δ5 Fatty Acid Desaturase Inhibitor As a Potential Anti-Inflammatory Agent
Obukowicz, M. G., Raz, A., Pyla, P. D., Rico, J. G., Wendling, J. M., & Needleman, P. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00665-5 · Cited by 56
Long Chain n-3 Polyunsaturated Fatty Acids in the Prevention of Allergic and Cardiovascular Disease
van den Elsen, L. W. J., Garssen, J., & Willemsen, L. E. M. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212800165960 · Cited by 55
Bioactive Lipid Signaling in Cardiovascular Disease, Development, and Regeneration
Wasserman, A. H., Venkatesan, M., & Aguirre, A. (2020) · Cells · doi:10.3390/cells9061391 · Cited by 50
Differential membrane binding and diacylglycerol recognition by C1 domains of RasGRPs
Johnson, J. E., Goulding, R. E., Ding, Z., Partovi, A., Anthony, K., Beaulieu, N., Tazmini, G., Cornell, R. B., & Kay, R. J. (2007) · Biochemical Journal · doi:10.1042/bj20070294 · Cited by 53
Phosphoproteomics identify arachidonic-acid-regulated signal transduction pathways modulating macrophage functions with implications for ovarian cancer
Dietze, R., Hammoud, M. K., Gómez‐Serrano, M., Unger, A., Bieringer, T., Finkernagel, F., Sokòl, A. M., Nist, A., Stiewe, T., Reinartz, S., et al. (2020) · Theranostics · doi:10.7150/thno.52442 · Cited by 54
Oleic Acid Inhibits Gap Junction Permeability and Increases Glucose Uptake in Cultured Rat Astrocytes
Lavado, E. M., Sánchez-Abarca, L. I., Tabernero, A., Bolaños, J. P., & Medina, J. M. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69020721.x · Cited by 52
Long-term effects of fatty acids on cell viability and gene expression of neonatal cardiac myocytes
van Bilsen, M., Vries, J. E. D., & Vusse, G. J. (1997) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/s0952-3278(97)90491-9 · Cited by 52
Protein kinase C
Marks, F., & Gschwendt, M. (1996) · doi:10.1002/9783527615032.ch3 · Cited by 52
Electrospray ionization mass spectrometry analyses of nuclear membrane phospholipid loss after reperfusion of ischemic myocardium
Williams, S. D., Hsu, F., & Ford, D. A. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)31991-x · Cited by 51
Novel, Selective Δ6 or Δ5 Fatty Acid Desaturase Inhibitors as Antiinflammatory Agents in Mice
Obukowicz, M. G., Welsch, D. J., Salsgiver, W. J., Martin-Berger, C. L., Chinn, K. S., Duffin, K. L., Raz, A., & Needleman, P. (1998) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)37776-6 · Cited by 50
Impaired NADPH oxidase activity in Rac2-deficient murine neutrophils does not result from defective translocation of p47phox and p67phox and can be rescued by exogenous arachidonic acid
Kim, C., & Dinauer, M. C. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0705371 · Cited by 49
Activation of phospholipase A2 in human neutrophils by polyunsaturated fatty acids and its role in stimulation of superoxide production
Robinson, B. S., Hii, C. S. T., & Ferrante, A. (1998) · Biochemical Journal · doi:10.1042/bj3360611 · Cited by 49
Unsaturated Fatty Acids Stimulate LH Secretion via Novel PKCε and -θ in Gonadotrope Cells and Inhibit GnRH-Induced LH Release
Garrel, G., Simon, V., Denoyelle, C., Cruciani‐Guglielmacci, C., Migrenne, S., Counis, R., Magnan, C., & Cohen-Tannoudji, J. (2011) · Endocrinology · doi:10.1210/en.2011-1167 · Cited by 48
Lipid peroxidation, arachidonic acid and products of the lipoxygenase pathway in ischaemic preconditioning of rat heart
Starkopf, J. (1998) · Cardiovascular Research · doi:10.1016/s0008-6363(97)00240-x · Cited by 48
Cellular Membrane Fluidity in Amyloid Precursor Protein Processing
Yang, X., Sun, G. Y., Eckert, G. P., & Lee, J. C. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8652-6 · Cited by 49
Arachidonic Acid Differentially Affects Basal and Lipopolysaccharide-Induced sPLA2-IIA Expression in Alveolar Macrophages through NF-κB and PPAR-γ–Dependent Pathways
Alaoui-El-Azher, M., Wu, Y., Havet, N., Israël, A., Lilienbaum, A., & Touqui, L. (2002) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12329-2 · Cited by 43
Arachidonic Acid Mediates Interferon-γ–Induced Sphingomyelin Hydrolysis and Monocytic Marker Expression in HL-60 Cell Line
Višnjić, D., Batinić, D., & Banfíƈ, H. (1997) · Blood · doi:10.1182/blood.v89.1.81 · Cited by 44
Regulation of Lipid Signaling Pathways for Cell Survival and Apoptosis by bcl-2 in Prostate Carcinoma Cells
Herrmann, J. L., Menter, D. G., Beham, A. W., von Eschenbach, A., & McDonnell, T. J. (1997) · Experimental Cell Research · doi:10.1006/excr.1997.3653 · Cited by 43
Involvement of Phosphatidylinositol 3′‐Kinase in Stem‐Cell‐Factor‐Induced Phospholipase D Activation and Arachidonic Acid Release
Kozawa, O., Blume‐Jensen, P., Heldin, C., & Rönnstrand, L. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00149.x · Cited by 43
Cooperative cobinding of synthetic and natural ligands to the nuclear receptor PPARγ
Shang, J., Brust, R., Mosure, S. A., Bass, J., Munoz‐Tello, P., Lin, H., Hughes, T., Tang, M., Ge, Q., Kamenekca, T. M., et al. (2018) · eLife · doi:10.7554/elife.43320 · Cited by 95
Peroxisome-proliferator-activated receptors and the control of levels of prostaglandin-endoperoxide synthase 2 by arachidonic acid in the bovine uterus
Sheldrick, E. L., Derecka, K., Marshall, E., Chin-Smith, E. C., Hodges, L., Wathes, D. C., Abayasekara, D. R. E., & Flint, A. P. F. (2007) · Biochemical Journal · doi:10.1042/bj20070089 · Cited by 40
Molecular and Signaling Mechanisms of Atherosclerosis in Insulin Resistance
Schwartz, E. A., & Reaven, P. D. (2006) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/j.ecl.2006.06.005 · Cited by 39
Arachidonic Acid Regulation of Intracellular Signaling Pathways and Target Gene Expression in Bovine Ovarian Granulosa Cells
Zhang, N., Wang, L., Luo, G., Tang, X., Ma, L., Zheng, Y., Liu, S., Price, C. A., & Jiang, Z. (2019) · Animals · doi:10.3390/ani9060374 · Cited by 37
Arachidonate-Induced Tyrosine Phosphorylation of Epidermal Growth Factor Receptor and Shc-Grb2-Sos Association
Dulin, N. O., Sorokin, A., & Douglas, J. G. (1998) · Hypertension · doi:10.1161/01.hyp.32.6.1089 · Cited by 36
Clinical concentrations of doxorubicin inhibit activity of myocardial membrane-associated, calcium-independent phospholipase A(2).
McHowat, J., Swift, L., Arutunyan, A. H., & Sarvazyan, N. A. (2001) · PubMed · Cited by 36
Central Role of Arachidonate 5-Lipoxygenase in the Regulation of Cell Growth and Apoptosis in Human Prostate Cancer Cells
Ghosh, J., & Myers, C. E. (1999) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4793-8_84 · Cited by 36
Impacts of Membrane Biophysics in Alzheimer′s Disease: From Amyloid Precursor Protein Processing to Aβ Peptide‐Induced Membrane Changes
Askarova, S., Yang, X., & Lee, J. C. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/134971 · Cited by 36
Effect of Dietary Lipids on Macrophage Function, Stress Susceptibility and Disease Esistance in Atlantic Salmon (Salmo salar)
Gjøen, T., Obach, A., Røsjø, C., Helland, B. G., Rosenlund, G., Hvattum, E., & Ruyter, B. (2004) · Fish Physiology and Biochemistry · doi:10.1007/s10695-005-4318-7 · Cited by 35
Eicosanoid Activation of Protein Kinase C ϵ
Mikule, K. W., Sunpaweravong, S., Gatlin, J. C., & Pfenninger, K. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211828200 · Cited by 33
Differential modulation of the lipid metabolism as a model for cellular resistance to fumonisin B1–induced cytotoxic effects in vitro
Riedel, S., Abel, S., Burger, H.-M., Westhuizen, L. V. D., Swanevelder, S. A., & Gelderblom, W. C. A. (2016) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2016.04.006 · Cited by 33
Calcium-dependence of synexin binding may determine aggregation and fusion of lamellar bodies
Sen, N., Spitzer, A. R., & Chander, A. (1997) · Biochemical Journal · doi:10.1042/bj3220103 · Cited by 33
Mechanisms of neuronal membrane sealing following mechanical trauma
Hendricks, B. K., & Shi, R. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1446-4 · Cited by 32
Phospholipid Profile and Distribution in the Receptive Oviduct and Uterus During Early Diestrus in Cattle
Belaz, K. R. A., Tata, A., França, M. R., da Silva, M. I. S., Vendramini, P. H., Fernandes, A. M. A. P., D’Alexandri, F. L., Eberlin, M. N., & Binelli, M. (2016) · Biology of Reproduction · doi:10.1095/biolreprod.116.142257 · Cited by 32

Authors: Khan, W. A., Blobe, G. C., & Hannun, Y. A.
Affiliations: Duke Medical Center (US)
Duke University (US)
Corresponding author: Khan, Wasiuddin A.
ORCID: Blobe, Gerard C.
Hannun, Yusuf A.
Venue: Cellular Signalling
Publisher: Elsevier BV
Published: 1995-03
Volume: 7
Issue: 3
Pages: 171-184
ISSN: 0898-6568 (ISSN-L)
DOI: 10.1016/0898-6568(94)00089-t
OpenAlex: W2002668908
Cited by: 225
References: 105
Citations by year: 2025: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 3 · 2018: 6 · 2017: 2 · 2016: 5 · 2015: 5 · 2014: 4 · 2013: 7 · 2012: 2
FWCI: 7.56
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cellular Signalling (publishedVersion)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (HL43707, R01HL043707)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Health Sciences › Nursing › Nutrition and Dietetics › Fatty Acid Research and Health
Keywords: arachidonic acid, free fatty acids, second messengers, protein kinase C, eicosanoids, fatty acid signaling
MeSH terms: Animals, Enzyme Activation, Fatty Acids, Nonesterified, Homeostasis, Humans, Models, Biological, Protein Kinase C, Second Messenger Systems, Eicosanoids, Arachidonic Acid

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Arachidonic acid and free fatty acids as second messengers and the role of protein kinase C

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks