LipidsVolume 55, Issue 1 p. 3-4 Editorial My Tenure as Editor-in-Chief of Lipids: What I Learned Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@ndus.edu Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, Grand Forks, ND, 58202-9037 USA Eric J. Murphy eric.murphy@ndus.eduSearch for more papers by this author Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@ndus.edu Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, Grand Forks, ND, 58202-9037 USA Eric J. Murphy eric.murphy@ndus.eduSearch for more papers by this author First published: 27 January 2020 https://doi.org/10.1002/lipd.12215Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume55, Issue1January 2020Pages 3-4 RelatedInformation

LipidsVolume 54, Issue 1 p. 3-4 Editorial Why We Care about Ethics and Ethical Publishing at Lipids Eric J. Murphy, Corresponding Author eric.murphy@ndus.edu Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, 1301 N. Columbia Rd., Grand Forks, ND 58201, USA Eric J. Murphy eric.murphy@ndus.eduSearch for more papers by this author Eric J. Murphy, Corresponding Author eric.murphy@ndus.edu Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, 1301 N. Columbia Rd., Grand Forks, ND 58201, USA Eric J. Murphy eric.murphy@ndus.eduSearch for more papers by this author First published: 18 February 2019 https://doi.org/10.1002/lipd.12129Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinked InRedditWechat No abstract is available for this article. Volume54, Issue1January 2019Pages 3-4 RelatedInformation

LipidsVolume 52, Issue 7 p. 573-574 Editorial An Ethical Dilemma: To Share or Not To Share Your Paper Published in Lipids Using an On-Line Outlet Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, 1301 N. Columbia Rd., Grand Forks, ND, 58202-9037 USA 1-701-777-3450 eric.murphy@med.und.eduSearch for more papers by this author Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, 1301 N. Columbia Rd., Grand Forks, ND, 58202-9037 USA 1-701-777-3450 eric.murphy@med.und.eduSearch for more papers by this author First published: 12 June 2017 https://doi.org/10.1007/s11745-017-4268-8Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume52, Issue7July 2017Pages 573-574 RelatedInformation

Emerging evidence indicates that the fatty acid composition of obesogenic diets influences physiologic outcomes. There are scant data regarding how the content of non-essential fatty acids like monounsaturated fatty acids (MUFA) and saturated fatty acids (SFAs) impact the metabolism of polyunsaturated fatty acids (PUFAs). In this work, we tested the hypothesis that obesogenic diets enriched in oleic acid (OA; 18:1n-9) reduce polyunsaturated fatty acid (PUFA) levels vs an obesogenic diet enriched in SFAs. Adult male mice were fed for eight weeks either (1) a control 16% fat energy (en) diet with 5.7% en OA and 4.4% en SFA, (2) a 50% fat en diet with 33% en OA and 9.9% en SFA, or (3) a 50% en diet with a high SFA diet with 33% en SFA and 9.1% en OA. Dietary levels and intake of linoleic acid (LA; 18:2n-6) and α-linolenic acid (ALA; 18:3n-3) were constant between the experimental groups. Several peripheral organs (liver, heart, kidney, and adipose) were analyzed for lipid composition and oxylipin analysis was performed for liver and adipose. Our data demonstrate that a high OA diet reduced tissue content of LA and ALA (≥30%) in phospholipid and neutral lipid fractions, reduced the content of some LA-derived and ALA-derived oxylipins in liver and adipose, and conversely, elevated hepatic content of PGF2α. In all tissues examined, except for adipose, levels of arachidonic acid (ARA; 20:4n-6) and docosahexaenoic acid (DHA; 22:6n-3) were either elevated or unaffected by the obesogenic diets. Our data indicate that the non-essential fatty content of obesogenic diets impacts PUFA content in peripheral tissues and influences the levels of bioactive oxylipins.

LipidsVolume 51, Issue 2 p. 149-150 Editorial A New Era for Lipids: Introduction of Rapid Communications Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu Department of Basic Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Rd, Grand Forks, ND, 58202-9037 USA 701-777-3450 eric.murphy@med.und.eduSearch for more papers by this author Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu Department of Basic Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Rd, Grand Forks, ND, 58202-9037 USA 701-777-3450 eric.murphy@med.und.eduSearch for more papers by this author First published: 27 January 2016 https://doi.org/10.1007/s11745-016-4126-0Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume51, Issue2February 2016Pages 149-150 RelatedInformation

C57BL/6 and Swiss Webster mice are used to study lipid metabolism, although differences in fatty acid uptake between these strains have not been reported. Using a steady state kinetic model, [1- 14 C]16:0, [1- 14 C]20:4n-6, or [1- 14 C]22:6n-3 was infused into awake, adult male mice and uptake into liver, heart, and brain determined. The integrated area of [1- 14 C]20:4n-6 in plasma was significantly increased in C57BL/6 mice, but [1- 14 C]16:0 and [1- 14 C]22:6n-3 were not different between groups. In heart, uptake of [1- 14 C]20:4n-6 was increased 1.7-fold in C57BL/6 mice. However, trafficking of [1- 14 C]22:6n-3 into the organic fraction of heart was significantly decreased 33 % in C57BL/6 mice. Although there were limited differences in fatty acid tracer trafficking in liver or brain, [1- 14 C]16:0 incorporation into liver neutral lipids was decreased 18 % in C57BL/6 mice. In heart, the amount of [1- 14 C]16:0 and [1- 14 C]22:6n-3 incorporated into total phospholipids were decreased 45 and 49 %, respectively, in C57BL/6 mice. This was accounted for by a 53 and 37 % decrease in [1- 14 C]16:0 and 44 and 52 % decrease in [1- 14 C]22:6n-3 entering ethanolamine glycerophospholipids and choline glycerophospholipids, respectively. In contrast, there was a significant increase in [1- 14 C]20:4n-6 esterification into all heart phospholipids of C57BL/6 mice. Although changes in uptake were limited to heart, several significant differences were found in fatty acid trafficking into heart, liver, and brain phospholipids. In summary, our data demonstrates differences in tissue fatty acid uptake and trafficking between mouse strains is an important consideration when carrying out fatty acid metabolic studies.

Astrocytes play a vital role in brain lipid metabolism; however the impact of the phenotypic shift in astrocytes to a reactive state on arachidonic acid metabolism is unknown. Therefore, we determined the impact of dibutyryl-cAMP (dBcAMP) treatment on radiolabeled arachidonic acid ([1-(14)C]20:4n-6) and palmitic acid ([1-(14)C]16:0) uptake and metabolism in primary cultured murine cortical astrocytes. In dBcAMP treated astrocytes, total [1-(14)C]20:4n-6 uptake was increased 1.9-fold compared to control, while total [1-(14)C]16:0 uptake was unaffected. Gene expression of long-chain acyl-CoA synthetases (Acsl), acyl-CoA hydrolase (Acot7), fatty acid binding protein(s) (Fabp) and alpha-synuclein (Snca) were determined using qRT-PCR. dBcAMP treatment increased expression of Acsl3 (4.8-fold) and Acsl4 (1.3-fold), which preferentially use [1-(14)C]20:4n-6 and are highly expressed in astrocytes, consistent with the increase in [1-(14)C]20:4n-6 uptake. However, expression of Fabp5 and Fabp7 were significantly reduced by 25% and 45%, respectively. Acot7 (20%) was also reduced, suggesting dBcAMP treatment favors acyl-CoA formation. dBcAMP treatment enhanced [1-(14)C]20:4n-6 (2.2-fold) and [1-(14)C]16:0 (1.6-fold) esterification into total phospholipids, but the greater esterification of [1-(14)C]20:4n-6 is consistent with the observed uptake through increased Acsl, but not Fabp expression. Although total [1-(14)C]16:0 uptake was not affected, there was a dramatic decrease in [1-(14)C]16:0 in the free fatty acid pool as esterification into the phospholipid pool was increased, which is consistent with the increase in Acsl3 and Acsl4 expression. In summary, our data demonstrates that dBcAMP treatment increases [1-(14)C]20:4n-6 uptake in astrocytes and this increase appears to be due to increased expression of Acsl3 and Acsl4 coupled with a reduction in Acot7 expression.

LipidsVolume 51, Issue 5 p. 505-506 Editorial Northern Great Plains Lipid Conference: An International Conference Coalescing the Lipid Scientists in the Northern Great Plains Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Road, Room 3700, Grand Forks, ND, 58202-9037 USA 701-777-3450 eric.murphy@med.und.eduSearch for more papers by this author Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Road, Room 3700, Grand Forks, ND, 58202-9037 USA 701-777-3450 eric.murphy@med.und.eduSearch for more papers by this author First published: 13 April 2016 https://doi.org/10.1007/s11745-016-4151-zRead the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume51, Issue5Proceedings of the Northern Great Plains Lipid ConferenceMay 2016Pages 505-506 RelatedInformation

Considerable research has focused upon the role of linoleic acid (LNA; 18:2n-6) as a competitive inhibitor of α-linolenic (ALA; 18:3n-3) metabolism; however, little data exist as to the impact of saturated fatty acids (SFA) and monounsaturated fatty acids (MUFA) on ALA metabolism. We tested the hypothesis that a high SFA diet, compared to a high MUFA (oleic acid 18:1n-9) diet, reduces ALA conversion to long chain n-3 fatty acids. Mice were fed for 12 weeks on three diets: (1) a control, 16 % fat energy diet consisting of similar levels of SFA and MUFA (2) a 50 % fat energy high MUFA energy diet (35 % MUFA and 7 % SFA) or (3) a 50 % fat energy, high SFA energy diet (34 % SFA, 8 % MUFA). ALA and LNA content remained constant. Analysis of hepatic lipids demonstrated a selective reduction (40 %) in ALA but not LNA and a 35 % reduction in eicosapentaenoic acid (EPA; 20:5n-3) in the high MUFA mice compared to the other groups. Lower content of ALA was reflected in the neutral lipid fraction, while smaller levels of phospholipid esterified EPA and docosapentaenoic acid (DPA; 22:5n-3) were evident. Docosahexaenoic acid (DHA; 22:6n-3) content was elevated by the high SFA diet. Expression of Fads1 (Δ5 desaturase) and Fads2 (Δ6 desaturase) was elevated by the high MUFA and reduced by the high SFA diet. These data indicate that a high MUFA diet, but not a high SFA diet, reduces ALA metabolism and point to selective hepatic disposition of ALA versus LNA.

The first discovered member of the mammalian FABP family, liver fatty acid binding protein (FABP1, L-FABP), occurs at high cytosolic concentration in liver, intestine, and in the case of humans also in kidney. While the rat FABP1 is well studied, the extent these findings translate to human FABP1 is not clear—especially in view of recent studies showing that endocannabinoids and cannabinoids represent novel rat FABP1 ligands and FABP1 gene ablation impacts the hepatic endocannabinoid system, known to be involved in non-alcoholic fatty liver (NAFLD) development. Although not detectable in brain, FABP1 ablation nevertheless also impacts brain endocannabinoids. Despite overall tertiary structure similarity, human FABP1 differs significantly from rat FABP1 in secondary structure, much larger ligand binding cavity, and affinities/specificities for some ligands. Moreover, while both mouse and human FABP1 mediate ligand induction of peroxisome proliferator activated receptor-α (PPARα), they differ markedly in pattern of genes induced. This is critically important because a highly prevalent human single nucleotide polymorphism (SNP) (26–38 % minor allele frequency and 8.3 ± 1.9 % homozygous) results in a FABP1 T94A substitution that further accentuates these species differences. The human FABP1 T94A variant is associated with altered body mass index (BMI), clinical dyslipidemias (elevated plasma triglycerides and LDL cholesterol), atherothrombotic cerebral infarction, and non-alcoholic fatty liver disease (NAFLD). Resolving human FABP1 and the T94A variant’s impact on the endocannabinoid and cannabinoid system is an exciting challenge due to the importance of this system in hepatic lipid accumulation as well as behavior, pain, inflammation, and satiety.

LipidsVolume 50, Issue 1 p. 1-2 Editorial Lipids: 50th Anniversary Celebration and the Future Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu 701-777-3450 Department of Basic Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Rd., Grand Forks, ND, 58202-9037 USAeric.murphy@med.und.eduSearch for more papers by this author Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu 701-777-3450 Department of Basic Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Rd., Grand Forks, ND, 58202-9037 USAeric.murphy@med.und.eduSearch for more papers by this author First published: 01 January 2018 https://doi.org/10.1007/s11745-014-3986-4Citations: 3Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article.Citing Literature Volume50, Issue1January 2015Pages 1-2 RelatedInformation

LipidsVolume 50, Issue 12 p. 1165-1166 Editorial The Importance of Ethical Peer-Review: Why Do We Ask Authors to Suggest Reviewers Anyway? Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu Department of Basic Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Rd., Room 3700, Grand Forks, ND, 58202-9037 USA 701-777-3450 eric.murphy@med.und.eduSearch for more papers by this author Eric J. Murphy, Corresponding Author Eric J. Murphy eric.murphy@med.und.edu Department of Basic Sciences, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Rd., Room 3700, Grand Forks, ND, 58202-9037 USA 701-777-3450 eric.murphy@med.und.eduSearch for more papers by this author First published: 17 November 2015 https://doi.org/10.1007/s11745-015-4094-9Citations: 5Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article.Citing Literature Volume50, Issue12December 2015Pages 1165-1166 RelatedInformation

EssentialsAntithrombin III (AT) binds heparin with higher affinity than AT. A conformation-specific antibody against AT, TPP2009, was made to investigate AT in hemostasis. TPP2009 bound specifically to heparin-AT and greatly reduced the anticoagulant effect of AT. This antibody was effective in elucidating the importance of AT in hemostasis.SummaryBackground Antithrombin III (AT) is an isoform of AT that lacks the post-translational carbohydrate modification at Asn135. This isoform binds heparin with greater affinity than AT, and has been shown to target antithrombotic function to the extracellular vascular endothelial injury site.Objectives To characterize a conformation-specific antibody against AT and begin to investigate the role of AT in maintaining hemostasis.Methods Surface plasmon resonance (SPR), antigen binding and functional assays were conducted to characterize the mode of action of antibodies generated against heparin-bound AT (AT*H) by the use of phage display.Results SPR and binding studies showed that one of the antibodies, TPP2009, bound specifically to AT*H and glycosaminoglycan-associated AT on endothelial cells. In diluted prothrombin and activated factor X (FXa)-induced clotting assays, TPP2009 dose-dependently reduced the anticoagulant effect of heparin in non-hemophilic and FVIII-deficient human plasma, with half-maximal effective concentrations (EC50) of 10.5 nm and 4.7 nm, respectively. In AT-deficient human plasma, TPP2009 dose-dependently inhibited the effects of exogenously added AT and heparin. In purified systems with AT and pentasaccharide, TPP2009 restored > 91% of FXa activity. TPP2009 dose-dependently reversed the effects of heparin in rabbit (EC50, 25.7 nm) and cynomolgus monkey (EC50, 21.5 nm) plasma, but not in mouse plasma. TPP2009 was also effective in partially restoring FXa activity in rabbit and cynomolgus monkey plasma treated with FVIII function-neutralizing antibodies.Conclusions TPP2009 specifically targets a unique conformational epitope on AT*H and blocks AT-mediated anticoagulation. It effectively promotes coagulation in plasma, indicating the importance of AT in hemostasis.

SummaryPatients with haemophilia (PWH) are usually monitored by the one‐stage activated partial thromboplastin time (aPTT) factor VIII (FVIII) assay. Different aPTT activators may affect clotting time (CT) and FVIII:C levels in patients treated with PEGylated FVIII. To evaluate the characteristics of PEGylated FVIII (BAY 94‐9027) in various aPTT clotting assays, and to identify suitable aPTT reagents for monitoring BAY 94‐9027 during the treatment of PWH, BAY 94‐9027 and World Health Organization (WHO) 8th FVIII standards (WHO‐8) were spiked into pooled and individual severe haemophilia A plasma at 1.0, 0.25 and 0.05 IU mL−1. Five commercial aPTT reagents widely used in clinical laboratories were compared and evaluated for BAY 94‐9027 activity in plasma from PWH. BAY 94‐9027 and WHO‐8 bestowed similar CT and excellent precision when ellagic acid (SynthAFax, Dade Actin, and Cephascreen) aPTT reagents were used. In contrast, BAY 94‐9027 showed significantly prolonged CT and poor precision compared with WHO‐8 using silica aPTT reagents (APTT‐SP and STA PTT 5). Furthermore, free 60‐kDa polyethylene glycol (PEG), used for the conjugation of FVIII, showed a dose‐dependent prolongation of CT in the APTT‐SP assay. There was no effect on the SynthAFax‐APTT, prothrombin time, or FXIa‐initiated thrombin generation assay, demonstrating that the PEG moiety on FVIII has no general effect on the coagulation cascade. In summary, ellagic aPTT reagents (SynthAFax, Dade Actin, and Cephascreen) are most suitable for evaluating potency of BAY 94‐9027 and should be the preferred aPTT reagents used in clinical laboratories for monitoring FVIII activity after infusion of BAY 94‐9027 to PWH.

LipidsVolume 48, Issue 1 p. 1-2 Editorial Scientific Misconduct and Lipids: A View from an Editor-in-Chief Eric J. Murphy, Corresponding Author Eric J. Murphy [email protected] Department of Pharmacology, Physiology, and Therapeutics, University of North Dakota, Grand Forks, ND, 58202-9037 USA[email protected]Search for more papers by this author Eric J. Murphy, Corresponding Author Eric J. Murphy [email protected] Department of Pharmacology, Physiology, and Therapeutics, University of North Dakota, Grand Forks, ND, 58202-9037 USA[email protected]Search for more papers by this author First published: 01 January 2018 https://doi.org/10.1007/s11745-012-3743-5Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume48, Issue1January 2013Pages 1-2 RelatedInformation

Read the full article ‘Unesterified docosahexaenoic acid is protective in neuroinflammation’ on doi: 10.1111/jnc.12392.