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Artykuły w czasopismach na temat „Stearoyl CoA desaturase”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 25 kwietnia 2022

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1

Oatman, Nicole, Julie Reisz, Angelo D’Alessandro, and Biplab Dasgupta. "TAMI-55. THE EVOLUTIONARY ENIGMA OF FATTY ACID DESATURATION IN GLIOBLASTOMA." Neuro-Oncology 22, Supplement_2 (November 2020): ii225. http://dx.doi.org/10.1093/neuonc/noaa215.942.

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Abstract Fatty acid desaturation is an enzymatic reaction in which a double bond is introduced into an acyl chain. Of the four functionally distinct desaturase subfamilies, the First Desaturase Family of enzymes introduce the first double bond into a saturated fatty acid, resulting in the synthesis of monounsaturated fatty acids (MUFA). MUFA are essential components of membrane and storage lipids and exert a profound influence on the fluidity of biological membranes. A disequilibrium in saturated to unsaturated fatty acid ratio alters cell growth, differentiation and response to external stimuli, and thus affects a range of pathologies including cancer. The most abundant and key First Desaturase Family enzyme is the delta 9 desaturate called Stearoyl Co-A Desaturase (SCD and SCD5 in humans, and SCD1-4 in mice). SCD desaturates Stearoyl-CoA (C18) and palmitoyl-CoA (C16) to oleoyl-CoA (C18:1) and palmitoyl-CoA (C16:1), respectively. Besides SCD, the only known First Desaturase in mammals with dual function is FADS2 which desaturates palmitate to Sapienate (C16:1, a positional isomer of palmitoleate) in skin cells. A recent study showed that some cancer cells can use FADS2 to bypass the SCD reaction. SCD and SCD5 are by far the most abundant desaturases expressed in the human brain. We made an unexpected discovery that SCD undergoes monoallelic codeletion with PTEN on chromosome 10, and is also highly methylated in glioblastoma (GBM). More surprisingly, all GBM cell lines with SCD codeletion/methylation (that expressed very little SCD protein) are completely resistant to SCD/SCD5 inhibition, yet their phospholipids contained abundant oleic acid. It is unknown if GBMs bypassed SCD, but retained the delta 9 desaturation reaction through a novel enzymatic activity. Our targeted and untargeted metabolomics studies revealed unexpected findings that cannot be explained by conventional wisdom, and may lead to identification of novel lipogenic targets in GBM.

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2

Oatman, Nicole, and Biplab Dasgupta. "DDRE-15. THE EVOLUTIONARY ENIGMA OF FATTY ACID DESATURATION IN GLIOBLASTOMA." Neuro-Oncology Advances 3, Supplement_1 (March 1, 2021): i9. http://dx.doi.org/10.1093/noajnl/vdab024.037.

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Abstract Fatty acid desaturation is an enzymatic reaction in which a double bond is introduced into an acyl chain. Of the four functionally distinct desaturase subfamilies, the First Desaturase Family of enzymes introduce the first double bond into a saturated fatty acid, resulting in the synthesis of monounsaturated fatty acids (MUFA). MUFA are essential components of membrane and storage lipids and exert a profound influence on the fluidity of biological membranes. A disequilibrium in saturated to unsaturated fatty acid ratio alters cell growth, differentiation and response to external stimuli, and thus affects a range of pathologies including cancer. The most abundant and key First Desaturase Family enzyme is the delta 9 desaturate called Stearoyl Co-A Desaturase (SCD and SCD5 in humans, and SCD1-4 in mice). SCD desaturates Stearoyl-CoA (C18) and palmitoyl-CoA (C16) to oleoyl-CoA (C18:1) and palmitoyl-CoA (C16:1), respectively. Besides SCD, the only known First Desaturase in mammals with dual function is FADS2 which desaturates palmitate to Sapienate (C16:1, a positional isomer of palmitoleate) in skin cells. A recent study showed that some cancer cells can use FADS2 to bypass the SCD reaction. SCD and SCD5 are by far the most abundant desaturases expressed in the human brain. We made an unexpected discovery that SCD undergoes monoallelic codeletion with PTEN on chromosome 10, and is also highly methylated in glioblastoma (GBM). More surprisingly, all GBM cell lines with SCD codeletion/methylation (that expressed very little SCD protein) are completely resistant to SCD/SCD5 inhibition, yet their phospholipids contained abundant oleic acid. It is unknown if GBMs bypassed SCD, but retained the delta 9 desaturation reaction through a novel enzymatic activity. Our targeted and untargeted metabolomics studies revealed unexpected findings that cannot be explained by conventional wisdom, and may lead to identification of novel lipogenic targets in GBM.

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3

Kawashima, Y., N. Uy-Yu, and H. Kozuka. "Sex-related differences in the enhancing effects of perfluoro-octanoic acid on stearoyl-CoA desaturase and its influence on the acyl composition of phospholipid in rat liver. Comparison with clofibric acid and tiadenol." Biochemical Journal 263, no. 3 (November 1, 1989): 897–904. http://dx.doi.org/10.1042/bj2630897.

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The effects of the peroxisome proliferators clofibric acid (p-chlorophenoxyisobutyric acid), tiadenol [2,2′-(decamethylenedithio)diethanol] and perfluoro-octanoic acid (PFOA) on hepatic stearoyl-CoA desaturation in male and female rats were compared. Treatment of male rats with the three peroxisome proliferators increased markedly the activity of stearoyl-CoA desaturase. Administration of clofibric acid or tiadenol to female rats increased greatly the hepatic activity of stearoyl-CoA desaturase, the extent of the increases being slightly less pronounced than those of male rats. In contrast with the other two peroxisome proliferators, however, PFOA did not change the activity of stearoyl-CoA desaturase in female rats. Hormonal manipulations revealed that this sex-related difference in the effect of PFOA on stearoyl-CoA desaturase activity is strongly dependent on testosterone. The increase in stearoyl-CoA desaturase activity by peroxisome proliferators was not accompanied by any notable increases in the microsomal content of cytochrome b5 or the activity of NADH: cytochrome b5 reductase. The administration of the peroxisome proliferators greatly altered the acyl composition of hepatic phosphatidylcholine and phosphatidylethanolamine (namely the proportions of C18:1 and C20:3,n-9 fatty acids increased in both phospholipids), and the alterations were partially associated with the increase in stearoyl-CoA desaturase activity.

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4

Kikuchi, Kohtaro, and Hidekazu Tsukamoto. "Stearoyl-CoA desaturase and tumorigenesis." Chemico-Biological Interactions 316 (January 2020): 108917. http://dx.doi.org/10.1016/j.cbi.2019.108917.

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5

Lu, He, Xin Qin, Jing Zhang, Shuang Zhang, Yu Zhu, and Wei Hua Wu. "Molecular target analysis of stearoyl-CoA desaturase genes of protozoan parasites." Acta Parasitologica 63, no. 1 (March 26, 2018): 48–54. http://dx.doi.org/10.1515/ap-2018-0006.

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AbstractProtozoan parasites can synthesize polyunsaturated fatty acids. They possess stearoyl-CoA desaturase to convert stearate into oleate and linoleate. Stearoyl-CoA desaturase are the key enzymes required for the synthesis of unsaturated fatty acids. It seems attractive to evaluate the possibility of using unsaturated fatty acid biosynthesis pathways as drug targets. In this study, the authors investigate codon usage bias, base composition variations and protein sequence in ten available complete stearoyl-CoA desaturase gene sequences fromToxoplasma gondii,Neospora caninumetc. The results show that fatty acid desaturase genes GC content high of parasitic protozoa genes, GC content up to 63.37%, while fatty acid desaturase genes of parasitic protozoa prefers to use codon ending with G/C. In addition, the expected curve was also drawn to reveal the relationship of ENC and GC3s when the codon usage was only subjected to the nucleotide composition constraint. The genes lied on the expected curve in ENC-plot, indicating nucleotide composition constraint played a role in the condon usage pattern. Protein analysis, we find that all proteins are stearoyl-CoA desaturase, have sites of iron-binding active centers and contain three conserved His-rich motifs. If stearoyl-CoA desaturase is unusual to these parasites, it provides basis as a promising target for the development of selective chemical intervention. Therefore, the Bioinformatics analysis of protein and codon can help improve the work of genetic engineering and drug screening.

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6

Hao, Pan, Xia Cui, Jing Liu, Muzi Li, Yong Fu, and Qun Liu. "Identification and characterization of stearoyl-CoA desaturase in Toxoplasma gondii." Acta Biochimica et Biophysica Sinica 51, no. 6 (May 29, 2019): 615–26. http://dx.doi.org/10.1093/abbs/gmz040.

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Abstract Few information of the function of stearoyl-coenzyme A (CoA) desaturase (SCD) in apicomplaxan parasite has been obtained. In this study, we retrieved a putative fatty acyl-CoA desaturase (TGGT1_238950) by a protein alignment with Plasmodium falciparum SCD in ToxoDB. A typical Δ9-desaturase domain was revealed in this protein. The putative desaturase was tagged with HA endogenously in Toxoplasma gondii, and the endoplasmic reticulum localization of the putative desaturase was revealed, which was consistent with the fatty acid desaturases in other organisms. Therefore, the TGGT1_238950 was designated T. gondii SCD. Based on CRISPR/Cas9 gene editing technology, SCD conditional knockout mutants in the T. gondii TATi strain were obtained. The growth in vitro and pathogenicity in mice of the mutants suggested that SCD might be dispensable for tachyzoite growth and proliferation. The SCD-overexpressing line was constructed to further explore SCD function. The portion of palmitoleic acid and oleic acid were increased in SCD-overexpressing parasites, compared with the RH parental strain, indicating that T. gondii indeed is competent for unsaturated fatty acid synthesis. The SCD-overexpressing tachyzoites propagated slower than the parental strain, with a decreased invasion capability and weaker pathogenicity in mice. The TgIF2α phosphorylation and the expression changes of several genes demonstrated that ER stress was triggered in the SCD-overexpressing parasites, which were more apt toward autophagy and apoptosis. The function of unsaturated fatty acid synthesis of TgSCD was consistent with our hypothesis. On the other hand, SCD might also be involved in tachyzoite autophagy and apoptosis.

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7

Ntambi, James M., Makoto Miyazaki, and Agnieszka Dobrzyn. "Regulation of stearoyl-CoA desaturase expression." Lipids 39, no. 11 (November 2004): 1061–65. http://dx.doi.org/10.1007/s11745-004-1331-2.

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8

Ntambi, James M., Youngjin Choi, Yeonhwa Park, Jeffrey M. Peters, and Michael W. Pariza. "Effects of Conjugated Linoleic Acid (CLA) on Immune Responses, Body Composition and Stearoyl-CoA Desaturase." Canadian Journal of Applied Physiology 27, no. 6 (December 1, 2002): 617–27. http://dx.doi.org/10.1139/h02-036.

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Conjugated linoleic acid (CLA) has shown a wide range of biologically beneficial effects; reduction of incidence and severity of animal carcinogenesis, reduction of the adverse effects of immune stimulation, reduction of severity of atherosclerosis, growth promotion in young rats, and modulation of stearoyl-CoA desaturase (SCD). One of the most interesting aspects of CLA is its ability to reduce body fat while enhancing lean body mass which is associated with the trans-10,cis-12 isomer of CLA. The effects of CLA are unique characteristics that have not been observed with other polyunsaturated fatty acids. In this review, we will focus on the effects of CLA on immune responses, body compositional changes and stearoyl-CoA desaturase. Key words:trans-10,cis-12 CLA

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9

Sæther, Thomas, Thien N. Tran, Helge Rootwelt, Bjørn O. Christophersen та Trine B. Haugen. "Expression and Regulation of Δ5-Desaturase, Δ6-Desaturase, Stearoyl-Coenzyme A (CoA) Desaturase 1, and Stearoyl-CoA Desaturase 2 in Rat Testis". Biology of Reproduction 69, № 1 (1 липня 2003): 117–24. http://dx.doi.org/10.1095/biolreprod.102.014035.

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10

Murphy, D. J., I. E. Woodrow, and K. D. Mukherjee. "Substrate specificities of the enzymes of the oleate desaturase system from photosynthetic tissue." Biochemical Journal 225, no. 1 (January 1, 1985): 267–70. http://dx.doi.org/10.1042/bj2250267.

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In the microsomal fraction from young pea (Pisum sativum L.) leaves, the oleoyl moieties from oleoyl-CoA are principally transferred to the sn-2 position of phosphatidylcholine by oleoyl-CoA:1-acyl-lysophosphatidylcholine acyltransferase. The major product of this acyl transfer is 1-palmitoyl(stearoyl)-2-oleoyl phosphatidylcholine. The 1-palmitoyl(stearoyl)-2-oleoyl phosphatidylcholine is subsequently converted into 1-palmitoyl(stearoyl)-2-linoleoyl phosphatidylcholine by the oleate desaturase complex without equilibrating with the bulk membrane phosphatidylcholine pool. Hence, both the acyl transfer to phosphatidylcholine and the subsequent desaturation of oleoyl moieties occur on the sn-2 position of phosphatidylcholine, and there is also a functional coupling of the acyltransferase and oleate desaturase.

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11

Kucharski, Mirosław, and Urszula Kaczor. "Stearoyl-CoA desaturase – the lipid metabolism regulator." Postępy Higieny i Medycyny Doświadczalnej 68 (March 27, 2014): 334–42. http://dx.doi.org/10.5604/17322693.1095856.

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12

Hodson, Leanne, and Barbara A. Fielding. "Stearoyl-CoA desaturase: rogue or innocent bystander?" Progress in Lipid Research 52, no. 1 (January 2013): 15–42. http://dx.doi.org/10.1016/j.plipres.2012.08.002.

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13

Tebbey, Paul W., and Thomas M. Buttke. "Stearoyl-CoA desaturase gene expression in lymphocytes." Biochemical and Biophysical Research Communications 186, no. 1 (July 1992): 531–36. http://dx.doi.org/10.1016/s0006-291x(05)80840-x.

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14

Ntambi, James M., and Makoto Miyazaki. "Recent insights into stearoyl-CoA desaturase-1." Current Opinion in Lipidology 14, no. 3 (June 2003): 255–61. http://dx.doi.org/10.1097/00041433-200306000-00005.

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15

Ntambi, James M. "The regulation of stearoyl-CoA desaturase (SCD)." Progress in Lipid Research 34, no. 2 (January 1995): 139–50. http://dx.doi.org/10.1016/0163-7827(94)00010-j.

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16

Cai, Yuanheng, Xiao-Hong Yu, Jin Chai, Chang-Jun Liu та John Shanklin. "A conserved evolutionary mechanism permits Δ9 desaturation of very-long-chain fatty acyl lipids". Journal of Biological Chemistry 295, № 32 (11 червня 2020): 11337–45. http://dx.doi.org/10.1074/jbc.ra120.014258.

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Δ9 fatty acyl desaturases introduce a cis–double bond between C9 and C10 of saturated fatty acyl chains. From the crystal structure of the mouse stearoyl-CoA desaturase (mSCD1) it was proposed that Tyr-104, a surface residue located at the distal end of the fatty acyl binding pocket plays a key role in specifying 18C selectivity. We created mSCD1-Y104G to test the hypothesis that eliminating this bulky side chain would create an opening and permit the substrate's methyl end to protrude through the enzyme into the lipid bilayer, facilitating the desaturation of very-long-chain (VLC) substrates. Consistent with this hypothesis, Y104G acquired the ability to desaturate 24C and 26C acyl-CoAs while maintaining its Δ9-regioselectivity. We also investigated two distantly related very-long-chain fatty acyl (VLCFA) desaturases from Arabidopsis, ADS1.2 and ADS1.4, which have Ala and Gly, respectively, in place of the gatekeeping Tyr found in mSCD1. Substitution of Tyr for Ala and Gly in ADS1.2 and ADS1.4, respectively, blocked their ability to desaturate VLCFAs. Further, we identified a pair of fungal desaturase homologs which contained either an Ile or a Gly at this location and showed that only the Gly-containing desaturase was capable of very-long-chain desaturation. The conserved desaturase architecture wherein a surface residue with a single bulky side chain forms the end of the substrate binding cavity predisposes them to single amino acid substitutions that enable a switch between long- and very-long-chain selectivity. The data presented here show that such changes have independently occurred multiple times during evolution.

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17

O’Neill, Lucas M., Chang-An Guo, Fang Ding, Yar Xin Phang, Zhaojin Liu, Sohel Shamsuzzaman, and James M. Ntambi. "Stearoyl-CoA Desaturase-2 in Murine Development, Metabolism, and Disease." International Journal of Molecular Sciences 21, no. 22 (November 16, 2020): 8619. http://dx.doi.org/10.3390/ijms21228619.

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Stearoyl-CoA Desaturase-2 (SCD2) is a member of the Stearoyl-CoA Desaturase (SCD) family of enzymes that catalyze the rate-limiting step in monounsaturated fatty acid (MUFA) synthesis. The MUFAs palmitoleoyl-CoA (16:1n7) and oleoyl-CoA (18:1n9) are the major products of SCD2. Palmitoleoyl-CoA and oleoyl-CoA have various roles, from being a source of energy to signaling molecules. Under normal feeding conditions, SCD2 is ubiquitously expressed and is the predominant SCD isoform in the brain. However, obesogenic diets highly induce SCD2 in adipose tissue, lung, and kidney. Here we provide a comprehensive review of SCD2 in mouse development, metabolism, and various diseases, such as obesity, chronic kidney disease, Alzheimer′s disease, multiple sclerosis, and Parkinson′s disease. In addition, we show that bone mineral density is decreased in SCD2KO mice under high-fat feeding conditions and that SCD2 is not required for preadipocyte differentiation or the expression of PPARγ in vivo despite being required in vitro.

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18

Paton, Chad M., and James M. Ntambi. "Biochemical and physiological function of stearoyl-CoA desaturase." American Journal of Physiology-Endocrinology and Metabolism 297, no. 1 (July 2009): E28—E37. http://dx.doi.org/10.1152/ajpendo.90897.2008.

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A key and highly regulated enzyme that is required for the biosynthesis of monounsaturated fatty acids is stearoyl-CoA desaturase (SCD), which catalyzes the D9- cis desaturation of a range of fatty acyl-CoA substrates. The preferred substrates are palmitoyl- and stearoyl-CoA, which are converted into palmitoleoyl- and oleoyl-CoA respectively. Oleate is the most abundant monounsaturated fatty acid in dietary fat and is therefore readily available. Studies of mice that have a naturally occurring mutation in the SCD-1 gene isoform as well as a mouse model with a targeted disruption of the SCD gene (SCD-1−/−) have revealed the role of de novo synthesized oleate and thus the physiological importance of SCD-1 expression. SCD-1 deficiency results in reduced body adiposity, increased insulin sensitivity, and resistance to diet-induced obesity. The expression of several genes of lipid oxidation are upregulated, whereas lipid synthesis genes are downregulated. SCD-1 was also found to be a component of the novel metabolic response to the hormone leptin. Therefore, SCD-1 appears to be an important metabolic control point, and inhibition of its expression could be of benefit for the treatment of obesity, diabetes, and other metabolic diseases. In this article, we summarize the recent and timely advances concerning the important role of SCD in the biochemistry and physiology of lipid metabolism.

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19

Cohen, Paul, James M. Ntambi, and Jeffrey M. Friedman. "Stearoyl-CoA Desaturase-1 and the Metabolic Syndrome." Current Drug Targets - Immune, Endocrine & Metabolic Disorders 3, no. 4 (December 1, 2003): 271–80. http://dx.doi.org/10.2174/1568008033340117.

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Williams, Noelle S., Stephen Gonzales, Jacinth Naidoo, Giomar Rivera-Cancel, Sukesh Voruganti, Prema Mallipeddi, Panayotis C. Theodoropoulos, et al. "Tumor-Activated Benzothiazole Inhibitors of Stearoyl-CoA Desaturase." Journal of Medicinal Chemistry 63, no. 17 (August 5, 2020): 9773–86. http://dx.doi.org/10.1021/acs.jmedchem.0c00899.

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Attie, Alan D., Matthew T. Flowers, Jessica B. Flowers, Albert K. Groen, Folkert Kuipers, and James M. Ntambi. "Stearoyl-CoA Desaturase Deficiency, Hypercholesterolemia, Cholestasis, and Diabetes." Nutrition Reviews 65 (June 28, 2008): S35—S38. http://dx.doi.org/10.1111/j.1753-4887.2007.tb00326.x.

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Attie, Alan D., Matthew T. Flowers, Jessica B. Flowers, Albert K. Groen, Folkert Kuipers, and James M. Ntambi. "Stearoyl-CoA Desaturase Deficiency, Hypercholesterolemia, Cholestasis, and Diabetes." Nutrition Reviews 65, no. 6 (June 1, 2007): 35–38. http://dx.doi.org/10.1301/nr.2007.jun.s35-s38.

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Man, Weng Chi, Makoto Miyazaki, Kiki Chu, and James M. Ntambi. "Membrane Topology of Mouse Stearoyl-CoA Desaturase 1." Journal of Biological Chemistry 281, no. 2 (November 7, 2005): 1251–60. http://dx.doi.org/10.1074/jbc.m508733200.

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Liu, Gang. "Stearoyl-CoA desaturase inhibitors: update on patented compounds." Expert Opinion on Therapeutic Patents 19, no. 9 (August 19, 2009): 1169–91. http://dx.doi.org/10.1517/13543770903061311.

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Vincent, Benjamin M., Daniel F. Tardiff, Jeff S. Piotrowski, Rebecca Aron, Matthew C. Lucas, Chee Yeun Chung, Helene Bacherman та ін. "Inhibiting Stearoyl-CoA Desaturase Ameliorates α-Synuclein Cytotoxicity". Cell Reports 25, № 10 (грудень 2018): 2742–54. http://dx.doi.org/10.1016/j.celrep.2018.11.028.

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Kamal, Shagufta, Ayesha Saleem, Saima Rehman, Ismat Bibi, and Hafiz M. N. Iqbal. "Protein engineering: Regulatory perspectives of stearoyl CoA desaturase." International Journal of Biological Macromolecules 114 (July 2018): 692–99. http://dx.doi.org/10.1016/j.ijbiomac.2018.03.171.

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Li, Chun Sing, Liette Belair, Jocelyne Guay, Renata Murgasva, Wayne Sturkenboom, Yeeman K. Ramtohul, Lei Zhang, and Zheng Huang. "Thiazole analog as stearoyl-CoA desaturase 1 inhibitor." Bioorganic & Medicinal Chemistry Letters 19, no. 17 (September 2009): 5214–17. http://dx.doi.org/10.1016/j.bmcl.2009.07.015.

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Koeberle, Andreas, Konstantin Löser, and Maria Thürmer. "Stearoyl-CoA desaturase-1 and adaptive stress signaling." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1861, no. 11 (November 2016): 1719–26. http://dx.doi.org/10.1016/j.bbalip.2016.08.009.

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Shen, Jiemin, Gang Wu, Ah-Lim Tsai, and Ming Zhou. "Structure and Function of Mammalian Stearoyl-COA Desaturase." Biophysical Journal 114, no. 3 (February 2018): 426a. http://dx.doi.org/10.1016/j.bpj.2017.11.2361.

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Petroff, Anna B., Rebecca L. Weir, Charles R. Yates, Joseph D. Ng, and Jerome Baudry. "Sequential Dynamics of Stearoyl-CoA Desaturase-1(SCD1)/Ligand Binding and Unbinding Mechanism: A Computational Study." Biomolecules 11, no. 10 (September 30, 2021): 1435. http://dx.doi.org/10.3390/biom11101435.

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Stearoyl-CoA desaturase-1 (SCD1 or delta-9 desaturase, D9D) is a key metabolic protein that modulates cellular inflammation and stress, but overactivity of SCD1 is associated with diseases, including cancer and metabolic syndrome. This transmembrane endoplasmic reticulum protein converts saturated fatty acids into monounsaturated fatty acids, primarily stearoyl-CoA into oleoyl-CoA, which are critical products for energy metabolism and membrane composition. The present computational molecular dynamics study characterizes the molecular dynamics of SCD1 with substrate, product, and as an apoprotein. The modeling of SCD1:fatty acid interactions suggests that: (1) SCD1:CoA moiety interactions open the substrate-binding tunnel, (2) SCD1 stabilizes a substrate conformation favorable for desaturation, and (3) SCD1:product interactions result in an opening of the tunnel, possibly allowing product exit into the surrounding membrane. Together, these results describe a highly dynamic series of SCD1 conformations resulting from the enzyme:cofactor:substrate interplay that inform drug-discovery efforts.

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Miyazaki, Makoto, Francisco Enrique Gomez та James M. Ntambi. "Lack of stearoyl-CoA desaturase-1 function induces a palmitoyl-CoA Δ6 desaturase and represses the stearoyl-CoA desaturase-3 gene in the preputial glands of the mouse". Journal of Lipid Research 43, № 12 (16 вересня 2002): 2146–54. http://dx.doi.org/10.1194/jlr.m200271-jlr200.

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NAKASHIMA, Shigeru, Yutong ZHAO та Yoshinori NOZAWA. "Molecular cloning of Δ9 fatty acid desaturase from the protozoan Tetrahymena thermophila and its mRNA expression during thermal membrane adaptation". Biochemical Journal 317, № 1 (1 липня 1996): 29–34. http://dx.doi.org/10.1042/bj3170029.

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In response to a decrease in its growth temperature, the protozoan Tetrahymena is known to increase the level of unsaturated fatty acids in its membrane phospholipids so as to maintain the correct physical state (fluidity) of the membranes. In this organism, synthesis of unsaturated fatty acids is initiated by Δ9 acyl-CoA desaturase. Our previous studies have shown that, during cold adaptation, the activity of microsomal palmitoyl- and stearoyl-CoA desaturase increases, reaching a maximal level at 2 h after a temperature down-shift to 15 °C. Two hypotheses have been proposed to explain this increase in desaturase activity: (1) self-regulation via a direct effect of reduced membrane fluidity, and (2) induction of desaturase mRNA. However, the precise mechanism is not clearly understood. In order to obtain further insight into the mechanism of regulation of the desaturase, we have isolated a gene that encodes Δ9 fatty acid desaturase from T. thermophila and examined its expression during cold adaptation. The nucleotide sequence indicates that the 1.4 kbp gene encodes a polypeptide of 292 amino acid residues which shows marked sequence similarity to Δ9 acyl-CoA desaturases from other sources, e.g. rat, mouse, Amblyomma americanum and Saccharomyces cerevisiae. This protein has three histidine-cluster motifs (one HXXXXH and two HXXHH), and two hydrophobic regions which are conserved among Δ9 acyl-CoA desaturases. The level of desaturase mRNA was sensitive to decreasing the temperature of the culture media, and was close to maximal immediately after the temperature was shifted down from 35 °C to 15 °C (0.8 °C/min). Thereafter, the amount of mRNA gradually decreased with time, but remained above the control level for at least 5 h. Furthermore, during the course of the cooling process to 15 °C, the increased expression of desaturase mRNA became evident at 27 °C. Nuclear run-on analysis and actinomycin D chase experiments revealed that the elevation of the mRNA level was due to increases in both transcription and mRNA stability. These results suggest that the enhanced desaturase activity is controlled, at least in part, at the transcriptional level.

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Milanesi, E., L. Nicoloso, and P. Crepaldi. "Stearoyl CoA desaturase gene polymorphism in Italian cattle breeds." Italian Journal of Animal Science 6, sup1 (January 2007): 167. http://dx.doi.org/10.4081/ijas.2007.1s.167.

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Moioli, B., L. Orrù, G. Catillo, G. B. Congiu, and F. Napolitano. "Partial sequencing of Stearoyl-CoA desaturase gene in buffalo." Italian Journal of Animal Science 4, sup2 (January 2005): 25–27. http://dx.doi.org/10.4081/ijas.2005.2s.25.

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Dobrzyn, Pawel, Tomasz Bednarski, and Agnieszka Dobrzyn. "Metabolic reprogramming of the heart through stearoyl-CoA desaturase." Progress in Lipid Research 57 (January 2015): 1–12. http://dx.doi.org/10.1016/j.plipres.2014.11.003.

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Savino, Angela Maria, Orianne Olivares, Shani Barel, Lev Yakimov, Ifat Geron, Hila Fishman, Inbal Mor, et al. "Stearoyl-CoA Desaturase (SCD) Enhances Central Nervous System Leukemia." Blood 132, Supplement 1 (November 29, 2018): 389. http://dx.doi.org/10.1182/blood-2018-99-114749.

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Abstract Background: Central nervous system (CNS) involvement by acute lymphoblastic leukemia (ALL) is a major clinical concern. Leukemic cells can be found in the CNS at diagnosis (1-2%) or, more frequently, at relapse (30%). Very little is known about the pathogenesis and therefore there are no targeted therapies. Prophylactic CNS-directed conventional intrathecal chemotherapy or irradiation are required for relapse-free survival. However, they are associated with substantial rates of short and long term toxicity. Therefore, elucidation of molecular mechanisms and pathways mediating leukemia-cell entry and survival in the CNS is needed to develop alternative CNS-directed treatment strategies. Previous studies showed an increased expression of Stearoyl-CoA desaturase (SCD), a key enzyme of the de novo fatty acid synthesis pathway, in B cell precursor (BCP) ALL cells isolated from cerebrospinal fluid (CSF) of patients at the time of CNS relapse. A small SCD positive population was detected in the bone marrow (BM) at leukemia diagnosis in patients who later developed isolated CNS relapse, defining a potential biomarker for CNS relapse. It is unknown, however, if SCD has a functional role in CNS leukemia. Aim: To examine the hypothesis that increased expression of SCD enhances trafficking and survival of human B-ALL cells in the CNS Methods: We analyzed leukemia-cell entry into the CNS using xenografts of human BCP-ALL cell lines. Microarray profile of cells isolated from CNS and BM of transplanted mice was performed. Cell lines were transduced to overexpress human SCD and evaluated in vitro for proliferation kinetics and metabolic SCD activity. In vivo, SCD overexpressing cells were transplanted in NSG mice,sacrificed upon the first symptoms of CNS involvement, e.g. hind limb paralysis. BM, spleen and meninges were collected and analyzed to check human engraftment by FACS. The tumor load was expressed as total amount of leukemic cells in each organ. Competition assays were performed by transplanting SCD overexpressing and WT cells in the same mouse in a 1:1 ratio. Results: BCP-ALL cells transplanted into NSG mice faithfully recapitulated pathological features of meningeal infiltration seen in patients with ALL. Gene expression analysis of cells collected from BM and meninges of leukemic mice revealed up-regulation of the genes belonging to the signaling pathway of sterol regulatory element binding proteins (SREBPs) in ALL cells isolated from the CNS. SCD, whose transcription is controlled by the SREBP family, was significantly upregulated. SCD overexpression did not alter proliferation in vitro. Since SCD introduces a double bond in Stearoyl-CoA, its activity was measured as the ratio of unsaturated/saturated fatty acids in the cells. That ratio was increased in SCD overexpressing cells in vitro, confirming the functionality of the enzyme. In vivo, mice transplanted with SCD overexpressing cells led to a faster onset of CNS disease manifested by a clinical phenotype of earlier hind limb paralysis compared to control and significant increased number of leukemic cells in the CNS (Figure 1A).SCD overexpression also induced CNS engraftment of another B-ALL cell line, REH, which is not naturally prone to invade the central nervous system. Mice transplanted with SCD overexpressing REH cells showed the same phenotype of earlier hind limb paralysis and accumulation of leukemic cells in the CNS as the CNS-prone 018z cells, while WT REH did not show any CNS engraftment but comparable tumor load in BM and spleen (Figure1B). To reproduce the clonal heterogeneity in SCD expression observed previously in patients' BM, we performed a competition assay transplanting SCD overexpressing cells and control cells, expressing different fluorochromes, in the same mouse in a 1:1 ratio. In the CNS, the ratio between SCD overexpressing and WT cells ranged from 2 to 20 fold. This effect was unique to the CNS and not reproducible in the other hematopoietic organs where the 1:1 ratio was maintained (Figure 1C). Moreover, SCD overexpression sensitized leukemic cells to mTOR inhibitors, suggesting a potential therapeutic option Conclusion: SCD has a role in homing and survival of leukemic cells in the CNS and may be used as early predictor of CNS relapse. This study reveals a role for SCD and fatty acid metabolism in the pathogenesis of CNS leukemia suggesting that this pathway maybe targeted for specific therapy of this devastating disease. Figure 1. Figure 1. Disclosures Halsey: Jazz Pharmaceuticals: Honoraria, Other: Support for conference attendance.

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Dobrzyn, Agnieszka, and Pawel Dobrzyn. "Inhibition of stearoyl-CoA desaturase by cyclic amine derivatives." Expert Opinion on Therapeutic Patents 18, no. 4 (April 2008): 457–60. http://dx.doi.org/10.1517/13543776.18.4.457.

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Bai, Yonghong, Jason G. McCoy, Elena J. Levin, Pablo Sobrado, Kanagalaghatta R. Rajashankar, Brian G. Fox, and Ming Zhou. "X-ray structure of a mammalian stearoyl-CoA desaturase." Nature 524, no. 7564 (June 22, 2015): 252–56. http://dx.doi.org/10.1038/nature14549.

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NERGİS, Hazniye, Seyrani KONCAGÜL, and Selahaddin KİRAZ. "Hereford ırkı sığırlarda stearoyl-CoA desaturase (SCD) gen polimorfizmi." Harran Tarım ve Gıda Bilimleri Dergisi 23, no. 2 (June 18, 2019): 247–53. http://dx.doi.org/10.29050/harranziraat.487490.

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Sampath, Harini, and James M. Ntambi. "Role of stearoyl-CoA desaturase in human metabolic disease." Future Lipidology 3, no. 2 (April 2008): 163–73. http://dx.doi.org/10.2217/17460875.3.2.163.

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UMEKI, Shigenobu, and Yoshiniri NOZAWA. "Effect of Local Anesthetics on Stearoyl-CoA Desaturase ofTetrahymenaMicrosomes." Biological Chemistry Hoppe-Seyler 367, no. 1 (January 1986): 61–66. http://dx.doi.org/10.1515/bchm3.1986.367.1.61.

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Fenner, Annette. "Stearoyl-CoA desaturase: a novel therapeutic target for RCC." Nature Reviews Urology 10, no. 7 (May 21, 2013): 370. http://dx.doi.org/10.1038/nrurol.2013.116.

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Zhang, Chun-Lei, Xue-Yuan Gao, Ru-Ying Shao, Yan-Hong Wang, Xing-Tang Fang, and Hong Chen. "Stearoyl-CoA Desaturase (SCD) Gene Polymorphism in Goat Breeds." Biochemical Genetics 48, no. 9-10 (July 14, 2010): 822–28. http://dx.doi.org/10.1007/s10528-010-9363-y.

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Koltun, Dmitry O., Natalya I. Vasilevich, Eric Q. Parkhill, Andrei I. Glushkov, Timur M. Zilbershtein, Elena I. Mayboroda, Melanie A. Boze, et al. "Orally bioavailable, liver-selective stearoyl-CoA desaturase (SCD) inhibitors." Bioorganic & Medicinal Chemistry Letters 19, no. 11 (June 2009): 3050–53. http://dx.doi.org/10.1016/j.bmcl.2009.04.004.

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Wang, Jian, Lan Yu, He Wang, Yunling Gao, James P. Schrementi, Regina K. Porter, David A. Yurek, et al. "Identification and Characterization of Hamster Stearoyl-CoA Desaturase Isoforms." Lipids 43, no. 3 (December 15, 2007): 197–205. http://dx.doi.org/10.1007/s11745-007-3139-0.

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Liu, Xueqing, Makoto Miyazaki, Matthew T. Flowers, Harini Sampath, Minghui Zhao, Kiki Chu, Chad M. Paton, Diane Seohee Joo, and James M. Ntambi. "Loss of Stearoyl-CoA Desaturase-1 Attenuates Adipocyte Inflammation." Arteriosclerosis, Thrombosis, and Vascular Biology 30, no. 1 (January 2010): 31–38. http://dx.doi.org/10.1161/atvbaha.109.195636.

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Liu, Lulu, Yu Wang, Xiaojuan Liang, Xiao Wu, Jiali Liu, Shulin Yang, Cong Tao, et al. "Stearoyl-CoA Desaturase Is Essential for Porcine Adipocyte Differentiation." International Journal of Molecular Sciences 21, no. 7 (April 1, 2020): 2446. http://dx.doi.org/10.3390/ijms21072446.

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Fat deposition, which influences pork production, meat quality and growth efficiency, is an economically important trait in pigs. Numerous studies have demonstrated that stearoyl-CoA desaturase (SCD), a key enzyme that catalyzes the conversion of saturated fatty acids into monounsaturated fatty acids, is associated with fatty acid composition in pigs. As SCD was observed to be significantly induced in 3T3-L1 preadipocytes differentiation, we hypothesized that it plays a role in porcine adipocyte differentiation and fat deposition. In this study, we revealed that SCD is highly expressed in adipose tissues from seven-day-old piglets, compared to its expression in tissues from four-month-old adult pigs. Moreover, we found that SCD and lipogenesis-related genes were induced significantly in differentiated porcine adipocytes. Using CRISPR/Cas9 technology, we generated SCD-/- porcine embryonic fibroblasts (PEFs) and found that the loss of SCD led to dramatically decreased transdifferentiation efficiency, as evidenced by the decreased expression of known lipid synthesis-related genes, lower levels of oil red O staining and significantly lower levels of triglyceride content. Our study demonstrates the critical role of SCD expression in porcine adipocyte differentiation and paves the way for identifying it as the promising candidate gene for less fat deposition in pigs.

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ZHANG, Lin, Lan GE, Tai TRAN, Kurt STENN, and Stephen M. PROUTY. "Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element." Biochemical Journal 357, no. 1 (June 25, 2001): 183–93. http://dx.doi.org/10.1042/bj3570183.

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Stearoyl-CoA desaturase is the rate-limiting enzyme in the production of mono-unsaturated fatty acids. We have recently cloned and characterized the human Scd cDNA and SCD (the stearoyl-CoA desaturase structural gene) on chromosome 10, as well as the non-transcribed pseudogene on chromosome 17. In order to further define SCD regulation and function, we have isolated and characterized the promoter of the structural gene. Screening of chromosome-10-specific libraries resulted in the isolation of 4.1kb of SCD sequence upstream of the translation start site. Binding sites for transcription factors critical for mouse Scd1 and Scd2 promoter activity, such as sterol-regulated-element-binding protein and nuclear factor Y, were present in the human SCD promoter (Scd is the mouse stearoyl-CoA desaturase gene). Deletion analysis in HaCaT keratinocytes identified a critical region for promoter activity between nts 496–609 upstream of the translation start site. Site-directed mutagenesis of binding sites in this region identified the CCAAT box as the critical cis-element for SCD promoter activity. An electrophoretic mobility-shift assay confirmed that this element binds nuclear proteins from HaCaT keratinocytes. The polyunsaturated-fatty-acid (PUFA) response element, previously identified in the promoters of mouse Scd1 and Scd2, was found to be conserved in the human SCD promoter, and contained the critical CCAAT cis-element. A minimal promoter construct including this region was responsive to fatty acids, with oleate and linoleate decreasing transcription and stearate increasing it. These studies indicate that CCAAT-box-binding proteins activate SCD transcription in cultured keratinocytes and that fatty acids modulate transcription, most likely through the conserved PUFA response element.

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Li, Weihua, Huimin Bai, Shiping Liu, Dongyan Cao, Hongying Wu, Keng Shen, Yanhong Tai, and Jiaxin Yang. "Targeting stearoyl-CoA desaturase 1 to repress endometrial cancer progression." Oncotarget 9, no. 15 (January 24, 2018): 12064–78. http://dx.doi.org/10.18632/oncotarget.24304.

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Dobrzyn, A. "The Role of Stearoyl-CoA Desaturase in Body Weight Regulation." Trends in Cardiovascular Medicine 14, no. 2 (February 2004): 77–81. http://dx.doi.org/10.1016/j.tcm.2003.12.005.

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