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Journal articles on the topic 'PLSCR1[Phospholipide Scramblase]'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Zhou, Quansheng, Ji Zhao, Therese Wiedmer, and Peter J. Sims. "Normal hemostasis but defective hematopoietic response to growth factors in mice deficient in phospholipid scramblase 1." Blood 99, no. 11 (2002): 4030–38. http://dx.doi.org/10.1182/blood-2001-12-0271.

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Phospholipid scramblase 1 (PLSCR1) is an endofacial plasma membrane protein proposed to participate in transbilayer movement of phosphatidylserine and other phospholipids. In addition to its putative role in the reorganization of plasma membrane phospholipids, PLSCR1 is a substrate of intracellular kinases that imply its possible participation in diverse signaling pathways underlying proliferation, differentiation, or apoptosis. Because PLSCR1 is prominently expressed in a variety of blood cells, we evaluated PLSCR activity in platelets and erythrocytes, and cytokine-dependent growth of hemato

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2

Zhou, Quansheng, Ji Zhao, Fahad Al-Zoghaibi та ін. "Transcriptional control of the human plasma membranephospholipid scramblase 1 gene is mediated by interferon-α". Blood 95, № 8 (2000): 2593–99. http://dx.doi.org/10.1182/blood.v95.8.2593.

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Abstract Interferons (IFNs) mediate their diverse biologic activities through induction of the expression of multiple genes. Whereas the mode of action of certain of these IFN-regulated genes has been well characterized, most of the molecular and cellular events underlying the constellation of biologic responses to the IFNs remain unresolved. This study showed that the newly identified PLSCR1 gene for phospholipid scramblase, previously implicated in remodeling of plasma membrane phospholipids, is regulated at the transcriptional level by IFN-. Analysis of 5′ flanking genomic sequence in repo

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3

Zhou, Quansheng, Ji Zhao, Fahad Al-Zoghaibi та ін. "Transcriptional control of the human plasma membranephospholipid scramblase 1 gene is mediated by interferon-α". Blood 95, № 8 (2000): 2593–99. http://dx.doi.org/10.1182/blood.v95.8.2593.008k32_2593_2599.

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Interferons (IFNs) mediate their diverse biologic activities through induction of the expression of multiple genes. Whereas the mode of action of certain of these IFN-regulated genes has been well characterized, most of the molecular and cellular events underlying the constellation of biologic responses to the IFNs remain unresolved. This study showed that the newly identified PLSCR1 gene for phospholipid scramblase, previously implicated in remodeling of plasma membrane phospholipids, is regulated at the transcriptional level by IFN-. Analysis of 5′ flanking genomic sequence in reporter cons

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4

Benhamou, M. "Scrambling des phospholipides et Phospholipid Scramblase 1 (PLSCR1) dans les mastocytes activés." Revue Française d'Allergologie 57, no. 5 (2017): 389–95. http://dx.doi.org/10.1016/j.reval.2017.02.235.

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5

Li, Youjun, Kenneth Rogulski, Quansheng Zhou, Peter J. Sims, and Edward V. Prochownik. "The Negative c-Myc Target Onzin Affects Proliferation and Apoptosis via Its Obligate Interaction with Phospholipid Scramblase I." Molecular and Cellular Biology 26, no. 9 (2006): 3401–13. http://dx.doi.org/10.1128/mcb.26.9.3401-3413.2006.

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ABSTRACT Onzin, the product of a negatively c-Myc-regulated target gene, is highly expressed in myeloid cells. As a result of its interaction with and activation of Akt1 and Mdm2, onzin down-regulates p53. The apoptotic sensitivity of several cell lines is thus directly related to onzin levels. We have conducted a search for additional onzin-interacting proteins and identified phospholipid scramblase 1 (PLSCR1), an endofacial membrane protein, which is proposed to mediate the bidirectional movement of plasma membrane phospholipids during proliferation and apoptosis. PLSCR1 interacts with the s

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6

Dong, Beihua, Quansheng Zhou, Ji Zhao, et al. "Phospholipid Scramblase 1 Potentiates the Antiviral Activity of Interferon." Journal of Virology 78, no. 17 (2004): 8983–93. http://dx.doi.org/10.1128/jvi.78.17.8983-8993.2004.

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ABSTRACT Phospholipid scramblase 1 (PLSCR1) is an interferon (IFN)- and growth factor-inducible, calcium-binding protein that either inserts into the plasma membrane or binds DNA in the nucleus depending on its state of palmyitoylation. In certain hematopoietic cells, PLSCR1 is required for normal maturation and terminal differentiation from progenitor cells as regulated by select growth factors, where it promotes recruitment and activation of Src kinases. PLSCR1 is a substrate of Src (and Abl) kinases, and transcription of the PLSCR1 gene is regulated by the same growth factor receptor pathwa

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7

Wiedmer, Therese, and Peter Sims. "Unraveling the Mysteries of Phospholipid Scrambling." Thrombosis and Haemostasis 86, no. 07 (2001): 266–75. http://dx.doi.org/10.1055/s-0037-1616224.

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SummaryPlasma membrane phospholipid asymmetry is maintained by an aminophospholipid translocase that transports phosphatidylserine (PS) and phosphatidylethanolamine (PE) from outer to inner membrane leaflet. Cell activation or injury leads to redistribution of all major lipid classes within the plasma membrane, resulting in surface exposure of PS and PE. Cell surface-exposed PS can serve as receptor sites for coagulation enzyme complexes, and contributes to cell clearance by the reticuloendothelial system. The mechanism(s) by which this PL ”scrambling” occurs is poorly understood. A protein ca

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8

Zhao, Ke-Wen, Xi Li, Qian Zhao та ін. "Protein kinase Cδ mediates retinoic acid and phorbol myristate acetate–induced phospholipid scramblase 1 gene expression: its role in leukemic cell differentiation". Blood 104, № 12 (2004): 3731–38. http://dx.doi.org/10.1182/blood-2004-04-1630.

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Although phospholipid scramblase 1 (PLSCR1) was originally identified based on its capacity to promote transbilayer movement of membrane phospholipids, subsequent studies also provided evidence for its role in cell proliferation, maturation, and apoptosis. In this report, we investigate the potential role of PLSCR1 in leukemic cell differentiation. We show that all-trans retinoic acid (ATRA), an effective differentiation-inducing agent of acute promyelocytic leukemic (APL) cells, can elevate PLSCR1 expression in ATRA-sensitive APL cells NB4 and HL60, but not in maturation-resistant NB4-LR1 cel

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9

SUZUKI, ERIKO, OLGA AMENGUAL, TATSUYA ATSUMI, et al. "Increased Expression of Phospholipid Scramblase 1 in Monocytes from Patients with Systemic Lupus Erythematosus." Journal of Rheumatology 37, no. 8 (2010): 1639–45. http://dx.doi.org/10.3899/jrheum.091420.

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Objective.A high incidence of thromboembolic events has been reported in patients with systemic lupus erythematosus (SLE). Phosphatidylserine (PS) is normally sequestered in the inner leaflet of cell membranes. Externalization of PS during cell activation is mediated by phospholipid scramblase 1 (PLSCR1) and has a central role in promoting blood coagulation. We investigated the underlying pathogenic status of thrombophilia in SLE by analyzing PLSCR1 expression on monocytes from patients with SLE.Methods.Sixty patients with SLE were evaluated. Twenty-three patients had antiphospholipid syndrome

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10

Chen, Yan, Bao-An Chen, and Qing-long Guo. "Wogonoside Exerts Anti-Leukemia of AML Cells Via Restricting Phospholipid Scramblase 1 Gene Expression and Promoting Its Translocation Into Nuclear." Blood 118, no. 21 (2011): 4282. http://dx.doi.org/10.1182/blood.v118.21.4282.4282.

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Abstract Abstract 4282 Objective: To evaluate the antileukemic effect of wogonoside and reveal the underlying mechanism. Method: In this study trypan blue dye exclusion assay, MTT assay, and soft agar colony formation assay were used to analysis growth inhibition of wogonoside the on AML (acute human promyelocytic) cell lines. Propidium iodide (PI)-staining and cell cycle-regulatory proteins detecting by western blots were applied to exam whether wogonoside could induce cell cycle arrest. Then a series of experiment were used to assess the ability of wogonoside to overcome the AML associated d

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11

Venegas, Victor, and Zheng Zhou. "Two Alternative Mechanisms That Regulate the Presentation of Apoptotic Cell Engulfment Signal in Caenorhabditis elegans." Molecular Biology of the Cell 18, no. 8 (2007): 3180–92. http://dx.doi.org/10.1091/mbc.e07-02-0138.

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Phosphatidylserine exposed on the surface of apoptotic mammalian cells is considered an “eat-me” signal that attracts phagocytes. The generality of using phosphatidylserine as a clearance signal for apoptotic cells in animals and the regulation of this event remain uncertain. Using ectopically expressed mouse MFG-E8, a secreted phosphatidylserine-binding protein, we detected specific exposure of phosphatidylserine on the surface of apoptotic cells in Caenorhabditis elegans. Masking the surface phosphatidylserine inhibits apoptotic cell engulfment. CED-7, an ATP-binding cassette (ABC) transport

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12

Berghold, Veronika M., Martin Gauster, Denise G. Hemmings, et al. "Phospholipid scramblase 1 (PLSCR1) in villous trophoblast of the human placenta." Histochemistry and Cell Biology 143, no. 4 (2014): 381–96. http://dx.doi.org/10.1007/s00418-014-1294-y.

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13

Guo, Jizheng, Jie Li, Lin Xia, et al. "Transient Receptor Potential Canonical 5-Scramblase Signaling Complex Mediates Neuronal Phosphatidylserine Externalization and Apoptosis." Cells 9, no. 3 (2020): 547. http://dx.doi.org/10.3390/cells9030547.

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Phospholipid scramblase 1 (PLSCR1), a lipid-binding and Ca2+-sensitive protein located on plasma membranes, is critically involved in phosphatidylserine (PS) externalization, an important process in cell apoptosis. Transient receptor potential canonical 5 (TRPC5), is a nonselective Ca2+ channel in neurons that interacts with many downstream molecules, participating in diverse physiological functions including temperature or mechanical sensation. The interaction between TRPC5 and PLSCR1 has never been reported. Here, we showed that PLSCR1 interacts with TRPC5 through their C-termini in HEK293 c

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14

Huang, Y., Q. Zhao, C.-X. Zhou, et al. "Antileukemic roles of human phospholipid scramblase 1 gene, evidence from inducible PLSCR1-expressing leukemic cells." Oncogene 25, no. 50 (2006): 6618–27. http://dx.doi.org/10.1038/sj.onc.1209677.

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15

Ostojić, Olga, Michael F. N. O'Leary, Kaustabh Singh, Keir J. Menzies, Anna Vainshtein, and David A. Hood. "The effects of chronic muscle use and disuse on cardiolipin metabolism." Journal of Applied Physiology 114, no. 4 (2013): 444–52. http://dx.doi.org/10.1152/japplphysiol.01312.2012.

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Cardiolipin (CL) is a phospholipid that maintains the integrity of mitochondrial membranes. We previously demonstrated that CL content increases with chronic muscle use, and decreases with denervation-induced disuse. To investigate the underlying mechanisms, we measured the mRNA expression of 1) CL synthesis enzymes cardiolipin synthase (CLS) and CTP:PA-cytidylyltransferase-1 (CDS-1); 2) remodeling enzymes tafazzin and acyl-CoA:lysocardiolipin acyltransferase-1 (ALCAT1); and 3) outer membrane CL enzymes, mitochondrial phospholipase D and phospholipid scramblase 3 (Plscr3), during chronic contr

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16

Lu, Biao, Peter J. Sims, Therese Wiedmer, et al. "Expression of the phospholipid scramblase (PLSCR) gene family during the acute phase response." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1771, no. 9 (2007): 1177–85. http://dx.doi.org/10.1016/j.bbalip.2007.05.002.

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17

Huang, Y., Q. Zhao, C.-X. Zhou, et al. "Erratum: Antileukemic roles of human phospholipid scramblase 1 gene, evidence from inducible PLSCR1-expressing leukemic cells." Oncogene 25, no. 54 (2006): 7224. http://dx.doi.org/10.1038/sj.onc.1210082.

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18

Frasch, S. Courtney, Peter M. Henson, Kaz Nagaosa, Michael B. Fessler, Niels Borregaard, and Donna L. Bratton. "Phospholipid Flip-Flop and Phospholipid Scramblase 1 (PLSCR1) Co-localize to Uropod Rafts in Formylated Met-Leu-Phe-stimulated Neutrophils." Journal of Biological Chemistry 279, no. 17 (2004): 17625–33. http://dx.doi.org/10.1074/jbc.m313414200.

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19

Barber, Latorya Arnold, Mary B. Palascak, Clinton H. Joiner, and Robert S. Franco. "Red Blood Cell Scramblase Activation Is Induced by Phorbol Ester and Prevented by Inhibition of Protein Kinase C." Blood 112, no. 11 (2008): 2494. http://dx.doi.org/10.1182/blood.v112.11.2494.2494.

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Abstract Phosphatidylserine (PS) is normally confined to the inner leaflet of the red blood cell (RBC) membrane, but is externalized in many sickle RBC. This external PS may contribute to decreased sickle RBC survival, increased thrombogenesis, and increased sickle RBC-endothelial interaction. Aminophospholipid Translocase (APLT) and Phospholipid Scramblase (PLSCR) are thought to regulate the distribution of PS between the inner and outer membrane leaflets. APLT maintains phospholipid (PL) asymmetry by returning externalized PS to the inner membrane leaflet. PLSCR disrupts PL asymmetry by caus

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20

Kantari, Chahrazade, Magali Pederzoli-Ribeil, Omid Amir-Moazami, et al. "Proteinase 3, the Wegener autoantigen, is externalized during neutrophil apoptosis: evidence for a functional association with phospholipid scramblase 1 and interference with macrophage phagocytosis." Blood 110, no. 12 (2007): 4086–95. http://dx.doi.org/10.1182/blood-2007-03-080457.

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Abstract Proteinase 3 (PR3), a serine proteinase contained in neutrophil azurophilic granules, is considered a risk factor for vasculitides and rheumatoid arthritis when expressed on the outer leaflet of neutrophil plasma membrane and is the preferred target of antineutrophil cytoplasm autoantibodies (ANCA) in Wegener granulomatosis. ANCA binding to PR3 expressed at the surface of neutrophils activates them. Evidence is provided that neutrophil apoptosis induced significantly more membrane PR3 expression without degranulation (but no enhanced membrane CD35, CD66b, CD63, myeloperoxidase, or ela

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21

Arnold, Latorya E., Mary B. Palascak, Clinton H. Joiner, and Robert S. Franco. "External PS in Sickle RBC: Relationships among Aminophospholipid Translocase (APLT), Phospholipid Scramblase (PLSCR), Cell Maturity, and Cell Density." Blood 110, no. 11 (2007): 148. http://dx.doi.org/10.1182/blood.v110.11.148.148.

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Abstract External phosphatidylserine (PS) is present on some sickle RBC and may contribute to thrombogenesis, endothelial adhesion, and shortened RBC lifespan. Phospholipid scramblase (PLSCR) disrupts phospholipid (PL) asymmetry by causing nonspecific PL equilibration across the membrane. Aminophospholipid translocase (APLT) maintains PL asymmetry by returning externalized PS to the inner membrane leaflet. It has been proposed that both APLT inhibition and PLSCR activation are required for PS externalization. Sickle RBC with low level external PS (Type I PS+) are present in cells of all densit

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22

Wiedmer, T., J. Zhao, L. Li, et al. "Adiposity, dyslipidemia, and insulin resistance in mice with targeted deletion of phospholipid scramblase 3 (PLSCR3)." Proceedings of the National Academy of Sciences 101, no. 36 (2004): 13296–301. http://dx.doi.org/10.1073/pnas.0405354101.

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23

Rami, A., J. Sims, G. Botez, and J. Winckler. "Spatial resolution of phospholipid scramblase 1 (PLSCR1), caspase-3 activation and DNA-fragmentation in the human hippocampus after cerebral ischemia." Neurochemistry International 43, no. 1 (2003): 79–87. http://dx.doi.org/10.1016/s0197-0186(02)00194-8.

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24

Song, Gwonhwa, Jo-Ann G. W. Fleming, Jinyoung Kim, Thomas E. Spencer та Fuller W. Bazer. "Pregnancy and interferon τ regulate DDX58 and PLSCR1 in the ovine uterus during the peri-implantation period". REPRODUCTION 141, № 1 (2011): 127–38. http://dx.doi.org/10.1530/rep-10-0348.

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Interferon τ (IFNT), the pregnancy recognition signal in ruminants, abrogates the luteolytic mechanism for maintenance of the corpus luteum for production of progesterone (P4). This study examined the expression of DEAD (Asp-Glu-Ala-Asp) box polypeptide 58 (DDX58) and phospholipid scramblase 1 (PLSCR1) mRNAs in the ovine uterus as these genes were increased most in 2fTGH (STAT1 positive) cells by IFNT. The results of this study indicated that IFNT regulates expression ofDDX58andPLSCR1mRNAs in the ovine uterus, which confirmed the results of thein vitrotranscriptional profiling experiment with

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25

Liu, Xiaobin, Dong Wang, Xiaoning Zhang, et al. "Effect and mechanism of phospholipid scramblase 4 (PLSCR4) on lipopolysaccharide (LPS)-induced injury to human pulmonary microvascular endothelial cells." Annals of Translational Medicine 9, no. 2 (2021): 159. http://dx.doi.org/10.21037/atm-20-7983.

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26

Bailey, Kendra, Harold W. Cook та Christopher R. McMaster. "The phospholipid scramblase PLSCR1 increases UV induced apoptosis primarily through the augmentation of the intrinsic apoptotic pathway and independent of direct phosphorylation by protein kinase C δ". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1733, № 2-3 (2005): 199–209. http://dx.doi.org/10.1016/j.bbalip.2004.12.013.

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27

Inokawa, Akira, Tatsutoshi Inuzuka, Terunao Takahara, Hideki Shibata, and Masatoshi Maki. "Tubby-like protein superfamily member PLSCR3 functions as a negative regulator of adipogenesis in mouse 3T3-L1 preadipocytes by suppressing induction of late differentiation stage transcription factors." Bioscience Reports 36, no. 1 (2016). http://dx.doi.org/10.1042/bsr20150215.

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Decrease in intracellular amount of phospholipid scramblase 3 (PLSCR3) is accompanied by enhanced unconventional secretion during differentiation of mouse preadipocytic 3T3-L1 cells. Forced overexpression of PLSCR3 in 3T3-L1 cells inhibited adipogenesis by suppressing induction of late stage pro-adipogenic transcription factors.

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28

Inuzuka, Tatsutoshi, Akira Inokawa, Cen Chen, et al. "ALG-2-interacting Tubby-like protein superfamily member PLSCR3 is secreted by an exosomal pathway and taken up by recipient cultured cells." Bioscience Reports 33, no. 2 (2013). http://dx.doi.org/10.1042/bsr20120123.

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PLSCRs (phospholipid scramblases) are palmitoylated membrane-associating proteins. Regardless of the given names, their physiological functions are not clear and thought to be unrelated to phospholipid scrambling activities observed in vitro. Using a previously established cell line of HEK-293 (human embryonic kidney-293) cells constitutively expressing human Scr3 (PLSCR3) that interacts with ALG-2 (apoptosis-linked gene 2) Ca2+-dependently, we found that Scr3 was secreted into the culture medium. Secretion of Scr3 was suppressed by 2-BP (2-bromopalmitate, a palmitoylation inhibitor) and by GW

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