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Journal articles on the topic 'Phosphatidylinositols'

Author: Grafiati

Published: 4 June 2021

Last updated: 21 February 2023

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1

Morisaki, Naoko, Koji Morita, Asuka Nishikawa, Noriyuki Nakatsu, Yasuhisa Fukui, Yuichi Hashimoto, and Ryuichi Shirai. "Phosphorylation of Unnatural Phosphatidylinositols with Phosphatidylinositol 3-Kinase." Tetrahedron 56, no. 17 (April 2000): 2603–14. http://dx.doi.org/10.1016/s0040-4020(00)00161-7.

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2

Shirai, Ryuichi, Koji Morita, Asuka Nishikawa, Noriyuki Nakatsu, Yasuhisa Fukui, Naoko Morisaki, and Yuichi Hashimoto. "The structural requirement of phosphatidylinositols as substrate of phosphatidylinositol 3-kinase." Tetrahedron Letters 40, no. 9 (February 1999): 1693–96. http://dx.doi.org/10.1016/s0040-4039(99)00004-0.

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3

Fan, Zheng, Lizhi Gao, and Wenxia Wang. "Phosphatidic acid stimulates cardiac KATPchannels like phosphatidylinositols, but with novel gating kinetics." American Journal of Physiology-Cell Physiology 284, no. 1 (January 1, 2003): C94—C102. http://dx.doi.org/10.1152/ajpcell.00255.2002.

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Membrane-bound anionic phospholipids such as phosphatidylinositols have the capacity to modulate ATP-sensitive potassium (KATP) channels through a mechanism involving long-range electrostatic interaction between the lipid headgroup and channel. However, it has not yet been determined whether the multiple effects of phosphatidylinositols reported in the literature all result from this general electrostatic interaction or require a specific headgroup structure. The present study investigated whether phosphatidic acid (PA), an anionic phospholipid substantially different in structure from phosphatidylinositols, evokes effects similar to phosphatidylinositols on native KATP channels of rat heart and heterogeneous Kir6.2/SUR2A channels. Channels treated with PA (0.2–1 mg/ml applied to the cytoplasmic side of the membrane) exhibited higher activity, lower sensitivity to ATP inhibition, less Mg2+-dependent nucleotide stimulation, and poor sulfonylurea inhibition. These effects match the spectrum of phosphatidylinositols' effects, but, in addition, PA also induced a novel pattern in gating kinetics, represented by a decreased mean open time (from 12.2 ± 2.0 to 3.3 ± 0.7 ms). This impact on gating kinetics clearly distinguishes PA's effects from those of phosphatidylinositols. Results indicate that multiple effects of anionic phospholipids on KATP channels are related phenomena and can likely be attributed to a common mechanism, but additional specific effects due to other mechanisms may also coincide.

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4

Shirai, Ryuichi, Koji Morita, Asuka Nishikawa, Noriyuki Nakatsu, Yasuhisa Fukui, Naoko Morisaki, and Yuichi Hashimoto. "ChemInform Abstract: The Structural Requirement of Phosphatidylinositols as Substrate of Phosphatidylinositol 3-Kinase." ChemInform 30, no. 21 (June 15, 2010): no. http://dx.doi.org/10.1002/chin.199921219.

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5

Garigapati, Venkata R., and Mary F. Roberts. "Synthesis of short chain phosphatidylinositols." Tetrahedron Letters 34, no. 5 (January 1993): 769–72. http://dx.doi.org/10.1016/0040-4039(93)89007-d.

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6

Raper, J., T. L. Doering, L. U. Buxbaum, and P. T. Englund. "Glycosyl Phosphatidylinositols in Trypanosoma brucei." Experimental Parasitology 76, no. 2 (March 1993): 216–20. http://dx.doi.org/10.1006/expr.1993.1026.

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7

MCCONVILLE, M. "Glycosylated-phosphatidylinositols as virulence factors in." Cell Biology International Reports 15, no. 9 (September 1991): 779–98. http://dx.doi.org/10.1016/0309-1651(91)90033-f.

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8

EKHOLM, S. E., T. W. MORRIS, and G. V. MARINETTI. "Effects of Contrast Media on Synaptosomal Phosphatidylinositols." Investigative Radiology 25 (September 1990): S84—S85. http://dx.doi.org/10.1097/00004424-199009001-00039.

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9

Sandelius, Anna Stina, and Marianne Sommarin. "Phosphorylation of phosphatidylinositols in isolated plant membranes." FEBS Letters 201, no. 2 (June 9, 1986): 282–86. http://dx.doi.org/10.1016/0014-5793(86)80624-x.

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10

D'Souza, Kenneth, and Richard M. Epand. "Enrichment of phosphatidylinositols with specific acyl chains." Biochimica et Biophysica Acta (BBA) - Biomembranes 1838, no. 6 (June 2014): 1501–8. http://dx.doi.org/10.1016/j.bbamem.2013.10.003.

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11

Bozelli, José Carlos, and Richard M. Epand. "Specificity of Acyl Chain Composition of Phosphatidylinositols." PROTEOMICS 19, no. 18 (September 2019): 1900138. http://dx.doi.org/10.1002/pmic.201900138.

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12

GARIGAPATI, V. R., and M. F. ROBERT. "ChemInform Abstract: Synthesis of Short Chain Phosphatidylinositols." ChemInform 24, no. 25 (August 20, 2010): no. http://dx.doi.org/10.1002/chin.199325257.

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13

Mills, G. B., D. J. Stewart, A. Mellors, and E. W. Gelfand. "Interleukin 2 does not induce phosphatidylinositol hydrolysis in activated T cells." Journal of Immunology 136, no. 8 (April 15, 1986): 3019–24. http://dx.doi.org/10.4049/jimmunol.136.8.3019.

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Abstract Hydrolysis of phosphatidylinositol-4,5-bisphosphate to diacylglycerol and myoinositol-1,4,5-trisphosphate is thought to be a primary event in the activation of cells by some growth factors, mitogenic lectins, and oncogenes. The mechanism whereby interleukin 2 (IL 2) binding to its receptor on activated T lymphocytes leads to cell proliferation has not been determined. Because the mitogenic has not been determined. Because the mitogenic action of IL 2 resembles that of some growth factors, the possible role of phosphatidylinositol breakdown in the activation of T cells by IL 2 was examined. In human or murine IL 2-sensitive cells, incubation with IL 2 did not alter the rate of turnover of phosphatidylinositol, phosphatidylinositol-5-phosphate, phosphatidylinositol-4,5-bisphosphate, or phosphatidylcholine in 32PO4-loaded cells. IL 2 also did not alter either the isotopic labeling of diacylglycerol or [3H]arachidonic acid release from cells. In addition, IL 2 did not alter the rate of formation of the phosphatidylinositol breakdown products myoinositol-1,4,5-trisphosphate, myoinositol-1,4-bisphosphate, or myoinositol-1-phosphate. In contrast, under similar conditions, IL 2 induced significant increases in [3H]thymidine incorporation and cell proliferation. Mitogenic lectins such as concanavalin A and phytohemagglutinin gave significant changes in isotopic labeling of phosphoinositols, diacylglycerols, and phosphatidylinositols, indicating that phosphatidylinositol hydrolysis induced by mitogenic lectins was detectable in the assay systems. IL 2, in contrast to other growth factors, does not appear to signal cells by increasing phosphatidylinositol breakdown.

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14

Nybom, Pia, and Karl-Eric Magnusson. "Studies with wortmannin and cytochalasins suggest a pivotal role of phosphatidylinositols in the regulation of tight junction integrity." Bioscience Reports 16, no. 3 (June 1, 1996): 265–72. http://dx.doi.org/10.1007/bf01207340.

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Wortmannin, a selective inhibitor of phosphatidylinositol 3-kinase (P13K), was found to give a dose and time-dependent, bimodal effect-initial increase, followed by decrease on the tight junction integrity of MDCK-1 monolayers, as assessed by electrical resistance measurement of the epithelia. Moreover, dihydrocytochalasin B inhibited the wortmannin-induced alteration, whereas cytochalasin B had a negligible influence on the wortmannin effect. Wortmannin was also found to cause changes in the cytoskeleton structure. These alterations were also seen when wortmannin was combined with cytochalasin B. However, in accordance with the electrical resistance measurements, dihydrocytochalasin B was able to abolish wortmannin-induced filamentous (F-) actin changes. These findings suggest that the P13K, phosphatidylinositols, and filamentous actin rearrangements, in combination, play an important role in the modulation of the junctional integrity.

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15

Mukaida, N., T. Kasahara, H. Yagisawa, K. Shioiri-Nakano, and T. Kawai. "Signal requirement for interleukin-1-dependent interleukin 2 production by a human leukemia-derived HSB.2 subclone." Journal of Immunology 139, no. 10 (November 15, 1987): 3321–29. http://dx.doi.org/10.4049/jimmunol.139.10.3321.

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Abstract We have previously established subclones from human leukemia-derived HSB.2 cell line that produced high levels of interleukin (IL) 2 when stimulated with phytohemagglutinin (PHA) and IL-1. Herein, we investigated the signal requirement for IL-2 production, particularly concerning the role of IL-1 in this system. PHA but not IL-1 rendered marked protein kinase C (PKC) activation and IL-2 production induced by PHA plus IL-1 was totally abrogated by a potent PKC inhibitor, H-7. Concomitantly, PHA alone caused marked Ca2+ influx, whereas IL-1 neither induced Ca2+ influx nor augmented PHA-induced Ca2+ influx. As expected, a signal delivered by PHA could be substituted by phorbol 12-myristate 13-acetate (PMA) and ionomycin while IL-1 was still indispensable, indicating that at least three signals, i.e., those delivered by IL-1 as well as PKC activation and Ca2+ influx were required for optimal IL-2 production. Kinetic study indicated that while PMA and ionomycin should be added at the initiation of culture, delayed addition of IL-1 up to 4 hr later induced even higher levels of IL-2 production, demonstrating the requirement for IL-1 after PKC activation and Ca2+ influx. In this system, it was revealed that IL-1 was not involved in PKC activation, Ca2+ influx, and breakdown of phosphatidylinositols. Whereas PMA, ionomycin, and IL-1 stimulated high levels of IL-2 production, those combinations of signals did not induce breakdown of phosphatidylinositols. It should be noted that IL-2 production induced by these three signals seemed to bypass hydrolysis of phosphatidylinositols in contrast to PHA plus IL-1 stimulation that was accompanied with a marked breakdown of phosphatidylinositols.

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16

Brearley, C. A., and D. E. Hanke. "Evidence for substrate-cycling of 3-, 3,4-, 4-, and 4,5-phosphorylated phosphatidylinositols in plants." Biochemical Journal 311, no. 3 (November 1, 1995): 1001–7. http://dx.doi.org/10.1042/bj3111001.

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Short-term 32P labelling and enzymic dissection of inositol phospholipids was used to study the turnover of 3-, 3,4-, 4-, and 4,5-phosphorylated phosphatidylinositols in the plant Spirodela polyrhiza L. Analysis of label in the whole headgroup reveals that phosphatidylinositol 3- and 4-monophosphates (PtdIns3P and PtdIns4P) and phosphatidylinositol 3,4- and 4,5-bisphosphates [PtdIns(3,4)P2 and PtdIns(4,5)P2] all turn over with a half-life of approximately 2-5 h. Analysis of the labelling of individual phosphomonoesters and phosphodiesters of these lipids indicates a rapid equilibration of label between the 4- and 5-monoester phosphates of PtdIns(4,5)P2 within 5 h and largely independent of changes of labelling in the diester. We observed substantially slower equilibration of label (within approximately 27 h) between the monoester and diester of PtdIns4P. These studies therefore indicate that PtdIns4P and PtdIns(4,5)P2 participate in substrate-cycling reactions, evidence for which has been described experimentally only in erythrocytes, and give confirmation in vivo of the previous detection of inositol phospholipid phosphomonoesterase activity. Similar analyses of label in PtdIns3P and PtdIns(3,4)P2 reveal the likely participation of these molecules in substrate cycles and hence for the first time the presence of PtdIns3P 3-phosphatase and PtdIns(3,4)P2 4-phosphatase activities in plants. PtdIns3P and PtdIns(3,4)P2 undergo turnover at rates similar to those of PtdIns4P and PtdIns(4,5)P2. Estimates are made of the relative sizes of the pools of phospholipid participating in the turnover process.

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17

Shashidhar, M. S. "Synthesis and applications of phosphatidylinositols and their analogues." Proceedings / Indian Academy of Sciences 106, no. 5 (October 1994): 1231–51. http://dx.doi.org/10.1007/bf02841930.

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18

D'Andrea, Gabriele, and M. Luisa Salucci. "Structures and names for inositol phosphates and phosphatidylinositols." Biochemical Education 21, no. 2 (April 1993): 98–101. http://dx.doi.org/10.1016/0307-4412(93)90056-6.

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19

Doering, T. L., M. S. Pessin, G. W. Hart, D. M. Raben, and P. T. Englund. "The fatty acids in unremodelled trypanosome glycosyl-phosphatidylinositols." Biochemical Journal 299, no. 3 (May 1, 1994): 741–46. http://dx.doi.org/10.1042/bj2990741.

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Glycolipid A, the precursor of the glycosyl-phosphatidylinositol (GPI) anchor of the trypanosome variant surface glycoprotein, is constructed in two phases. First, the glycan is assembled on phosphatidylinositol (PI), yielding a glycolipid termed A'. Second, glycolipid A' undergoes fatty acid remodelling, by deacylation and reacylation, to become the dimyristoyl species glycolipid A. In this paper, we examine the fatty acid content of glycolipid A' and its cellular progenitors. A' contains exclusively stearate at the sn-1 position and a complex mixture of fatty acids (including 18:0, 18:1, 18:2, 20:4 and 22:6) at sn-2. Presumably these fatty acids derive from stearate-containing PI species which initially enter the biosynthetic pathway. We compared the diacylglycerol species from glycolipid A' with those from phosphatidylinositol to determine whether a subset of stearate-containing PIs is utilized for GPI biosynthesis. We found that the spectrum of stearate-containing diacylglycerols in PI is similar to that in A', although the proportions of each compound differ. Total PI in general was highly enriched in stearate-containing species. Differences in composition between glycosylated PI and total cellular PI may be due to the substrate specificity of the sugar transferase which initiates the GPI biosynthetic pathway. Alternatively, the species of PI present at the endoplasmic reticulum site of GPI biosynthesis may differ from those in total PI.

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20

Min, Sang H., and Charles S. Abrams. "Why do phosphatidylinositol kinases have so many isoforms?" Biochemical Journal 423, no. 1 (September 14, 2009): e5-e8. http://dx.doi.org/10.1042/bj20091274.

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Macromolecules can be transported into the cells by endocytosis, either by phagocytosis or by pinocytosis. Typically, phagocytosis involves the uptake of solid large particles mediated by cell-surface receptors, whereas pinocytosis takes up fluid and solutes. The synthesis of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 plays fundamental roles in all forms of endocytosis. Curiously, almost all eukaryotic cells have multiple isoforms of the kinases that synthesize these critical phosphatidylinositols. In this issue of the Biochemical Journal, Namiko Tamura, Osamu Hazeki and co-workers report that the subunit p110α of the type I PI3K (phosphoinositide 3-kinase) is implicated in the phagocytosis and the pinocytosis of large molecules, whereas the receptor-mediated pinocytosis and micropinocytosis of small molecules do not seem to be controlled by this mechanism. The present commentary discusses recent literature that has begun to unravel why cells need so many phosphatidylinositol kinase isoforms, which were previously believed to be redundant.

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21

Abidi, S. L., T. L. Mounts, and K. A. Rennick. "Reversed-Phase Ion-Pair High-Performance Liquid Chromatography of Phosphatidylinositols." Journal of Liquid Chromatography 14, no. 3 (February 1991): 573–88. http://dx.doi.org/10.1080/01483919108049271.

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22

Leung, Lawrence W., Catherine Vilchèze, and Robert Bittman. "Synthesis of fluorescent phosphatidylinositols using a novel inositol H-phosphonate." Tetrahedron Letters 39, no. 19 (May 1998): 2921–24. http://dx.doi.org/10.1016/s0040-4039(98)00418-3.

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23

Kubiak, Robert J., and Karol S. Bruzik. "Comprehensive and Uniform Synthesis of All Naturally Occurring Phosphorylated Phosphatidylinositols." Journal of Organic Chemistry 68, no. 3 (February 2003): 960–68. http://dx.doi.org/10.1021/jo0206418.

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24

SHASHIDHAR, M. S. "ChemInform Abstract: Synthesis and Applications of Phosphatidylinositols and Their Analogues." ChemInform 26, no. 32 (August 17, 2010): no. http://dx.doi.org/10.1002/chin.199532279.

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25

Liu, Yinghui, Cornelia Mihai, Robert J. Kubiak, Mario Rebecchi, and Karol S. Bruzik. "Phosphorothiolate Analogues of Phosphatidylinositols as Assay Substrates for Phospholipase C." ChemBioChem 8, no. 12 (August 13, 2007): 1430–39. http://dx.doi.org/10.1002/cbic.200700061.

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26

Shi, J., M. Ju, WA Large, and AP Albert. "Pharmacological profile of phosphatidylinositol 3-kinases and related phosphatidylinositols mediating endothelinA receptor-operated native TRPC channels in rabbit coronary artery myocytes." British Journal of Pharmacology 166, no. 7 (July 9, 2012): 2161–75. http://dx.doi.org/10.1111/j.1476-5381.2012.01937.x.

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27

Saltiel, A. R., and P. Cuatrecasas. "In search of a second messenger for insulin." American Journal of Physiology-Cell Physiology 255, no. 1 (July 1, 1988): C1—C11. http://dx.doi.org/10.1152/ajpcell.1988.255.1.c1.

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Despite significant advances in the past few years on the chemistry and biology of insulin and its receptor, the molecular events that couple the insulin-receptor interaction to the regulation of cellular metabolism remain uncertain. Progress in this area has been complicated by the pleiotropic nature of insulin's actions. These most likely involve a complex network of pathways resulting in the coordination of mechanistically distinct cellular effects. Because the well-recognized mechanisms of signal transduction (i.e., cyclic nucleotides, ion channels) appear not to be central to insulin action, investigators have searched for a novel second messenger system. A low-molecular-weight substance has been identified that mimics certain actions of insulin on metabolic enzymes. This substance has an inositol glycan structure and is produced by the insulin-sensitive hydrolysis of a glycosyl-phosphatidylinositol in the plasma membrane. This hydrolysis reaction, which is catalyzed by a specific phospholipase C, also results in the production of a structurally distinct diacylglycerol that may selectively regulate one or more of the protein kinases C. The glycosyl-phosphatidyl-inositol precursor for the inositol glycan enzyme modulator is structurally analogous to the recently described glycosyl-phosphatidylinositol membrane protein anchor. Preliminary studies suggest that a subset of proteins anchored in this fashion might be released from cells by a similar insulin-sensitive, phospholipase-catalyzed reaction. Efforts are underway to determine the precise role of the metabolism of glycosyl-phosphatidylinositols in insulin action.

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28

Naslavsky, Naava, Juliati Rahajeng, Sylvie Chenavas, Paul L. Sorgen, and Steve Caplan. "EHD1 and Eps15 Interact with Phosphatidylinositols via Their Eps15 Homology Domains." Journal of Biological Chemistry 282, no. 22 (April 5, 2007): 16612–22. http://dx.doi.org/10.1074/jbc.m609493200.

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29

Ozaki, Akari, Atsushi Masayama, Hideo Nakano, and Yugo Iwasaki. "Synthesis of phosphatidylinositols having various inositol stereoisomers by engineered phospholipase D." Journal of Bioscience and Bioengineering 109, no. 4 (April 2010): 337–40. http://dx.doi.org/10.1016/j.jbiosc.2009.09.045.

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30

Hasanally, Devin, Andrea Edel, Rakesh Chaudhary, and Amir Ravandi. "Identification of Oxidized Phosphatidylinositols Present in OxLDL and Human Atherosclerotic Plaque." Lipids 52, no. 1 (December 2, 2016): 11–26. http://dx.doi.org/10.1007/s11745-016-4217-y.

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31

Bach, Tami L., Wesley T. Kerr, Yanfeng Wang, Eve Marie Bauman, Purnima Kine, Eileen L. Whiteman, Renell S. Morgan, et al. "PI3K regulates pleckstrin-2 in T-cell cytoskeletal reorganization." Blood 109, no. 3 (September 28, 2006): 1147–55. http://dx.doi.org/10.1182/blood-2006-02-001339.

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Abstract Pleckstrin-2 is composed of 2 pleckstrin homology (PH) domains and a disheveled–Egl-10–pleckstrin (DEP) domain. A lipid-binding assay revealed that pleckstrin-2 binds with greatest affinity to D3 and D5 phosphoinositides. Pleckstrin-2 expressed in Jurkat T cells bound to the cellular membrane and enhanced actin-dependent spreading only after stimulation of the T-cell antigen receptor or the integrin α4β1. A pleckstrin-2 variant containing point mutations in both PH domains failed to associate with the Jurkat membrane and had no effect on spreading under the same conditions. Although still membrane bound, a pleckstrin-2 variant containing point mutations in the DEP domain demonstrated a decreased ability to induce membrane ruffles and spread. Pleckstrin-2 also colocalized with actin at the immune synapse and integrin clusters via its PH domains. Although pleckstrin-2 can bind to purified D3 and D5 phosphoinositides, the intracellular membrane association of pleckstrin-2 and cell spreading are dependent on D3 phosphoinositides, because these effects were disrupted by pharmacologic inhibition of phosphatidylinositol 3-kinase (PI3K). Our results indicate that pleckstrin-2 uses its modular domains to bind to membrane-associated phosphatidylinositols generated by PI3K, whereby it coordinates with the actin cytoskeleton in lymphocyte spreading and immune synapse formation.

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32

MORRIS, THOMAS W., SVEN E. EKHOLM, GUIDO V. MARINETTI, LINDA I. PRENTICE, and PAULINE LEAKEY. "Gd-DTPA and Gd-DOTA Effects on Metabolism of Glucose and Phosphatidylinositols." Investigative Radiology 26 (November 1991): S209—S211. http://dx.doi.org/10.1097/00004424-199111001-00072.

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33

Hawse, William F., and Richard T. Cattley. "T cells transduce T-cell receptor signal strength by generating different phosphatidylinositols." Journal of Biological Chemistry 294, no. 13 (January 28, 2019): 4793–805. http://dx.doi.org/10.1074/jbc.ra118.006524.

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34

Xia, Tian, Hanlin Ren, Wenpeng Zhang, and Yu Xia. "Lipidome-wide characterization of phosphatidylinositols and phosphatidylglycerols on C C location level." Analytica Chimica Acta 1128 (September 2020): 107–15. http://dx.doi.org/10.1016/j.aca.2020.06.017.

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35

Brearley, C. A., and D. E. Hanke. "3- and 4-phosphorylated phosphatidylinositols in the aquatic plant Spirodela polyrhiza L." Biochemical Journal 283, no. 1 (April 1, 1992): 255–60. http://dx.doi.org/10.1042/bj2830255.

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Labelling of Spirodela polyrhiza L. plants with [3H]inositol and [32P]Pi yielded a series of phosphoinositides which were identified as PtdIns, PtdIns4P and PtdIns(4,5)P2. In addition, systematic degradation of a phospholipid extract identified PtdIns3P. Analysis of the distribution of 32P label between the monoester and diester phosphate groups of PtdIns3P and PtdIns4P revealed differences in the labelling of the monoester phosphate, suggesting that the two PtdInsP species are not synthesized or metabolized in a co-ordinate manner.

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36

Schares, Gereon, Christina F. Zinecker, Jörg Schmidt, Nahid Azzouz, Franz J. Conraths, Peter Gerold, and Ralph T. Schwarz. "Structural analysis of free and protein-bound glycosyl-phosphatidylinositols of Neospora caninum." Molecular and Biochemical Parasitology 105, no. 1 (January 5, 2000): 155–61. http://dx.doi.org/10.1016/s0166-6851(99)00168-1.

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37

Gerold, Peter, Boris Striepen, Barbara Reitter, Hildegard Geyer, Rudolf Geyer, Erwin Reinwald, Hans-Jörg Risse, and Ralph T. Schwarz. "Glycosyl-phosphatidylinositols ofTrypanosoma congolense: Two Common Precursors but a New Protein-anchor." Journal of Molecular Biology 261, no. 2 (August 1996): 181–94. http://dx.doi.org/10.1006/jmbi.1996.0451.

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38

Takahashi, Kei, Nao Shimada, Akihiko Nakajima, Satoshi Sawai, and Taro Toyota. "2P223 Development of a reconstituted system for localized phosphatidylinositols signaling on lipid membrane(13E. Biological & Artifical membrane: Signal transduction,Poster)." Seibutsu Butsuri 53, supplement1-2 (2013): S195. http://dx.doi.org/10.2142/biophys.53.s195_6.

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39

Hehnly, Heidi, and Stephen Doxsey. "Polarity sets the stage for cytokinesis." Molecular Biology of the Cell 23, no. 1 (January 2012): 7–11. http://dx.doi.org/10.1091/mbc.e11-06-0512.

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Cell polarity is important for a number of processes, from chemotaxis to embryogenesis. Recent studies suggest a new role for polarity in the orchestration of events during the final cell separation step of cell division called abscission. Abscission shares several features with cell polarization, including rearrangement of phosphatidylinositols, reorganization of microtubules, and trafficking of exocyst-associated membranes. Here we focus on how the canonical pathways for cell polarization and cell migration may play a role in spatiotemporal membrane trafficking events required for the final stages of cytokinesis.

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40

Finkelstein, Stella, Sidney M. Gospe, Kai Schuhmann, Andrej Shevchenko, Vadim Y. Arshavsky, and Ekaterina S. Lobanova. "Phosphoinositide Profile of the Mouse Retina." Cells 9, no. 6 (June 7, 2020): 1417. http://dx.doi.org/10.3390/cells9061417.

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Phosphoinositides are known to play multiple roles in eukaryotic cells. Although dysregulation of phosphoinositide metabolism in the retina has been reported to cause visual dysfunction in animal models and human patients, our understanding of the phosphoinositide composition of the retina is limited. Here, we report a characterization of the phosphoinositide profile of the mouse retina and an analysis of the subcellular localization of major phosphorylated phosphoinositide forms in light-sensitive photoreceptor neurons. Using chromatography of deacylated phosphatidylinositol headgroups, we established PI(4,5)P2 and PI(4)P as two major phosphorylated phosphoinositides in the retina. Using high-resolution mass spectrometry, we revealed 18:0/20:4 and 16:0/20:4 as major fatty-acyl chains of retinal phosphoinositides. Finally, analysis of fluorescent phosphoinositide sensors in rod photoreceptors demonstrated distinct subcellular distribution patterns of major phosphoinositides. The PI(4,5)P2 reporter was enriched in the inner segments and synapses, but was barely detected in the light-sensitive outer segments. The PI(4)P reporter was mostly found in the outer and inner segments and the areas around nuclei, but to a lesser degree in the synaptic region. These findings provide support for future mechanistic studies defining the biological significance of major mono- (PI(4)P) and bisphosphate (PI(4,5)P2) phosphatidylinositols in photoreceptor biology and retinal health.

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Perez, Marcos A., and Jennifer L. Watts. "Worms, Fat, and Death: Caenorhabditis elegans Lipid Metabolites Regulate Cell Death." Metabolites 11, no. 2 (February 23, 2021): 125. http://dx.doi.org/10.3390/metabo11020125.

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Caenorhabditis elegans is well-known as the model organism used to elucidate the genetic pathways underlying the first described form of regulated cell death, apoptosis. Since then, C. elegans investigations have contributed to the further understanding of lipids in apoptosis, especially the roles of phosphatidylserines and phosphatidylinositols. More recently, studies in C. elegans have shown that dietary polyunsaturated fatty acids can induce the non-apoptotic, iron-dependent form of cell death, ferroptosis. In this review, we examine the roles of various lipids in specific aspects of regulated cell death, emphasizing recent work in C. elegans.

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York, J. D., and P. W. Majerus. "Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells." Journal of Biological Chemistry 269, no. 11 (March 1994): 7847–50. http://dx.doi.org/10.1016/s0021-9258(17)37126-0.

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Schofield, L. "Regulation of host cell function by glycosyl-phosphatidylinositols of Plasmodium. Trypanosoma and Leishmania." Parasitology International 47 (August 1998): 51. http://dx.doi.org/10.1016/s1383-5769(98)80086-x.

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Heim, Sabina, and Karl G. Wagner. "Evidence of phosphorylated phosphatidylinositols in the growth cycle of suspension cultured plant cells." Biochemical and Biophysical Research Communications 134, no. 3 (February 1986): 1175–81. http://dx.doi.org/10.1016/0006-291x(86)90374-8.

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Schneider, P., J. E. Ralton, M. J. Mcconville, and M. A. J. Ferguson. "Analysis of the Neutral Glycan Fractions of Glycosyl-phosphatidylinositols by Thin-Layer Chromatography." Analytical Biochemistry 210, no. 1 (April 1993): 106–12. http://dx.doi.org/10.1006/abio.1993.1158.

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Hiroi, Y., R. Chen, H. Sawa, T. Hosoda, S. Kudoh, Y. Kobayashi, H. Aburatani, et al. "Cloning of murine glycosyl phosphatidylinositol anchor attachment protein, GPAA1." American Journal of Physiology-Cell Physiology 279, no. 1 (July 1, 2000): C205—C212. http://dx.doi.org/10.1152/ajpcell.2000.279.1.c205.

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Glycosyl phosphatidylinositols (GPIs) are used to anchor many proteins to the cell surface membrane and are utilized in all eukaryotic cells. GPI anchoring units are attached to proteins via a transamidase reaction mediated by a GPI transamidase complex. We isolated one of the components of this complex, mGPAA1 (murine GPI anchor attachment), by the signal sequence trap method. mGPAA1 cDNA is about 2 kb in length and encodes a putative 621 amino acid protein. The mGPAA1gene has 12 small exons and 11 small introns. mGPAA1 mRNA is ubiquitously expressed in mammalian cells, and in situ hybridization analysis revealed that it is abundant in the choroid plexus, skeletal muscle, osteoblasts of rib, and occipital bone in mouse embryos. Its expression levels and transamidation efficiency decreased with differentiation of embryonic stem cells. The 3T3 cell lines expressing antisense mGPAA1 failed to express GPI-anchored proteins on the cell surface membrane.

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Medh, J. D., and P. H. Weigel. "Separation of phosphatidylinositols and other phospholipids by two-step one-dimensional thin-layer chromatography." Journal of Lipid Research 30, no. 5 (May 1989): 761–64. http://dx.doi.org/10.1016/s0022-2275(20)38335-8.

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48

Hohman, R. J., T. Hultsch, and E. Talbot. "IgE receptor-mediated phosphatidylinositol hydrolysis and exocytosis from rat basophilic leukemia cells are independent of extracellular Ca2+ in a hypotonic buffer containing a high concentration of K+." Journal of Immunology 145, no. 11 (December 1, 1990): 3876–82. http://dx.doi.org/10.4049/jimmunol.145.11.3876.

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Abstract In isotonic buffer, IgE receptor-mediated exocytosis from rat basophilic leukemia cells is dependent on extracellular Ca2+, with half-maximal degranulation requiring 0.4 mM Ca2+. No significant exocytosis occurs in the absence of extracellular Ca2+. This absolute requirement for Ca2+ is eliminated by suspending the cells in a hypotonic buffer containing 60 to 80 mM K+; Na+ cannot substitute for K+. Optimal Ca2(+)-independent exocytosis occurs in a buffer containing 20 mM dipotassium Pipes, pH 7.1, 40 mM KCl, 5 mM glucose, 7 mM Mg acetate, 0.1% BSA, and 1 mM EGTA. The cells maintain this Ca2(+)-independent exocytosis even if they are preincubated with 1 mM EGTA for 40 min at 37 degrees C before triggering. Exocytosis is eliminated as isotonicity is approached by adding sucrose, NaCl, KCl, or potassium glutamate to the buffer. Quin 2 fluorescence measurements reveal only a very small rise in [Ca2+]i when the cells are triggered in hypotonic buffer in the absence of extracellular Ca2+ and the presence of 1 mM EGTA. In isotonic buffer, degranulation does not occur under conditions that lead to such a small rise in [Ca2+]i. Sustained IgE receptor-mediated phosphatidylinositol hydrolysis, which is also Ca2+ dependent in isotonic buffer, becomes independent of Ca2+ in the hypotonic buffer. In fact, the rate of phosphatidylinositol hydrolysis in hypotonic buffer in the absence of Ca2+ (and presence of 1 mM EGTA) is twice that observed in isotonic buffer in the presence of 1 mM Ca2+. These data show that in hypotonic buffer, the requirement of IgE receptor-mediated PI hydrolysis for extracellular Ca2+ is eliminated, and degranulation proceeds with a [Ca2+]i of 0.1 microM, the baseline level of [Ca2+]i found in resting cells. These results are consistent with the hypothesis that, in isotonic buffer, the Ca2+ requirement for mast cell degranulation is for the generation of second messengers via hydrolysis of membrane phosphatidylinositols.

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Grupp, S. A., and J. A. Harmony. "Increased phosphatidylinositol metabolism is an important but not an obligatory early event in B lymphocyte activation." Journal of Immunology 134, no. 6 (June 1, 1985): 4087–94. http://dx.doi.org/10.4049/jimmunol.134.6.4087.

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Abstract The phosphatidylinositol (PI) response has been implicated in membrane signaling and cell activation. The role of phospholipid metabolism among the early events in B cell activation has not been clear. We have treated murine B cells with anti-Ig antibody and lipopolysaccharide (LPS) and have found that, although anti-IgM induces the PI response, LPS does not. The increase in metabolic labeling of PI is specific to PI, and not the phosphatidylinositols. Anti-IgM unresponsive B cells from CBA/N mice, which may correspond to a specific functional subpopulation of normal B cells, do not increase PI metabolism in response to anti-IgM, nor do they undergo blastogenesis or DNA synthesis. Moreover, when these deficient B cells are given a stimulus sufficient to drive them into S (LPS + anti-IgM), there is still no corresponding activation of PI metabolism. These results are consistent with a two-signal model of xid B cell activation by anti-IgM. One very early signal primes the cells but does not induce the PI response. A second early signal is supplied by LPS. This signal sustains cells in the activated state, allowing them to receive yet other signals to proceed through G1 and progress further along the cell cycle. A similar sequence of events may occur in the normal B cell, with the first signal provided by priming with anti-IgM, and the second signal, the PI response, supported by a sufficiently high dose of anti-IgM to induce PI turnover and maintain the cell in G1.

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Parmar, Paroo N., and Charles A. Brearley. "Metabolism of 3- and 4-phosphorylated phosphatidylinositols in stomatal guard cells of Commelina communis L." Plant Journal 8, no. 3 (September 1995): 425–33. http://dx.doi.org/10.1046/j.1365-313x.1995.08030425.x.

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