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Journal articles on the topic 'Glycophosphatidylinositol'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

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1

PAQUETTE, CARRIE A., VILLA RAKOCHY, ALISON BUSH, and JUDITH L. VAN HOUTEN. "GLYCOPHOSPHATIDYLINOSITOL-ANCHORED PROTEINS INPARAMECIUM TETRAURELIA." Journal of Experimental Biology 204, no. 16 (2001): 2899–910. http://dx.doi.org/10.1242/jeb.204.16.2899.

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SUMMARYWe have begun to characterize the glycophosphatidylinositol (GPI)-anchored proteins of the Paramecium tetraurelia cell body surface where receptors and binding sites for attractant stimuli are found. We demonstrate here (i) that inositol-specific exogenous phospholipase C (PLC) treatment of the cell body membranes (pellicles) removes proteins with GPI anchors, (ii)that, as in P. primaurelia, there is an endogenous lipase that responds differently to PLC inhibitors compared with its response to an exogenous PLC, (iii) that salt and ethanol treatment of cells removes GPI-anchored proteins

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2

Coussen, Françoise, Annick Ayon, Anne Le Goff, Jacqueline Leroy, Jean Massoulié, and Suzanne Bon. "Addition of a Glycophosphatidylinositol to Acetylcholinesterase." Journal of Biological Chemistry 276, no. 30 (2001): 27881–92. http://dx.doi.org/10.1074/jbc.m010817200.

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3

Chen, Rui, Elizabeth I. Walter, Gregory Parker, et al. "Mammalian glycophosphatidylinositol anchor transfer to proteins and posttransfer deacylation." Proceedings of the National Academy of Sciences 95, no. 16 (1998): 9512–17. http://dx.doi.org/10.1073/pnas.95.16.9512.

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The glycophosphatidylinositol (GPI) anchors of proteins expressed on human erythrocytes and nucleated cells differ with respect to acylation of an inositol hydroxyl group, a structural feature that modulates their cleavability by PI-specific phospholipase C (PI-PLC). To determine how this GPI anchor modification is regulated, the precursor and protein-associated GPIs in two K562 cell transfectants (ATCC and .48) exhibiting alternatively PI-PLC-sensitive and resistant surface proteins were analyzed and the temporal relationship between GPI protein transfer and acquisition of PI-PLC sensitivity

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SCHENKMAN, S., N. YOSHIDA, and M. CARDOSODEALMEIDA. "Glycophosphatidylinositol-anchored proteins in metacyclic trypomastigotes of Trypanosoma cruzi." Molecular and Biochemical Parasitology 29, no. 2-3 (1988): 141–51. http://dx.doi.org/10.1016/0166-6851(88)90069-2.

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5

Nishina, Koren A., and Surachai Supattapone. "Immunodetection of glycophosphatidylinositol-anchored proteins following treatment with phospholipase C." Analytical Biochemistry 363, no. 2 (2007): 318–20. http://dx.doi.org/10.1016/j.ab.2007.01.032.

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6

Barboni, E., B. P. Rivero, A. J. George, et al. "The glycophosphatidylinositol anchor affects the conformation of Thy-1 protein." Journal of Cell Science 108, no. 2 (1995): 487–97. http://dx.doi.org/10.1242/jcs.108.2.487.

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Thy-1 has the structure of a single variable-type immunoglobulin domain anchored to the external face of the plasma membrane via a glycophosphatidylinositol moiety. When the lipid is removed from this anchor by either phospholipase C or D, the reactivity of the delipidated Thy-1 for a range of antibodies, including those known to be determined by amino acid residues, is impaired. We have investigated in detail the effect of delipidation on the reaction with the OX7 monoclonal antibody, determined by the allelic variant residue Arg 89. Analysis of the kinetics of OX7 binding shows that delipida

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7

Balsamo, Janne, and Jack Lilien. "The retina cell-surface N-acetylgalactosaminylphosphotransferase is anchored by a glycophosphatidylinositol." Biochemistry 32, no. 32 (1993): 8246–50. http://dx.doi.org/10.1021/bi00083a027.

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8

Kovač, Valerija, and Vladka Čurin Šerbec. "Prion Proteins Without the Glycophosphatidylinositol Anchor: Potential Biomarkers in Neurodegenerative Diseases." Biomarker Insights 13 (January 1, 2018): 117727191875664. http://dx.doi.org/10.1177/1177271918756648.

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Prion protein (PrP) is a biomolecule that is involved in neuronal signaling, myelinization, and the development of neurodegenerative diseases. In the cell, PrP is shed by the ADAM10 protease. This process generates PrP molecules that lack glycophosphatidylinositol anchor, and these molecules incorporate into toxic aggregates and neutralize toxic oligomers. Due to this dual role, these molecules are important biomarkers for neurodegenerative diseases. In this review, we present shed PrP as a potential biomarker, with a focus on PrP226*, which may be the main biomarker for predicting neurodegene

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9

Khodagholi, Fariba, Razieh Yazdanparast, and Akram Sadeghirizi. "The Glycophosphatidylinositol Anchor Oppositely Affects Unfolding and Refolding of Alkaline Phosphatase." Journal of Biomolecular Structure and Dynamics 25, no. 2 (2007): 189–94. http://dx.doi.org/10.1080/07391102.2007.10507168.

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10

Kristoffersen, E. K., K. O. Haram, B. Edvardsen, P. Ernst, and L. Bjørge. "Placental Expression of Glycophosphatidylinositol (GPI)-anchored Proteins in Paroxysmal Nocturnal Haemoglobinuria." Scandinavian Journal of Immunology 64, no. 2 (2006): 140–44. http://dx.doi.org/10.1111/j.1365-3083.2006.01777.x.

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11

Moran, P., and I. W. Caras. "A nonfunctional sequence converted to a signal for glycophosphatidylinositol membrane anchor attachment." Journal of Cell Biology 115, no. 2 (1991): 329–36. http://dx.doi.org/10.1083/jcb.115.2.329.

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The COOH terminus of decay-accelerating factor (DAF) contains a signal that directs glycophosphatidylinositol (GPI) membrane anchor attachment in a process involving concerted proteolytic removal of 28 COOH-terminal residues. At least two elements are required for anchor addition: a COOH-terminal hydrophobic domain and a cleavage/attachment site located NH2-terminal to it, requiring a small amino acid as the acceptor for GPI addition. We previously showed that the last 29-37 residues of DAF, making up the COOH-terminal hydrophobic domain plus 20 residues of the adjacent serine/threonine-rich d

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12

LEDERKREMER, Rosa M., Carlos LIMA, Maria I. RAMIREZ, and Olga L. CASAL. "Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors." European Journal of Biochemistry 192, no. 2 (1990): 337–45. http://dx.doi.org/10.1111/j.1432-1033.1990.tb19232.x.

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13

Bon, Suzanne, Terrone L. Rosenberry, and Jean Massouli�. "Amphiphilic, glycophosphatidylinositol-specific phospholipase C (PI-PLC)-insensitive monomers and dimers of acetylcholinesterase." Cellular and Molecular Neurobiology 11, no. 1 (1991): 157–72. http://dx.doi.org/10.1007/bf00712807.

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14

Chapin, Cheryl, Nicole A. Bailey, Linda W. Gonzales, Jae-Woo Lee, Robert F. Gonzalez, and Philip L. Ballard. "Distribution and surfactant association of carcinoembryonic cell adhesion molecule 6 in human lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 302, no. 2 (2012): L216—L225. http://dx.doi.org/10.1152/ajplung.00055.2011.

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Carcinoembryonic cell adhesion molecule 6 (CEACAM6) is a glycosylated, glycophosphatidylinositol-anchored protein expressed in epithelial cells of various primate tissues. It binds gram-negative bacteria and is overexpressed in human cancers. CEACAM6 is associated with lamellar bodies of cultured type II cells of human fetal lung and protects surfactant function in vitro. In this study, we characterized CEACAM6 expression in vivo in human lung. CEACAM6 was present in lung lavage of premature infants at birth and increased progressively in intubated infants with lung disease. Of surfactant-asso

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15

Tripathy, Sandeep K., Hamish R. C. Smith, Erika A. Holroyd, Jeanette T. Pingel, and Wayne M. Yokoyama. "Expression of m157, a Murine Cytomegalovirus-Encoded Putative Major Histocompatibility Class I (MHC-I)-Like Protein, Is Independent of Viral Regulation of Host MHC-I." Journal of Virology 80, no. 1 (2006): 545–50. http://dx.doi.org/10.1128/jvi.80.1.545-550.2006.

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ABSTRACT A murine cytomegalovirus (MCMV)-encoded protein, m157, has a putative major histocompatibility complex class I (MHC-I) structure and is recognized by the Ly49H NK cell activation receptor. Using a monoclonal antibody against m157, in this study we directly demonstrated that m157 is a cell surface-expressed glycophosphatidylinositol-anchored protein with early viral gene kinetics. Beta-2 microglobulin and TAP1 (transporter associated with antigen processing 1) were not required for its expression. MCMV-encoded proteins that down-regulate MHC-I did not affect the expression of m157. Thu

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16

Madsen, Robert, Uko E. Udodong, Carmichael Roberts, David R. Mootoo, Peter Konradsson, and Bert Fraser-Reid. "Studies Related to Synthesis of Glycophosphatidylinositol Membrane-Bound Protein Anchors. 6. Convergent Assembly of Subunits." Journal of the American Chemical Society 117, no. 5 (1995): 1554–65. http://dx.doi.org/10.1021/ja00110a011.

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17

CARAS, I. "Probing the signal for glycophosphatidylinositol anchor attachment using decay accelerating factor as a model system." Cell Biology International Reports 15, no. 9 (1991): 815–26. http://dx.doi.org/10.1016/0309-1651(91)90035-h.

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18

Fan, Zhongqi, Zhe Li, Zongge Xu, et al. "cspAInfluences Biofilm Formation and Drug Resistance in Pathogenic FungusAspergillus fumigatus." BioMed Research International 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/960357.

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The microbial cell wall plays a crucial role in biofilm formation and drug resistance.cspAencodes a repeat-rich glycophosphatidylinositol-anchored cell wall protein in the pathogenic fungusAspergillus fumigatus. To determine whethercspAhas a significant impact on biofilm development and sensitivity to antifungal drugs inA. fumigatus, a ΔcspAmutant was constructed by targeted gene disruption, and we then reconstituted the mutant to wild type by homologous recombination of a functionalcspAgene. Deletion ofcspAresulted in a rougher conidial surface, reduced biofilm formation, decreased resistance

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19

Murakata, Chikara, and Tomoya Ogawa. "Synthetic studies on glycophosphatidylinositol anchor: a highly efficient synthesis of glycobiosyl phosphatidylinositol through H-phosphonate approach." Tetrahedron Letters 32, no. 1 (1991): 101–4. http://dx.doi.org/10.1016/s0040-4039(00)71229-9.

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20

Mersha, Fana B., Leslie K. Cortes, Ashley N. Luck, et al. "Computational and experimental analysis of the glycophosphatidylinositol-anchored proteome of the human parasitic nematode Brugia malayi." PLOS ONE 14, no. 9 (2019): e0216849. http://dx.doi.org/10.1371/journal.pone.0216849.

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21

Thomas, P. M., and L. E. Samelson. "The glycophosphatidylinositol-anchored Thy-1 molecule interacts with the p60fyn protein tyrosine kinase in T cells." Journal of Biological Chemistry 267, no. 17 (1992): 12317–22. http://dx.doi.org/10.1016/s0021-9258(19)49841-4.

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22

Ash, Josée, Michel Dominguez, John J. M. Bergeron, David Y. Thomas, and Yves Bourbonnais. "The Yeast Proprotein Convertase Encoded byYAP3Is a Glycophosphatidylinositol-anchored Protein That Localizes to the Plasma Membrane." Journal of Biological Chemistry 270, no. 35 (1995): 20847–54. http://dx.doi.org/10.1074/jbc.270.35.20847.

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23

Davis, Eric M., Jihye Kim, Bridget L. Menasche, et al. "Comparative Haploid Genetic Screens Reveal Divergent Pathways in the Biogenesis and Trafficking of Glycophosphatidylinositol-Anchored Proteins." Cell Reports 11, no. 11 (2015): 1727–36. http://dx.doi.org/10.1016/j.celrep.2015.05.026.

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24

Lucia Cardoso de Almeida, M., Mervyn J. Turner, Boris B. Stambuk, and Sergio Schenkman. "Identification of an acid-lipase in human serum which is capable of solubilizing glycophosphatidylinositol-anchored proteins." Biochemical and Biophysical Research Communications 150, no. 1 (1988): 476–82. http://dx.doi.org/10.1016/0006-291x(88)90545-1.

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25

Chen, Rui, Jansen J. Knez, William C. Merrick, and M. Edward Medof. "Comparative efficiencies of C-terminal signals of native glycophosphatidylinositol (GPI)-anchored proproteins in conferring GPI-anchoring." Journal of Cellular Biochemistry 84, no. 1 (2001): 68–83. http://dx.doi.org/10.1002/jcb.1267.

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26

Puoti, A., and A. Conzelmann. "Structural characterization of free glycolipids which are potential precursors for glycophosphatidylinositol anchors in mouse thymoma cell lines." Journal of Biological Chemistry 267, no. 31 (1992): 22673–80. http://dx.doi.org/10.1016/s0021-9258(18)41724-3.

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27

Carlin, Lindsey E., Natalya V. Guseva, Michael R. Shey, Zuhair K. Ballas, and Jonathan W. Heusel. "The Glycophosphatidylinositol Anchor of the MCMV Evasin, m157, Facilitates Optimal Cell Surface Expression and Ly49 Receptor Recognition." PLoS ONE 8, no. 6 (2013): e67295. http://dx.doi.org/10.1371/journal.pone.0067295.

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28

Moran, P., and I. W. Caras. "Proteins containing an uncleaved signal for glycophosphatidylinositol membrane anchor attachment are retained in a post-ER compartment." Journal of Cell Biology 119, no. 4 (1992): 763–72. http://dx.doi.org/10.1083/jcb.119.4.763.

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Glycophosphatidylinositol (GPI)-anchored membrane proteins are initially synthesized with a cleavable COOH-terminal extension that signals anchor attachment. Overexpression in COS cells of hGH-DAF fusion proteins containing the GPI signal of decay accelerating factor (DAF) fused to the COOH-terminus of human growth hormone (hGH), produces both GPI-anchored hGH-DAF and uncleaved precursors that retain the GPI signal. Using hGH-DAF fusion proteins containing a mutated, noncleavable GPI signal, we show that uncleaved polypeptides are retained inside the cell and accumulate in a brefeldin A-sensit

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29

Nagata, Norikazu, Shigeru Taketani, Yasushi Adachi, et al. "A monoclonal antibody reactive with a glycophosphatidylinositol-anchored molecule on T cells defines CD4+ T cell subsets." European Journal of Immunology 23, no. 5 (1993): 1193–96. http://dx.doi.org/10.1002/eji.1830230535.

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30

FANKHAUSER, Christoph, and Andreas CONZELMANN. "Purification, biosynthesis and cellular localization of a major 125-kDa glycophosphatidylinositol-anchored membrane glycoprotein of Saccharomyces cerevisiae." European Journal of Biochemistry 195, no. 2 (1991): 439–48. http://dx.doi.org/10.1111/j.1432-1033.1991.tb15723.x.

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31

Kim, Jae-Il, Krystyna Surewicz, Pierluigi Gambetti, and Witold K. Surewicz. "The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro." FEBS Letters 583, no. 22 (2009): 3671–75. http://dx.doi.org/10.1016/j.febslet.2009.10.049.

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32

Ohashi, H., T. Hotta, A. Ichikawa, et al. "Peripheral blood cells are predominantly chimeric of affected and normal cells in patients with paroxysmal nocturnal hemoglobinuria: simultaneous investigation on clonality and expression of glycophosphatidylinositol-anchored proteins." Blood 83, no. 3 (1994): 853–59. http://dx.doi.org/10.1182/blood.v83.3.853.853.

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Abstract To investigate clonal compositions of hematologic cells in paroxysmal nocturnal hemoglobinuria (PNH), we analyzed peripheral blood (PB) cells of 12 female patients with PNH, by clonality analysis using X-chromosome inactivation and assessment of expression of glycophosphatidylinositol-anchored proteins (GPI-APs) by flow cytometry. Southern hybridization showed that granulocytes were monoclonal in three and polyclonal in eight patients, respectively, whereas lymphocytes were polyclonal in all nine patients examined. Expressions of CD16 and CD59 on granulocytes varied greatly in seven p

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Ohashi, H., T. Hotta, A. Ichikawa, et al. "Peripheral blood cells are predominantly chimeric of affected and normal cells in patients with paroxysmal nocturnal hemoglobinuria: simultaneous investigation on clonality and expression of glycophosphatidylinositol-anchored proteins." Blood 83, no. 3 (1994): 853–59. http://dx.doi.org/10.1182/blood.v83.3.853.bloodjournal833853.

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To investigate clonal compositions of hematologic cells in paroxysmal nocturnal hemoglobinuria (PNH), we analyzed peripheral blood (PB) cells of 12 female patients with PNH, by clonality analysis using X-chromosome inactivation and assessment of expression of glycophosphatidylinositol-anchored proteins (GPI-APs) by flow cytometry. Southern hybridization showed that granulocytes were monoclonal in three and polyclonal in eight patients, respectively, whereas lymphocytes were polyclonal in all nine patients examined. Expressions of CD16 and CD59 on granulocytes varied greatly in seven patients e

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34

Roberts, Carmichael, Robert Madsen, and Bert Fraser-Reid. "Studies Related to Synthesis of Glycophosphatidylinositol Membrane-Bound Protein Anchors. 5. n-Pentenyl Ortho Esters for Mannan Components." Journal of the American Chemical Society 117, no. 5 (1995): 1546–53. http://dx.doi.org/10.1021/ja00110a010.

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35

Yang, Hana, Seung Eun Lee, Seong Il Jeong, Cheung-Seog Park, Young-Ho Jin, and Yong Seek Park. "Differentially-expressed genes associated with glycophosphatidylinositol (GPI)-anchored proteins by diabetes-related toxic substances in human endothelial cells." BioChip Journal 6, no. 3 (2012): 262–70. http://dx.doi.org/10.1007/s13206-012-6309-y.

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36

Go, Gyeongyun, and Sang Hun Lee. "The Cellular Prion Protein: A Promising Therapeutic Target for Cancer." International Journal of Molecular Sciences 21, no. 23 (2020): 9208. http://dx.doi.org/10.3390/ijms21239208.

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Studies on the cellular prion protein (PrPC) have been actively conducted because misfolded PrPC is known to cause transmissible spongiform encephalopathies or prion disease. PrPC is a glycophosphatidylinositol-anchored cell surface glycoprotein that has been reported to affect several cellular functions such as stress protection, cellular differentiation, mitochondrial homeostasis, circadian rhythm, myelin homeostasis, and immune modulation. Recently, it has also been reported that PrPC mediates tumor progression by enhancing the proliferation, metastasis, and drug resistance of cancer cells.

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37

Longrée, Luc, Renaud Roufosse, Stéphanie Maréchal, Julie Goffinet, Renaud Maquet, and Christian Focan. "Paroxysmal nocturnal hemoglobinuria (PNH): An atypical case report." Case Reports in Internal Medicine 5, no. 1 (2018): 39. http://dx.doi.org/10.5430/crim.v5n1p39.

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Introduction: Paroxysmal nocturnal hemoglobinuria (PNH) also called Marchiafava-Micheli syndrome is a rare disease (1.3 case per million inviduals). It is a clonal disorder caused by a medullary stem cells acquired mutations on the PIG-A gene, inducing a partial or general deficit of proteins linking to cell membrane through a glycophosphatidylinositol (GPI) anchor.Case presentation: We confirmed the diagnosis of PNH in a 35-year-old woman presenting a relatively well tolerated but progressive pancytopenia and also a concomitant cyanocobalamin deficiency. The diagnosis was classically obtained

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38

Nicholson, Thomas B., and Clifford P. Stanners. "Specific inhibition of GPI-anchored protein function by homing and self-association of specific GPI anchors." Journal of Cell Biology 175, no. 4 (2006): 647–59. http://dx.doi.org/10.1083/jcb.200605001.

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The functional specificity conferred by glycophosphatidylinositol (GPI) anchors on certain membrane proteins may arise from their occupancy of specific membrane microdomains. We show that membrane proteins with noninteractive external domains attached to the same carcinoembryonic antigen (CEA) GPI anchor, but not to unrelated neural cell adhesion molecule GPI anchors, colocalize on the cell surface, confirming that the GPI anchor mediates association with specific membrane domains and providing a mechanism for specific signaling. This directed targeting was exploited by coexpressing an externa

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Nitzan, Keren, Roni Toledano, Shiran Shapira, Nadir Arber, and Ravid Doron. "Behavioral Characterizing of CD24 Knockout Mouse—Cognitive and Emotional Alternations." Journal of Personalized Medicine 11, no. 2 (2021): 105. http://dx.doi.org/10.3390/jpm11020105.

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CD24 is a small, glycophosphatidylinositol-anchored cell surface protein, mostly investigated with respect to cancer, inflammation, and autoimmune diseases. CD24 knockdown or inhibition has been used to test various biochemical mechanisms and neurological conditions; however, the association between CD24 and behavioral phenotypes has not yet been examined. This study aims to characterize cognitive and emotional functions of CD24 knockout mice (CD24−/− )compared with CD24 wild-type mice at three time-points: adolescence, young adulthood, and adulthood. Our results show that CD24−/− mice exhibit

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40

Deng, Yongqiang, Felix E. Rivera-Molina, Derek K. Toomre, and Christopher G. Burd. "Sphingomyelin is sorted at the trans Golgi network into a distinct class of secretory vesicle." Proceedings of the National Academy of Sciences 113, no. 24 (2016): 6677–82. http://dx.doi.org/10.1073/pnas.1602875113.

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One of the principal functions of the trans Golgi network (TGN) is the sorting of proteins into distinct vesicular transport carriers that mediate secretion and interorganelle trafficking. Are lipids also sorted into distinct TGN-derived carriers? The Golgi is the principal site of the synthesis of sphingomyelin (SM), an abundant sphingolipid that is transported. To address the specificity of SM transport to the plasma membrane, we engineered a natural SM-binding pore-forming toxin, equinatoxin II (Eqt), into a nontoxic reporter termed Eqt-SM and used it to monitor intracellular trafficking of

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Nicholson, Thomas B., and Clifford P. Stanners. "Identification of a novel functional specificity signal within the GPI anchor signal sequence of carcinoembryonic antigen." Journal of Cell Biology 177, no. 2 (2007): 211–18. http://dx.doi.org/10.1083/jcb.200701158.

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Exchanging the glycophosphatidylinositol (GPI) anchor signal sequence of neural cell adhesion molecule (NCAM) for the signal sequence of carcinoembryonic antigen (CEA) generates a mature protein with NCAM external domains but CEA-like tumorigenic activity. We hypothesized that this resulted from the presence of a functional specificity signal within this sequence and generated CEA/NCAM chimeras to identify this signal. Replacing the residues (GLSAG) 6–10 amino acids downstream of the CEA anchor addition site with the corresponding NCAM residues resulted in GPI-anchored proteins lacking the CEA

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Fiore, Vincent F., Patrick W. Strane, Anton V. Bryksin, Eric S. White, James S. Hagood, and Thomas H. Barker. "Conformational coupling of integrin and Thy-1 regulates Fyn priming and fibroblast mechanotransduction." Journal of Cell Biology 211, no. 1 (2015): 173–90. http://dx.doi.org/10.1083/jcb.201505007.

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Progressive fibrosis is characterized by excessive deposition of extracellular matrix (ECM), resulting in gross alterations in tissue mechanics. Changes in tissue mechanics can further augment scar deposition through fibroblast mechanotransduction. In idiopathic pulmonary fibrosis, a fatal form of progressive lung fibrosis, previous work has shown that loss of Thy-1 (CD90) expression in fibroblasts correlates with regions of active fibrogenesis, thus representing a pathologically relevant fibroblast subpopulation. We now show that Thy-1 is a regulator of fibroblast rigidity sensing. Thy-1 phys

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43

Sikorska, Natalia, Leticia Lemus, Auxiliadora Aguilera-Romero, et al. "Limited ER quality control for GPI-anchored proteins." Journal of Cell Biology 213, no. 6 (2016): 693–704. http://dx.doi.org/10.1083/jcb.201602010.

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Endoplasmic reticulum (ER) quality control mechanisms target terminally misfolded proteins for ER-associated degradation (ERAD). Misfolded glycophosphatidylinositol-anchored proteins (GPI-APs) are, however, generally poor ERAD substrates and are targeted mainly to the vacuole/lysosome for degradation, leading to predictions that a GPI anchor sterically obstructs ERAD. Here we analyzed the degradation of the misfolded GPI-AP Gas1* in yeast. We could efficiently route Gas1* to Hrd1-dependent ERAD and provide evidence that it contains a GPI anchor, ruling out that a GPI anchor obstructs ERAD. Ins

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44

Nishida, Takahiro, and Hiroaki Kataoka. "Glypican 3-Targeted Therapy in Hepatocellular Carcinoma." Cancers 11, no. 9 (2019): 1339. http://dx.doi.org/10.3390/cancers11091339.

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Glypican-3 (GPC3) is an oncofetal glycoprotein attached to the cell membrane by a glycophosphatidylinositol anchor. GPC3 is overexpressed in some kinds of tumors, particularly hepatocellular carcinoma (HCC). The prognostic significance of serum GPC3 levels and GPC3 immunoreactivity in tumor cells has been defined in patients with HCC. In addition to its usefulness as a biomarker, GPC3 has attracted attention as a novel therapeutic target molecule, and clinical trials targeting GPC3 are in progress. The major mechanism of anti-GPC3 antibody (GPC3Ab) against cancer cells is antibody-dependent ce

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45

Dulau-Florea, Alina E., Neal S. Young, Irina Maric, et al. "Bone Marrow as a Source of Cells for Paroxysmal Nocturnal Hemoglobinuria Detection." American Journal of Clinical Pathology 150, no. 3 (2018): 273–82. http://dx.doi.org/10.1093/ajcp/aqy053.

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Abstract Objectives To determine fluorescently labeled aerolysin (FLAER) binding and glycophosphatidylinositol–anchored protein expression in bone marrow (BM) cells of healthy volunteers and patients with paroxysmal nocturnal hemoglobinuria (PNH) detected in peripheral blood (PB); compare PNH clone size in BM and PB; and detect PNH in BM by commonly used antibodies. Methods Flow cytometry analysis of FLAER binding to leukocytes and expression of CD55/CD59 in erythrocytes. Analysis of CD16 in neutrophils and CD14 in monocytes in BM. Results FLAER binds to all normal BM leukocytes, and binding i

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Maillard, Antoine P., and Yves Gaudin. "Rabies virus glycoprotein can fold in two alternative, antigenically distinct conformations depending on membrane-anchor type." Journal of General Virology 83, no. 6 (2002): 1465–76. http://dx.doi.org/10.1099/0022-1317-83-6-1465.

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Rabies virus glycoprotein (G) is a trimeric type I transmembrane glycoprotein that mediates both receptor recognition and low pH-induced membrane fusion. We have previously demonstrated that a soluble form of the ectodomain of G (G1–439), although secreted, is folded in an alternative conformation, which is monomeric and antigenically distinct from the native state of the complete, membrane-anchored glycoprotein. This has raised questions concerning the role of the transmembrane domain (TMD) in the correct native folding of the ectodomain. Here, we show that an ectodomain anchored in the membr

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Moran, P., and I. W. Caras. "Fusion of sequence elements from non-anchored proteins to generate a fully functional signal for glycophosphatidylinositol membrane anchor attachment." Journal of Cell Biology 115, no. 6 (1991): 1595–600. http://dx.doi.org/10.1083/jcb.115.6.1595.

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Glycophosphatidylinositol (GPI) membrane anchor attachment is directed by a cleavable signal at the COOH terminus of the protein. The complete lack of homology among different GPI-anchored proteins suggests that this signal is of a general nature. Previous analysis of the GPI signal of decay accelerating factor (DAF) suggests that the minimal requirements for GPI attachment are (a) a hydrophobic domain and (b) a cleavage/attachment site consisting of a pair of small residues positioned 10-12 residues NH2-terminal to a hydrophobic domain. As an ultimate test of these rules we constructed four s

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Duval, N., J. Massoulié, and S. Bon. "H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms." Journal of Cell Biology 118, no. 3 (1992): 641–53. http://dx.doi.org/10.1083/jcb.118.3.641.

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We analyzed the production of Torpedo marmorata acetylcholinesterase (AChE) in transfected COS cells. We report that the presence of an aspartic acid at position 397, homologous to that observed in other cholinesterases and related enzymes (Krejci, E., N. Duval, A. Chatonnet, P. Vincens, and J. Massoulié. 1991. Proc. Natl. Acad. Sci. USA. 88:6647-6651), is necessary for catalytic activity. The presence of an asparagine in the previously reported cDNA sequence (Sikorav, J.L., E. Krejci, and J. Massoulié. 1987. EMBO (Eur. Mol. Biol. Organ.) J. 6:1865-1873) was most likely due to a cloning error

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Puoti, A., C. Desponds, C. Fankhauser, and A. Conzelmann. "Characterization of glycophospholipid intermediate in the biosynthesis of glycophosphatidylinositol anchors accumulating in the Thy-1-negative lymphoma line SIA-b." Journal of Biological Chemistry 266, no. 31 (1991): 21051–59. http://dx.doi.org/10.1016/s0021-9258(18)54819-5.

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Baron, Gerald S., Andrew G. Hughson, Gregory J. Raymond, et al. "Effect of Glycans and the Glycophosphatidylinositol Anchor on Strain Dependent Conformations of Scrapie Prion Protein: Improved Purifications and Infrared Spectra." Biochemistry 50, no. 21 (2011): 4479–90. http://dx.doi.org/10.1021/bi2003907.

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