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101. Polyglucosan neurotoxicity caused by glycogen branching enzyme deficiency can be reversed by inhibition of glycogen synthase

Author

Or Kakhlon, Tatsuo Terashima, Hasan O. Akman, Otto Baba, Salvatore DiMauro, Naomi Feinstein, Yan Liu, Hava Glickstein, and Alexander Lossos

Subjects
Primary Cell Culture, Apoptosis, Real-Time Polymerase Chain Reaction, Biochemistry, Glycogen debranching enzyme, Cellular and Molecular Neuroscience, chemistry.chemical_compound, Glycogen phosphorylase, Adenosine Triphosphate, Transduction, Genetic, 1,4-alpha-Glucan Branching Enzyme, Glycogen branching enzyme, Animals, Humans, Lymphocytes, Enzyme Inhibitors, Phosphorylation, RNA, Small Interfering, Glycogen synthase, GSK3B, Glucans, Aged, Cerebral Cortex, Glycogen binding, biology, Glycogen, TOR Serine-Threonine Kinases, Fibroblasts, Glycogen Storage Disease, Rats, Glycogen Branching Enzyme Deficiency, Glycogen Synthase, chemistry, Microscopy, Fluorescence, Starvation, biology.protein, Female, Neurotoxicity Syndromes
Abstract

Uncontrolled elongation of glycogen chains, not adequately balanced by their branching, leads to the formation of an insoluble, presumably neurotoxic, form of glycogen called polyglucosan. To test the suspected pathogenicity of polyglucosans in neurological glycogenoses, we have modeled the typical glycogenosis Adult Polyglucosan Body Disease (APBD) by suppressing glycogen branching enzyme 1 (GBE1, EC 2.4.1.18) expression using lentiviruses harboring short hairpin RNA (shRNA). GBE1 suppression in embryonic cortical neurons led to polyglucosan accumulation and associated apoptosis, which were reversible by rapamycin or starvation treatments. Further analysis revealed that rapamycin and starvation led to phosphorylation and inactivation of glycogen synthase (GS, EC 2.4.1.11), dephosphorylated and activated in the GBE1-suppressed neurons. These protective effects of rapamycin and starvation were reversed by overexpression of phosphorylation site mutant GS only if its glycogen binding site was intact. While rapamycin and starvation induce autophagy, autophagic maturation was not required for their corrective effects, which prevailed even if autophagic flux was inhibited by vinblastine. Furthermore, polyglucosans were not observed in any compartment along the autophagic pathway. Our data suggest that glycogen branching enzyme repression in glycogenoses can cause pathogenic polyglucosan buildup, which might be corrected by GS inhibition. Knockdown of glycogen branching enzyme in neurons led to accumulation of an insoluble form of glycogen called polyglucosan, to apoptosis and to activation of glycogen synthase. These effects were reversed by glycogen synthase inhibition through starvation and rapamycin treatments, suggesting a potential therapeutic value of glycogen synthase inhibition for treating glycogen storage disorders.

Published
2013

103. Adult polyglucosan body disease: Natural History and Key Magnetic Resonance Imaging Findings

Author

Thierry Maisonobe, Roseline Froissart, Alexis Brice, Marjo S. van der Knaap, Frédéric Sedel, Brent L. Fogel, Fanny Mochel, Richard Levy, Hanna Rosenmann, Or Kakhlon, Sophie Demeret, Mary Wallace, Catherine Lubetzki, Alexander Lossos, Hasan O. Akman, Marjan E. Steenweg, Alexandra Durr, Bruno Barcelos Da Nobrega, J. Michael Powers, J. Moshe Gomori, Marvin R. Natowicz, Pascal Laforêt, Raphael Schiffmann, Varda Barash, Neuroscience Campus Amsterdam - Childhood White Matter Diseases, Other departments, Neurology, Pediatric surgery, and NCA - Childhood White Matter Diseases

Subjects
Spastic gait, Pathology, medicine.medical_specialty, medicine.diagnostic_test, business.industry, Leukodystrophy, Magnetic resonance imaging, Adult polyglucosan body disease, medicine.disease, Article, Natural history, Peripheral neuropathy, Neurology, SDG 3 - Good Health and Well-being, Clinical diagnosis, medicine, Neurology (clinical), Glycogen storage disease type IV, business
Abstract

Objective: Adult polyglucosan body disease (APBD) is an autosomal recessive leukodystrophy characterized by neurogenic bladder, progressive spastic gait, and peripheral neuropathy. Polyglucosan bodies accumulate in the central and peripheral nervous systems and are often associated with glycogen branching enzyme (GBE) deficiency. To improve clinical diagnosis and enable future evaluation of therapeutic strategies, we conducted a multinational study of the natural history and imaging features of APBD. Methods: We gathered clinical, biochemical, and molecular findings in 50 APBD patients with GBE deficiency from Israel, the United States, France, and the Netherlands. Brain and spine magnetic resonance images were reviewed in 44 patients. Results: The most common clinical findings were neurogenic bladder (100%), spastic paraplegia with vibration loss (90%), and axonal neuropathy (90%). The median age was 51 years for the onset of neurogenic bladder symptoms, 63 years for wheelchair dependence, and 70 years for death. As the disease progressed, mild cognitive decline may have affected up to half of the patients. Neuroimaging showed hyperintense white matter abnormalities on T2 and fluid attenuated inversion recovery sequences predominantly in the periventricular regions, the posterior limb of the internal capsule, the external capsule, and the pyramidal tracts and medial lemniscus of the pons and medulla. Atrophy of the medulla and spine was universal. p.Y329S was the most common GBE1 mutation, present as a single heterozygous (28%) or homozygous (48%) mutation. Interpretation: APBD with GBE deficiency, with occasional exceptions, is a clinically homogenous disorder that should be suspected in patients with adult onset leukodystrophy or spastic paraplegia with early onset of urinary symptoms and spinal atrophy. ANN NEUROL 2012;72:433-441. Copyright © 2012 American Neurological Association.

Published
2012
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104. Neurological Disorders Associated with Iron Misdistribution: The Therapeutic Potential of Siderophores

Author

Arnold Munnich, Or Kakhlon, Z. Ioav Cabantchik, and Bill Breuer

Subjects
Siderophore, Ataxia, biology, Neurodegeneration with brain iron accumulation, business.industry, Oxidative phosphorylation, Mitochondrion, Pharmacology, medicine.disease, chemistry.chemical_compound, chemistry, Frataxin, biology.protein, medicine, medicine.symptom, Deferiprone, business, Cell damage
Abstract

The association between iron accumulation and oxidative cell damage in specific regions of the brain has raised the possibility of using iron chelation as a therapeutic strategy in neurodegenerative disorders. In this review, Friedreich’s ataxia (FRDA) is described as a paradigm of a disorder in which cell damage is associated with misdistribution of cell iron resulting from aberrant utilization of the metal by mitochondria. Frataxin-deficient cells, serving as an in vitro model of FRDA, were used as a model for testing the effects of a chelator with the ability to sequester cell iron as well as to donate it to biological acceptors inside or outside cells (termed here a siderophore). The clinically used siderophore deferiprone (DFP) was shown to reduce mitochondrial labile iron accumulation and restore cell functions affected by frataxin deficiency. In a translation of these findings to the clinical setting, moderate doses of DFP were administered to selected patients with FRDA or neurodegeneration with brain iron accumulation (NBIA) as part of open-label studies. Treatment with DFP resulted in a significant reduction in foci of brain iron accumulation and in some functional improvements, with only minor changes in body iron stores. The prospects of using drug-mediated iron relocation vs. chelation are critically discussed in relation to other neurodegenerative disorders in which accumulated (toxic) iron has been implicated as a causative factor in regional oxidative damage, such as Parkinson’s disease or Alzheimer’s disease.

Published
2010
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105. An exon trap with proper poly-A site in the GBE1 is the common missing cause in Adult Polyglucosan Body Disease (S42.006)

Author

Akman, Orhan H., primary, Kakhlon, Or, additional, Coku, Jorida, additional, Peverelli, Lorenzo, additional, Rosenmann, Hanna, additional, Rozenstein-Tsalkovich, Lea, additional, Turnbull, Julie, additional, Meiner, Vardiella, additional, Chama, Liat, additional, Lerer, Israela, additional, Shpitzen, Shoshi, additional, Leitersdorf, Eran, additional, Paradas Lopez, Carmen, additional, Wallace, Mary, additional, Schiffmann, Raphael, additional, DiMauro, Salvatore, additional, Lossos, Alexander, additional, and Minassian, Berge, additional

Published
2015
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106. Deep IntronicGBE1Mutation in Manifesting Heterozygous Patients With Adult Polyglucosan Body Disease

Author

Akman, H. Orhan, primary, Kakhlon, Or, additional, Coku, Jorida, additional, Peverelli, Lorenzo, additional, Rosenmann, Hanna, additional, Rozenstein-Tsalkovich, Lea, additional, Turnbull, Julie, additional, Meiner, Vardiella, additional, Chama, Liat, additional, Lerer, Israela, additional, Shpitzen, Shoshi, additional, Leitersdorf, Eran, additional, Paradas, Carmen, additional, Wallace, Mary, additional, Schiffmann, Raphael, additional, DiMauro, Salvatore, additional, Lossos, Alexander, additional, and Minassian, Berge A., additional

Published
2015
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109. Cell functions impaired by frataxin deficiency are restored by drug-mediated iron relocation

Author

Naomi Melamed-Book, Chunye Lu, Hila Manning, Or Kakhlon, Arnold Munnich, William Breuer, Z. Ioav Cabantchik, and Gino A Cortopassi

Subjects
Pyridones, Iron, Immunology, Mitochondrion, medicine.disease_cause, Iron Chelating Agents, Biochemistry, Aconitase, DNA, Mitochondrial, Cell Line, chemistry.chemical_compound, Adenosine Triphosphate, Oxygen Consumption, Sideroblastic anemia, Iron-Binding Proteins, medicine, Humans, Deferiprone, Inner mitochondrial membrane, biology, Cell Biology, Hematology, medicine.disease, Cell biology, Mitochondria, chemistry, Friedreich Ataxia, Frataxin, biology.protein, Oxidative stress, Anemia of chronic disease, DNA Damage
Abstract

Various human disorders are associated with misdistribution of iron within or across cells. Friedreich ataxia (FRDA), a deficiency in the mitochondrial iron-chaperone frataxin, results in defective use of iron and its misdistribution between mitochondria and cytosol. We assessed the possibility of functionally correcting the cellular properties affected by frataxin deficiency with a siderophore capable of relocating iron and facilitating its metabolic use. Adding the chelator deferiprone at clinical concentrations to inducibly frataxin-deficient HEK-293 cells resulted in chelation of mitochondrial labile iron involved in oxidative stress and in reactivation of iron-depleted aconitase. These led to (1) restoration of impaired mitochondrial membrane and redox potentials, (2) increased adenosine triphosphate production and oxygen consumption, and (3) attenuation of mitochondrial DNA damage and reversal of hypersensitivity to staurosporine-induced apoptosis. Permeant chelators of higher affinity than deferiprone were not as efficient in restoring affected functions. Thus, although iron chelation might protect cells from iron toxicity, rendering the chelated iron bioavailable might underlie the capacity of deferiprone to restore cell functions affected by frataxin deficiency, as also observed in FRDA patients. The siderophore-like properties of deferiprone provide a rational basis for treating diseases of iron misdistribution, such as FRDA, anemia of chronic disease, and X-linked sideroblastic anemia with ataxia.

Published
2008

110. Pompe disease: Shared and unshared features of lysosomal storage disorders

Author

Nina Raben, Rachel Myerowitz, Or Kakhlon, Jeong-A Lim, and Lishu Li

Subjects
autophagy, calcium, Glycogen, Autophagy, General Engineering, Pompe disease, Disease, Metabolic myopathy, Biology, Mitochondrion, medicine.disease, Addendum, Lipofuscin, mitochondria, chemistry.chemical_compound, medicine.anatomical_structure, chemistry, Lysosome, Immunology, lysosome, medicine, Substrate reduction therapy, lysosomal storage diseases
Abstract

Pompe disease, an inherited deficiency of lysosomal acid α-glucosidase (GAA), is a severe metabolic myopathy with a wide range of clinical manifestations. It is the first recognized lysosomal storage disorder and the first neuromuscular disorder for which a therapy (enzyme replacement) has been approved. As GAA is the only enzyme that hydrolyses glycogen to glucose in the acidic environment of the lysosome, its deficiency leads to glycogen accumulation within and concomitant enlargement of this organelle. Since the introduction of the therapy, the overall understanding of the disease has progressed significantly, but the pathophysiology of muscle damage is still not fully understood. The emerging complex picture of the pathological cascade involves disturbance of calcium homeostasis, mitochondrial abnormalities, dysfunctional autophagy, accumulation of toxic undegradable materials, and accelerated production of lipofuscin deposits that are unrelated to aging. The relationship of Pompe disease to other lysosomal storage disorders and potential therapeutic interventions for Pompe disease are discussed.

Published
2015
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111. GGA function is required for maturation of neuroendocrine secretory granules

Author

Banafshé Larijani, Or Kakhlon, Prabhat Sakya, Sharon A. Tooze, and Rose Watson

Subjects
endocrine system, Green Fluorescent Proteins, Prohormone convertase, Proprotein convertase 2, Down-Regulation, Clathrin, Membrane Fusion, PC12 Cells, General Biochemistry, Genetics and Molecular Biology, Receptor, IGF Type 2, Article, Chromogranins, Syntaxin, Animals, RNA, Small Interfering, Molecular Biology, Budding, General Immunology and Microbiology, biology, ADP-Ribosylation Factors, Qa-SNARE Proteins, General Neuroscience, Secretory Vesicles, Lipid bilayer fusion, Signal transducing adaptor protein, Clathrin-Coated Vesicles, Molecular biology, Transport protein, Cell biology, Rats, Adaptor Proteins, Vesicular Transport, Protein Transport, Proprotein Convertase 2, Mutation, biology.protein
Abstract

Secretory granule (SG) maturation has been proposed to involve formation of clathrin-coated vesicles (CCVs) from immature SGs (ISGs). We tested the effect of inhibiting CCV budding by using the clathrin adaptor GGA (Golgi-associated, gamma-ear-containing, ADP-ribosylation factor-binding protein) on SG maturation in neuroendocrine cells. Overexpression of a truncated, GFP-tagged GGA, VHS (Vps27, Hrs, Stam)-GAT (GGA and target of myb (TOM))-GFP led to retention of MPR, VAMP4, and syntaxin 6 in mature SGs (MSGs), suggesting that CCV budding from ISGs is inhibited by the SG-localizing VHS-GAT-GFP. Furthermore, VHS-GAT-GFP-overexpression disrupts prohormone convertase 2 (PC2) autocatalytic cleavage, processing of secretogranin II to its product p18, and the correlation between PC2 and p18 levels. All these effects were not observed if full-length GGA1-GFP was overexpressed. Neither GGA1-GFP nor VHS-GAT-GFP perturbed SG protein budding from the TGN, or homotypic fusion of ISGs. Reducing GGA3 levels by using short interfering (si)RNA also led to VAMP4 retention in SGs, and inhibition of PC2 activity. Our results suggest that inhibition of CCV budding from ISGs downregulates the sorting from the ISGs and perturbs the intragranular activity of PC2.

Published
2005

112. Defective ATP breakdown activity related to an ENTPD1 gene mutation demonstrated using 31P NMR spectroscopy.

Author

Nardi-Schreiber, Atara, Sapir, Gal, Gamliel, Ayelet, Kakhlon, Or, Sosna, Jacob, Gomori, J. Moshe, Meiner, Vardiella, Lossos, Alexander, and Katz-Brull, Rachel

Subjects
ADENOSINE triphosphate, GENETIC mutation, NUCLEAR magnetic resonance spectroscopy
Abstract

The ecto-nucleoside triphosphate diphosphohydrolase-1 (E-NTPDase-1, CD39) enzyme is responsible for the breakdown of extracellular ATP to ADP and then to AMP by a two-step process. Defective CD39 activity has been described in a variety of medical conditions including malignancy and rheumatic diseases and has been proved to be of major diagnostic and clinical importance. Here we show for the first time that a 31P NMR spectroscopy methodology enables the quantification of these two steps in a single blood sample. We have applied this assay to determine the E-NTPDase activity on human mononuclear cells taken from two siblings affected by a stop-codon mutation in the ENTPD1 gene, their obligatory heterozygous parents, and healthy volunteers. The affected subjects presented low ATP breakdown activity, mainly expressed as low AMP production. [ABSTRACT FROM AUTHOR]

Published
2017
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113. Intracellular and extracellular labile iron pools

Author

Z Ioav, Cabantchik, Or, Kakhlon, Silvina, Epsztejn, Giulianna, Zanninelli, and William, Breuer

Subjects
Intracellular Fluid, Iron, Transferrin, Deferoxamine, Iron Chelating Agents, Cell Line, Kinetics, Ferritins, Animals, Humans, Apoproteins, Extracellular Space, Fluorescent Dyes, Protein Binding
Published
2003

114. The labile iron pool: characterization, measurement, and participation in cellular processes(1)

Author

Or, Kakhlon and Z Ioav, Cabantchik

Subjects
Iron, Deferoxamine, Fluoresceins, Iron Chelating Agents, Oxidative Stress, Iron-Binding Proteins, Animals, Homeostasis, Humans, Fluorometry, Organic Chemicals, Reactive Oxygen Species, Oxidation-Reduction, Fluorescent Dyes, Subcellular Fractions
Abstract

The cellular labile iron pool (LIP) is a pool of chelatable and redox-active iron, which is transitory and serves as a crossroad of cell iron metabolism. Various attempts have been made to analyze the levels of LIP following cell disruption. The chemical identity of this pool has remained poorly characterized due to the multiplicity of iron ligands present in cells. However, the levels of LIP recently have been assessed with novel nondisruptive techniques that rely on the application of fluorescent metalosensors. Methodologically, a fluorescent chelator loaded into living cells binds to components of the LIP and undergoes stoichiometric fluorescence quenching. The latter is revealed and quantified in situ by addition of strong permeating iron chelators. Depending on the intracellular distribution of the sensing and chelating probes, LIP can be differentially traced in subcellular structures, allowing the dynamic assessment of its levels and roles in specific cell compartments. The labile nature of LIP was also revealed by its capacity to promote formation of reactive oxygen species (ROS), whether from endogenous or exogenous redox-active sources. LIP and ROS levels were shown to follow similar "rise and fall" patterns as a result of changes in iron import vs. iron chelation or ferritin (FT) degradation vs. ferritin synthesis. Those patterns conform with the accepted role of LIP as a self-regulatory pool that is sensed by cytosolic iron regulatory proteins (IRPs) and feedback regulated by IRP-dependent expression of iron import and storage machineries. However, LIP can also be modulated by biochemical mechanisms that override the IRP regulatory loops and, thereby, contribute to basic cellular functions. This review deals with novel methodologies for assessing cellular LIP and with recent studies in which changes in LIP and ROS levels played a determining role in cellular processes.

Published
2002

115. Intracellular and Extracellular Labile Iron Pools

Author

Or Kakhlon, Z. Ioav Cabantchik, William Breuer, Giulianna Zanninelli, and Silvina Epsztejn

Subjects
Siderophore, chemistry.chemical_compound, Membrane, biology, Biochemistry, Chemistry, Hereditary hemochromatosis, biology.protein, Extracellular, Phospholipid, Chelation, Intracellular, Organic anion
Abstract

Labile forms of iron present in biological systems are defined as ionic Fe complexes that are redox active. They comprise a heterogeneous population of organic anions (phosphates and carboxylates), poly-functional ligands (i.e. chelates, siderophores and polypeptides) or surface components of membranes (e.g. phospholipid head groups) or extracellular matrix (e.g. glycans and sulfonates), which bind both forms of iron (II and III). Collectively, they define the respective labile iron pools (LIP), which can be of cellular (CLIP) or extracellular (ECLIP) nature. Operationally, those pools are characterized in terms of their propensity to engage in redox-cycling in an oxygenated environment and/or following pro-oxidant challenges. Methodologically, CLIP and ECLIP can be assessed in terms of iron reactivity and/ or the ability of the metal to undergo chelation by high affinity binding siderophores or chelators. Therapeutically, the LIPs are the immediate targets of chelators designed to reduce iron load in the entire organism, with emphasis on organs of accumulation such as the liver.

Published
2002
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116. Repression of the heavy ferritin chain increases the labile iron pool of human K562 cells

Author

O, Kakhlon, Y, Gruenbaum, and Z I, Cabantchik

Subjects
Protein Subunits, Base Sequence, Iron, Ferritins, Receptors, Transferrin, Humans, RNA, Messenger, K562 Cells, Reactive Oxygen Species, Transfection, DNA, Antisense, DNA Primers, Research Article
Abstract

The role of ferritin in the modulation of the labile iron pool was examined by repressing the heavy subunit of ferritin in K562 cells transfected with an antisense construct. Repression of the heavy ferritin subunit evoked an increase in the chemical levels and pro-oxidant activity of the labile iron pool and, in turn, caused a reduced expression of transferrin receptors and increased expression of the light ferritin subunit.

Published
2001

117. Repression of ferritin expression increases the labile iron pool, oxidative stress, and short-term growth of human erythroleukemia cells

Author

Yosef Gruenbaum, Or Kakhlon, and Zvi Ioav Cabantchik

Subjects
biology, Cell growth, Protein subunit, Iron, Immunology, Transferrin receptor, Cell Biology, Hematology, Cell cycle, Protein oxidation, Biochemistry, Ferritin, Oxidative Stress, Ferritins, biology.protein, Humans, Leukemia, Erythroblastic, Acute, K562 Cells, Psychological repression, Cell Division, K562 cells
Abstract

The role of ferritin expression on the labile iron pool of cells and its implications for the control of cell proliferation were assessed. Antisense oligodeoxynucleotides were used as tools for modulating the expression of heavy and light ferritin subunits of K562 cells. mRNA and protein levels of each subunit were markedly reduced by 2-day treatment with antisense probes against the respective subunit. Although the combined action of antisense probes against both subunits reduced their protein expression, antisense repression of one subunit led to an increased protein expression of the other. Antisense treatment led to a rise in the steady-state labile iron pool, a rise in the production of reactive oxygen species after pro-oxidative challenges and in protein oxidation, and the down-regulation of transferrin receptors. When compared to the repression of individual subunits, co-repression of each subunit evoked a more than additive increase in the labile iron pool and the extent of protein oxidation. These treatments had no detectable effects on the long-term growth of cells. However, repression of ferritin synthesis facilitated the renewal of growth and the proliferation of cells pre-arrested at the G1/S phase. Renewed cell growth was significantly less dependent on external iron supply when ferritin synthesis was repressed and its degradation inhibited by lysosomal antiproteases. This study provides experimental evidence that links the effect of ferritin repression on growth stimulation to the expansion of the labile iron pool.

Published
2001

118. Searching for Efficient Therapeutic Avenues To Treat Adult Polyglucosan Body Disease (APBD) and Lafora Disease (LD) Using a High-Throughput Screening Platform (P03.053)

Author

Kakhlon, Or, primary, Glickstein, Hava, additional, Feinstein, Naomi, additional, Akman, Hasan, additional, DiMauro, Salvatore, additional, Minassian, Berge, additional, Michaeli, Amit, additional, Rayan, Anwar, additional, Grossman, Tamar, additional, Solmesky, Leonardo, additional, Weil, Miguel, additional, Kozakov, Dima, additional, and Lossos, Alexander, additional

Published
2013
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123. The labile iron pool: characterization, measurement, and participation in cellular processes1 <FN ID="FN1"><NO>1</NO>This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.</FN>

Author

Kakhlon, Or and Cabantchik, Z. Ioav

Subjects
*IRON metabolism, *CELL death
Abstract

The cellular labile iron pool (LIP) is a pool of chelatable and redox-active iron, which is transitory and serves as a crossroad of cell iron metabolism. Various attempts have been made to analyze the levels of LIP following cell disruption. The chemical identity of this pool has remained poorly characterized due to the multiplicity of iron ligands present in cells. However, the levels of LIP recently have been assessed with novel nondisruptive techniques that rely on the application of fluorescent metalosensors. Methodologically, a fluorescent chelator loaded into living cells binds to components of the LIP and undergoes stoichiometric fluorescence quenching. The latter is revealed and quantified in situ by addition of strong permeating iron chelators. Depending on the intracellular distribution of the sensing and chelating probes, LIP can be differentially traced in subcellular structures, allowing the dynamic assessment of its levels and roles in specific cell compartments. The labile nature of LIP was also revealed by its capacity to promote formation of reactive oxygen species (ROS), whether from endogenous or exogenous redox-active sources. LIP and ROS levels were shown to follow similar “rise and fall” patterns as a result of changes in iron import vs. iron chelation or ferritin (FT) degradation vs. ferritin synthesis. Those patterns conform with the accepted role of LIP as a self-regulatory pool that is sensed by cytosolic iron regulatory proteins (IRPs) and feedback regulated by IRP-dependent expression of iron import and storage machineries. However, LIP can also be modulated by biochemical mechanisms that override the IRP regulatory loops and, thereby, contribute to basic cellular functions. This review deals with novel methodologies for assessing cellular LIP and with recent studies in which changes in LIP and ROS levels played a determining role in cellular processes. [Copyright &y& Elsevier]

Published
2002
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124. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Author

Klionsky, Daniel J, Abdelmohsen, Kotb, Abe, Akihisa, Abedin, Md Joynal, Abeliovich, Hagai, Arozena, Abraham Acevedo, Adachi, Hiroaki, Adams, Christopher M, Adams, Peter D, Adeli, Khosrow, Adhihetty, Peter J, Adler, Sharon G, Agam, Galila, Agarwal, Rajesh, Aghi, Manish K, Agnello, Maria, Agostinis, Patrizia, Aguilar, Patricia V, Aguirre-Ghiso, Julio, Airoldi, Edoardo M, Ait-Si-Ali, Slimane, Akematsu, Takahiko, Akporiaye, Emmanuel T, Al-Rubeai, Mohamed, Albaiceta, Guillermo M, Albanese, Chris, Albani, Diego, Albert, Matthew L, Aldudo, Jesus, Alguel, Hana, Alirezaei, Mehrdad, Alloza, Iraide, Almasan, Alexandru, Almonte-Beceril, Maylin, Alnemri, Emad S, Alonso, Covadonga, Altan-Bonnet, Nihal, Altieri, Dario C, Alvarez, Silvia, Alvarez-Erviti, Lydia, Alves, Sandro, Amadoro, Giuseppina, Amano, Atsuo, Amantini, Consuelo, Ambrosio, Santiago, Amelio, Ivano, Amer, Amal O, Amessou, Mohamed, Amon, Angelika, An, Zhenyi, Anania, Frank A, Andersen, Stig U, Andley, Usha P, Andreadi, Catherine K, Andrieu-Abadie, Nathalie, Anel, Alberto, Ann, David K, Anoopkumar-Dukie, Shailendra, Antonioli, Manuela, Aoki, Hiroshi, Apostolova, Nadezda, Aquila, Saveria, Aquilano, Katia, Araki, Koichi, Arama, Eli, Aranda, Agustin, Araya, Jun, Arcaro, Alexandre, Arias, Esperanza, Arimoto, Hirokazu, Ariosa, Aileen R, Armstrong, Jane L, Arnould, Thierry, Arsov, Ivica, Asanuma, Katsuhiko, Askanas, Valerie, Asselin, Eric, Atarashi, Ryuichiro, Atherton, Sally S, Atkin, Julie D, Attardi, Laura D, Auberger, Patrick, Auburger, Georg, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Avantaggiati, Maria Laura, Avrahami, Limor, Awale, Suresh, Azad, Neelam, Bachetti, Tiziana, Backer, Jonathan M, Bae, Dong-Hun, Bae, Jae-Sung, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric H, Baek, Seung-Hoon, Baghdiguian, Stephen, Bagniewska-Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xue-Yuan, Bailly, Yannick, Balaji, Kithiganahalli Narayanaswamy, Balduini, Walter, Ballabio, Andrea, Balzan, Rena, Banerjee, Rajkumar, Banhegyi, Gabor, Bao, Haijun, Barbeau, Benoit, Barrachina, Maria D, Barreiro, Esther, Bartel, Bonnie, Bartolome, Alberto, Bassham, Diane C, Bassi, Maria Teresa, Bast, Robert C, Basu, Alakananda, Batista, Maria Teresa, Batoko, Henri, Battino, Maurizio, Bauckman, Kyle, Baumgarner, Bradley L, Bayer, Ulrich K, Beale, Rupert, Beaulieu, Jean-Francois, Beck, George R, Becker, Christoph, Beckham, David J, Bedard, Pierre-Andre, Bednarski, Patrick J, Begley, Thomas J, Behl, Christian, Behrends, Christian, Behrens, Georg MN, Behrns, Kevin E, Bejarano, Eloy, Belaid, Amine, Belleudi, Francesca, Benard, Giovanni, Berchem, Guy, Bergamaschi, Daniele, Bergami, Matteo, Berkhout, Ben, Berliocchi, Laura, Bernard, Amelie, Bernard, Monique, Bernassola, Francesca, Bertolotti, Anne, Bess, Amanda S, Besteiro, Sebastien, Bettuzzi, Saverio, Bhalla, Savita, Bhattacharyya, Shalmoli, Bhutia, Sujit K, Biagosch, Caroline, Bianchi, Michele Wolfe, Biard-Piechaczyk, Martine, Billes, Viktor, Bincoletto, Claudia, Bingol, Baris, Bird, Sara W, Bitoun, Marc, Bjedov, Ivana, Blackstone, Craig, Blanc, Lionel, Blanco, Guillermo A, Blomhoff, Heidi Kiil, Boada-Romero, Emilio, Boeckler, Stefan, Boes, Marianne, Boesze-Battaglia, Kathleen, Boise, Lawrence H, Bolino, Alessandra, Boman, Andrea, Bonaldo, Paolo, Bordi, Matteo, Bosch, Jurgen, Botana, Luis M, Botti, Joelle, Bou, German, Bouche, Marina, Bouchecareilh, Marion, Boucher, Marie-Josee, Boulton, Michael E, Bouret, Sebastien G, Boya, Patricia, Boyer-Guittaut, Michaeel, Bozhkov, Peter V, Brady, Nathan, Braga, Vania MM, Brancolini, Claudio, Braus, Gerhard H, Bravo-San Pedro, Jose M, Brennan, Lisa A, Bresnick, Emery H, Brest, Patrick, Bridges, Dave, Bringer, Marie-Agnes, Brini, Marisa, Brito, Glauber C, Brodin, Bertha, Brookes, Paul S, Brown, Eric J, Brown, Karen, Broxmeyer, Hal E, Bruhat, Alain, Brum, Patricia Chakur, Brumell, John H, Brunetti-Pierri, Nicola, Bryson-Richardson, Robert J, Buch, Shilpa, Buchan, Alastair M, Budak, Hikmet, Bulavin, Dmitry V, Bultman, 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125. The Implications for Cells of the Lipid Switches Driven by Protein–Membrane Interactions and the Development of Membrane Lipid Therapy

Author

Pablo V. Escribá, Victoria Lladó, Or Kakhlon, Manuel Torres, Catalina Ana Rosselló, and Paula Fernández-García

Subjects
Cell signaling, Membrane lipids, protein–membrane interactions, Cell, Lipid Bilayers, Review, Models, Biological, Catalysis, Biophysical Phenomena, Inorganic Chemistry, Cell membrane, lcsh:Chemistry, 03 medical and health sciences, Membrane Lipids, 0302 clinical medicine, melitherapy, peripheral amphitropic non-permanently bound membrane proteins, medicine, Animals, Humans, Disease, Physical and Theoretical Chemistry, Lipid bilayer, Molecular Biology, lcsh:QH301-705.5, Spectroscopy, 030304 developmental biology, 0303 health sciences, Chemistry, Organic Chemistry, Peripheral membrane protein, Cell Membrane, Membrane Proteins, General Medicine, membrane lipid switch, Computer Science Applications, Cell biology, lipid bilayer, Protein Transport, medicine.anatomical_structure, Membrane, Membrane protein, lcsh:Biology (General), lcsh:QD1-999, 030217 neurology & neurosurgery, Protein Binding, Signal Transduction
Abstract

The cell membrane contains a variety of receptors that interact with signaling molecules. However, agonist–receptor interactions not always activate a signaling cascade. Amphitropic membrane proteins are required for signal propagation upon ligand-induced receptor activation. These proteins localize to the plasma membrane or internal compartments; however, they are only activated by ligand-receptor complexes when both come into physical contact in membranes. These interactions enable signal propagation. Thus, signals may not propagate into the cell if peripheral proteins do not co-localize with receptors even in the presence of messengers. As the translocation of an amphitropic protein greatly depends on the membrane’s lipid composition, regulation of the lipid bilayer emerges as a novel therapeutic strategy. Some of the signals controlled by proteins non-permanently bound to membranes produce dramatic changes in the cell’s physiology. Indeed, changes in membrane lipids induce translocation of dozens of peripheral signaling proteins from or to the plasma membrane, which controls how cells behave. We called these changes “lipid switches”, as they alter the cell’s status (e.g., proliferation, differentiation, death, etc.) in response to the modulation of membrane lipids. Indeed, this discovery enables therapeutic interventions that modify the bilayer’s lipids, an approach known as membrane-lipid therapy (MLT) or melitherapy.

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