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Book ; Conference proceedings: Sphingolipids as signaling modulators in the nervous system

Ledeen, Robert W.

[papers presented at the 1997 satellite symposium to the combined meeting of the international and American societies for neurochemistry, in New York, on July 13 - 16, 1997]

(Annals of the New York Academy of Sciences ; 845)

1998

Event/congress	Meeting on Sphingolipids as Signaling Modulators in the Nervous System (1997, NewYorkNY)
Author's details	[Meeting on Sphingolipids as Signaling Modulators in the Nervous System]
Series title	Annals of the New York Academy of Sciences ; 845
Collection
Keywords	Sphingolipids / congresses ; Signal Transduction / congresses ; Nervous System / congresses ; Sphingolipide ; Nervensystem
Subject	Systema nervosum ; NS
Language	English
Size	XII, 435 S. : Ill., graph. Darst.
Publishing place	New York, NY
Publishing country	United States
Document type	Book ; Conference proceedings
HBZ-ID	HT009001825
ISBN	1-57331-137-5 ; 1-57331-138-3 ; 978-1-57331-137-3 ; 978-1-57331-138-0
Database	Catalogue ZB MED Medicine, Health

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Se 110 -845-	verfügbar in Königswinter	Königswinter

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Article ; Online: Gangliosides, α-Synuclein, and Parkinson's Disease.

Ledeen, Robert W / Wu, Gusheng

Progress in molecular biology and translational science

2018 Volume 156, Page(s) 435–454

Abstract: This review addresses the role of α-synuclein (αSyn) in the etiopathology of Parkinson's disease (PD), with emphasis on its interaction with GM1 ganglioside. We begin with a brief review of some of the milestone discoveries that helped to elucidate PD ... ...

Abstract	This review addresses the role of α-synuclein (αSyn) in the etiopathology of Parkinson's disease (PD), with emphasis on its interaction with GM1 ganglioside. We begin with a brief review of some of the milestone discoveries that helped to elucidate PD neuropathology, including the fibrous inclusions of Lewy that characterize the degenerating dopaminergic neurons of the substantia nigra and the presence of αSyn as a major constituent of these Lewy bodies and neurites. This enabled Braak et al. to define the progressive nature of PD in developing their staging hypothesis which described the topographically predictable sequence of neuropathological changes giving rise to prodromal nonmotor symptoms that precede the classical motor dysfunctions. We recount recent studies demonstrating strong, specific binding of αSyn to GM1 that serves to inhibit fibril formation and the key role of N-acetylation of αSyn in enhancing GM1 binding and specificity. The consequences of insufficient GM1 are illustrated in a newly presented mouse model of PD based on partial deletion of this ganglioside due to heterologous disruption of B4galnt1 (GM2/GD2 synthase), such mice presenting accurate recapitulation of the PD phenotype. A key feature of these mice was marked elevation of αSyn aggregates which accompanied motor impairment, both aggregates and motor dysfunction being corrected by GM1 replacement therapy. Such therapy was achieved with high dosage of GM1 and more effectively with lower doses of LIGA20, a membrane permeable analog of GM1. The accuracy of this mouse model was emphasized by the finding that various central nervous system and noncentral nervous system tissues from PD patients manifested similar GM1 deficiency as the B4galnt1
MeSH term(s)	Animals ; Gangliosides/metabolism ; Humans ; Parkinson Disease/physiopathology ; alpha-Synuclein/metabolism
Chemical Substances	Gangliosides ; alpha-Synuclein
Language	English
Publishing date	2018-02-24
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2471995-X
ISSN	1878-0814 ; 0079-6603 ; 1877-1173
ISSN (online)	1878-0814
ISSN	0079-6603 ; 1877-1173
DOI	10.1016/bs.pmbts.2017.12.009
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Book: New trends in ganglioside research

Ledeen, Robert W.

neurochemic. and neuroregenerative aspects ; [... took place on June 9 - 12, 1987, in Puerto La Cruz, Venezuela, organized as a satellite to the eleventh meeting of the International Society for Neurochemistry]

(FIDIA research series ; 14)

1988

Author's details	ed. by R. W. Ledeen
Series title	FIDIA research series ; 14
Collection
Keywords	Gangliosides ; Ganglioside ; Neurochemie ; Nervensystem ; Krankheit ; Regeneration
Subject	Restitution ; Erkrankung ; Krankheitszustand ; Krankheiten ; Morbus ; Nosos ; Pathos ; Systema nervosum ; NS ; Biochemie ; Neurobiochemie
Size	XIV, 660 S. : Ill., graph. Darst.
Publisher	Liviana Pr. u.a.
Publishing place	Padova
Publishing country	Italy
Document type	Book
HBZ-ID	HT003248786
ISBN	3-540-96797-4 ; 0-387-96797-4 ; 88-7675-530-6 ; 978-3-540-96797-2 ; 978-0-387-96797-4 ; 978-88-7675-530-9
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1989 A 653	order for loan	Magazin

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Article: The multi-tasked life of GM1 ganglioside, a true factotum of nature.

Ledeen, Robert W / Wu, Gusheng

Trends in biochemical sciences

2015 Volume 40, Issue 7, Page(s) 407–418

Abstract: GM1 ganglioside occurs widely in vertebrate tissues, where it exhibits many essential functions, both in the plasma membrane and intracellular loci. Its essentiality is revealed in the dire consequences resulting from genetic deletion. This derives from ... ...

Abstract	GM1 ganglioside occurs widely in vertebrate tissues, where it exhibits many essential functions, both in the plasma membrane and intracellular loci. Its essentiality is revealed in the dire consequences resulting from genetic deletion. This derives from its key roles in several signalosome systems, characteristically located in membrane rafts, where it associates with specific proteins that have glycolipid-binding domains. Thus, GM1 interacts with proteins that modulate mechanisms such as ion transport, neuronal differentiation, G protein-coupled receptors (GPCRs), immune system reactivities, and neuroprotective signaling. The latter occurs through intimate association with neurotrophin receptors, which has relevance to the etiopathogenesis of neurodegenerative diseases and potential therapies. Here, we review the current state of knowledge of these GM1-associated mechanisms.
MeSH term(s)	Animals ; Biological Transport ; Calcium/metabolism ; Cell Differentiation ; Cell Membrane ; G(M1) Ganglioside/physiology ; Glycoproteins/metabolism ; Humans ; Nerve Tissue Proteins/metabolism ; Protein Processing, Post-Translational ; Synaptic Transmission
Chemical Substances	Glycoproteins ; Nerve Tissue Proteins ; G(M1) Ganglioside (37758-47-7) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2015-07
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	194216-5
ISSN	1362-4326 ; 0968-0004 ; 0376-5067
ISSN (online)	1362-4326
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2015.04.005
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Article: The multi-tasked life of GM1 ganglioside, a true factotum of nature

Ledeen, Robert W / Gusheng Wu

Trends in biochemical sciences. 2015 July, v. 40

2015

Abstract	GM1 ganglioside occurs widely in vertebrate tissues, where it exhibits many essential functions, both in the plasma membrane and intracellular loci. Its essentiality is revealed in the dire consequences resulting from genetic deletion. This derives from its key roles in several signalosome systems, characteristically located in membrane rafts, where it associates with specific proteins that have glycolipid-binding domains. Thus, GM1 interacts with proteins that modulate mechanisms such as ion transport, neuronal differentiation, G protein-coupled receptors (GPCRs), immune system reactivities, and neuroprotective signaling. The latter occurs through intimate association with neurotrophin receptors, which has relevance to the etiopathogenesis of neurodegenerative diseases and potential therapies. Here, we review the current state of knowledge of these GM1-associated mechanisms.
Keywords	G-protein coupled receptors ; gangliosides ; immune system ; loci ; neurodegenerative diseases ; neurons ; plasma membrane ; tissues ; vertebrates
Language	English
Dates of publication	2015-07
Size	p. 407-418.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	194220-7
ISSN	0968-0004 ; 0376-5067
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2015.04.005
Database	NAL-Catalogue (AGRICOLA)

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Book ; Conference proceedings: Ganglioside structure, function, and biomedical potential

Ledeen, Robert W.

[proceedings of the Symposium on Ganglioside Structure, Function, and Biomedical Potential, held July 6 - 10, 1983, at Parksville, Vancouver Island, British Columbia, Canada ...]

(Advances in experimental medicine and biology; 174 ; 174)

1984

Event/congress	Symposium on Ganglioside Structure, Function, and Biomedical Potential (1983, ParksvilleBritishColumbia)
Author's details	ed. by Robert W. Ledeen
Series title	Advances in experimental medicine and biology; 174 ; 174 Advances in experimental medicine and biology Advances in experimental medicine and biology; 174
Collection	Advances in experimental medicine and biology Advances in experimental medicine and biology; 174
Keywords	GANGLIOSIDES / CONGRESSES ; GANGLIOSIDES / THERAPEUTIC USE / CONGRESSES ; PERIPHERAL NERVOUS SYSTEM DISEASES / DRUG THERAPY / CONGRESSES ; Ganglioside
Size	XII, 649 S. : Ill., graph. Darst.
Publisher	Plenum Pr
Publishing place	New York u.a.
Publishing country	United States
Document type	Book ; Conference proceedings
HBZ-ID	HT002483587
ISBN	0-306-41707-3 ; 978-0-306-41707-8
Database	Catalogue ZB MED Medicine, Health

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1984 A 3716	order for loan	Magazin

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Article ; Online: Glycan Chains of Gangliosides: Functional Ligands for Tissue Lectins (Siglecs/Galectins).

Ledeen, Robert W / Kopitz, Jürgen / Abad-Rodríguez, José / Gabius, Hans-Joachim

Progress in molecular biology and translational science

2018 Volume 156, Page(s) 289–324

Abstract: Molecular signals on the cell surface are responsible for adhesion and communication. Of relevance in this respect, their chemical properties endow carbohydrates with the capacity to store a maximum of information in a minimum of space. One way to ... ...

Abstract	Molecular signals on the cell surface are responsible for adhesion and communication. Of relevance in this respect, their chemical properties endow carbohydrates with the capacity to store a maximum of information in a minimum of space. One way to present glycans on the cell surface is their covalent conjugation to a ceramide anchor. Among the resulting glycosphingolipids, gangliosides are special due to the presence of at least one sialic acid in the glycan chains. Their spatial accessibility and the dynamic regulation of their profile are factors that argue in favor of a role of glycans of gangliosides as ligands (counterreceptors) for carbohydrate-binding proteins (lectins). Indeed, as discovered first for a bacterial toxin, tissue lectins bind gangliosides and mediate contact formation (trans) and signaling (cis). While siglecs have a preference for higher sialylated glycans, certain galectins also target the monosialylated pentasaccharide of ganglioside GM1. Enzymatic interconversion of ganglioside glycans by sialidase action, relevant for neuroblastoma cell differentiation and growth control in vitro, for axonogenesis and axon regeneration, as well as for proper communication between effector and regulatory T cells, changes lectin-binding affinity profoundly. The GD1a-to-GM1 "editing" is recognized by such lectins, for example, myelin-associated glycoprotein (siglec-4) losing affinity and galectin-1 gaining reactivity, and then translated into postbinding signaling. Orchestrations of loss/gain of affinity, of ganglioside/lectin expression, and of lectin presence in a network offer ample opportunities for fine-tuning. Thus glycans of gangliosides such as GD1a and GM1 are functional counterreceptors by a pairing with tissue lectins, an emerging aspect of ganglioside and lectin functionality.
MeSH term(s)	Animals ; Galectins/chemistry ; Galectins/metabolism ; Gangliosides/chemistry ; Gangliosides/metabolism ; Humans ; Ligands ; Metabolic Diseases/physiopathology ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Sialic Acid Binding Immunoglobulin-like Lectins/chemistry ; Sialic Acid Binding Immunoglobulin-like Lectins/metabolism ; Signal Transduction
Chemical Substances	Galectins ; Gangliosides ; Ligands ; Polysaccharides ; Sialic Acid Binding Immunoglobulin-like Lectins
Language	English
Publishing date	2018-03-28
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2471995-X
ISSN	1878-0814 ; 0079-6603 ; 1877-1173
ISSN (online)	1878-0814
ISSN	0079-6603 ; 1877-1173
DOI	10.1016/bs.pmbts.2017.12.004
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Article ; Online: Mice deficient in GM1 manifest both motor and non-motor symptoms of Parkinson's disease; successful treatment with synthetic GM1 ganglioside.

Wu, Gusheng / Lu, Zi-Hua / Seo, Joon Ho / Alselehdar, Samar K / DeFrees, Shawn / Ledeen, Robert W

Experimental neurology

2020 Volume 329, Page(s) 113284

Abstract: Parkinson's disease (PD) is a major neurodegenerative disorder characterized by a variety of non-motor symptoms in addition to the well-recognized motor dysfunctions that have commanded primary interest. We previously described a new PD mouse model based ...

Abstract	Parkinson's disease (PD) is a major neurodegenerative disorder characterized by a variety of non-motor symptoms in addition to the well-recognized motor dysfunctions that have commanded primary interest. We previously described a new PD mouse model based on heterozygous disruption of the B4galnt1 gene leading to partial deficiency of the GM1 family of gangliosides that manifested several nigrostriatal neuropathological features of PD as well as movement impairment. We now show this mouse also suffers three non-motor symptoms characteristic of PD involving the gastrointestinal, sympathetic cardiac, and cerebral cognitive systems. Treatment of these animals with a synthetic form of GM1 ganglioside, produced by transfected E. coli, proved ameliorative of these symptoms as well as the motor defect. These findings further suggest subnormal GM1 to be a systemic defect constituting a major risk factor in sporadic PD and indicate the B4galnt1(+/-) (HT) mouse to be a true neuropathological model that recapitulates both motor and non-motor lesions of this condition.
MeSH term(s)	Animals ; Disease Models, Animal ; Female ; G(M1) Ganglioside/administration & dosage ; G(M1) Ganglioside/deficiency ; G(M1) Ganglioside/genetics ; Gastrointestinal Diseases/drug therapy ; Gastrointestinal Diseases/genetics ; Gastrointestinal Diseases/metabolism ; Male ; Memory Disorders/drug therapy ; Memory Disorders/genetics ; Memory Disorders/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mice, Transgenic ; Motor Skills Disorders/drug therapy ; Motor Skills Disorders/genetics ; Motor Skills Disorders/metabolism ; N-Acetylgalactosaminyltransferases/deficiency ; N-Acetylgalactosaminyltransferases/genetics ; Parkinson Disease/drug therapy ; Parkinson Disease/genetics ; Parkinson Disease/metabolism
Chemical Substances	G(M1) Ganglioside (37758-47-7) ; N-Acetylgalactosaminyltransferases (EC 2.4.1.-) ; beta-1,4-N-acetyl-galactosaminyl transferase 1, mouse (EC 2.4.1.165)
Language	English
Publishing date	2020-03-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	207148-4
ISSN	1090-2430 ; 0014-4886
ISSN (online)	1090-2430
ISSN	0014-4886
DOI	10.1016/j.expneurol.2020.113284
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Article: Glycobiology of ion transport in the nervous system.

Nowycky, Martha C / Wu, Gusheng / Ledeen, Robert W

Advances in neurobiology

2014 Volume 9, Page(s) 321–342

Abstract: The nervous system is richly endowed with large transmembrane proteins that mediate ion transport, including gated ion channels as well as energy-consuming pumps and transporters. Transport proteins undergo N-linked glycosylation which can affect ... ...

Abstract	The nervous system is richly endowed with large transmembrane proteins that mediate ion transport, including gated ion channels as well as energy-consuming pumps and transporters. Transport proteins undergo N-linked glycosylation which can affect expression, location, stability, and function. The N-linked glycans of ion channels are large, contributing between 5 and 50 % of their molecular weight. Many contain a high density of negatively charged sialic acid residues which modulate voltage-dependent gating of ion channels. Changes in the size and chemical composition of glycans are responsible for developmental and cell-specific variability in the biophysical and functional properties of many ion channels. Glycolipids, principally gangliosides, exert considerable influence on some forms of ion transport, either through direct association with ion transport proteins or indirectly through association with proteins that activate transport through appropriate signaling. Examples of both pumps and ion channels have been revealed which depend on ganglioside regulation. While some of these processes are localized in the plasma membrane, ganglioside-regulated ion transport can also occur at various loci within the cell including the nucleus. This chapter will describe ion channel and ion pump structures with a focus on the functional effects of glycosylation on ion channel availability and function, and effects of alterations in glycosylation on nervous system function. It will also summarize highlights of the research on glycolipid/ganglioside-mediated regulation of ion transport.
Language	English
Publishing date	2014
Publishing country	United States
Document type	Journal Article
ISSN	2190-5215
ISSN	2190-5215
DOI	10.1007/978-1-4939-1154-7_15
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Article ; Online: In search of a solution to the sphinx-like riddle of GM1.

Ledeen, Robert W / Wu, Gusheng

Neurochemical research

2010 Volume 35, Issue 12, Page(s) 1867–1874

Abstract: Among the many glycoconjugates contributing to the sugar code, gangliosides have drawn special attention owing to their predominance as the major sialoglycoconjugate category within the nervous system. However, their occurrence, albeit at lower levels, ... ...

Abstract	Among the many glycoconjugates contributing to the sugar code, gangliosides have drawn special attention owing to their predominance as the major sialoglycoconjugate category within the nervous system. However, their occurrence, albeit at lower levels, appears ubiquitous in vertebrate cells and even some invertebrate tissues. Now that over 100 gangliosides have been structurally characterized, their diverse physiological functions constitute a remaining enigma. This has been especially true of GM1, for which a surprising array of functions has already been revealed. Our current research has focused on two areas of GM1 function: (a) signaling induced in neural and immune cells by cross-linking of GM1 in the plasma membrane that leads to activation of TRPC5 (transient receptor potiential, canonical form 5) channels, a process important in neuritogenesis and autoimmune suppression; (b) activation by GM1 of a sodium-calcium exchanger (NCX) in the inner membrane of the nuclear envelope (NE) with resulting modulation of nuclear and cellular calcium. The latter has a role in maintaining neuronal viability, loss of which renders neurons vulnerable to Ca(2+) overload. Pathological manifestations in mutant mice and their cultured neurons lacking GM1 have shown dramatic rescue with a membrane permeable derivative of GM1 that enters the nucleus and restores NCX activity. Nuclear function of GM1 is related to the presence of neuraminidase in the NE, an enzyme that generates GM1 through hydrolysis of GD1a. A different isoform of this enzyme was found in each of the two membranes of the NE.
MeSH term(s)	Animals ; Calcium/metabolism ; Carbohydrate Sequence ; Cell Nucleus/metabolism ; G(M1) Ganglioside/chemistry ; G(M1) Ganglioside/metabolism ; G(M1) Ganglioside/physiology ; Homeostasis ; Mice ; Molecular Sequence Data ; Neurons/cytology
Chemical Substances	G(M1) Ganglioside (37758-47-7) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2010-11-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	199335-5
ISSN	1573-6903 ; 0364-3190
ISSN (online)	1573-6903
ISSN	0364-3190
DOI	10.1007/s11064-010-0286-0
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