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Article ; Online: Harnessing Light: Girl with a Pulse-ox Earring.

Eckman Basiri, Louisa E H / Fabiszak, Margaret M / Stone, Alexander B / Connor, Christopher W

2024

Language	English
Publishing date	2024-04-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	269-0
ISSN	1528-1175 ; 0003-3022
ISSN (online)	1528-1175
ISSN	0003-3022
DOI	10.1097/ALN.0000000000004981
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Article ; Online: The Effects of Iron in a Rodent Model of Alzheimer Disease.

Griffin, Ian J / Eckman, Christopher B

The Journal of nutrition

2019 Volume 149, Issue 12, Page(s) 2079–2080

MeSH term(s)	Animals ; Mice ; Alzheimer Disease ; Hippocampus ; Homeostasis ; Iron ; Iron, Dietary ; Mice, Transgenic ; Disease Models, Animal
Chemical Substances	Iron (E1UOL152H7) ; Iron, Dietary
Language	English
Publishing date	2019-07-10
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	218373-0
ISSN	1541-6100 ; 0022-3166
ISSN (online)	1541-6100
ISSN	0022-3166
DOI	10.1093/jn/nxz208
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Article ; Online: Prospective, randomized, clinical trial on the effects of laparoscopic insufflation pressures on portal pressures in dogs.

Parlier, Mark / Thomson, Christopher B / Rendahl, Aaron / Strelchik, Alena / Baldo, Caroline / Eckman, Sarah K / Krueger, Amy / Gordon-Evans, Wanda J

Veterinary surgery : VS

2024

Abstract: Objective: The adverse effects of intra-abdominal pressure from capnoperitoneum on cardiovascular and pulmonary systems have been well documented, but the effects on portal pressures in dogs with various insufflation pressures is poorly defined. The aim ...

Abstract	Objective: The adverse effects of intra-abdominal pressure from capnoperitoneum on cardiovascular and pulmonary systems have been well documented, but the effects on portal pressures in dogs with various insufflation pressures is poorly defined. The aim of the present study was to measure the effect of a range of insufflation pressures on the portal pressure, using direct pressure measurements in patients undergoing laparoscopy. Study design: Clinical randomized prospective study. Animals: Nine client-owned dogs undergoing routine laparoscopy. Methods: Two rounds of direct portal pressure assessments were performed, at insufflation pressures of 0, 6, 10, and 14 mmHg in a predetermined randomized sequence. The data were analyzed for effects of insufflation pressure, hemodynamic alterations, and round. A best-fit exponential model of the relationship between portal pressure and insufflation pressure was created. Results: Portal pressure increased by 38% at 6 mmHg, 95% at 10 mmHg, and 175% at 14 mmHg compared to baseline. Portal pressure increased at an average rate of 7.45% per mmHg of insufflation pressure. Effects of weight, weight/insufflation pressure interaction, and round of insufflation were not statistically significant. No systemic hemodynamic adverse events were observed. Conclusion: Portal pressure increased as insufflation pressure increased. There was no clinically significant difference in baseline portal pressure between rounds of insufflation. Clinical significance: This exponential model of portal pressure supports the use of the minimum insufflation pressure to allow visualization during laparoscopy. The return of portal pressure to baseline following desufflation supports the comparison of portal pressure measurements before and after laparoscopic shunt attenuation.
Language	English
Publishing date	2024-02-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	1491071-8
ISSN	1532-950X ; 0161-3499
ISSN (online)	1532-950X
ISSN	0161-3499
DOI	10.1111/vsu.14074
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Article ; Online: Major amyloid-β-degrading enzymes, endothelin-converting enzyme-2 and neprilysin, are expressed by distinct populations of GABAergic interneurons in hippocampus and neocortex.

Pacheco-Quinto, Javier / Eckman, Christopher B / Eckman, Elizabeth A

Neurobiology of aging

2016 Volume 48, Page(s) 83–92

Abstract: Impaired clearance of amyloid-β peptide (Aβ) has been postulated to significantly contribute to the amyloid accumulation typical of Alzheimer's disease. Among the enzymes known to degrade Aβ in vivo are endothelin-converting enzyme (ECE)-1, ECE-2, and ... ...

Abstract	Impaired clearance of amyloid-β peptide (Aβ) has been postulated to significantly contribute to the amyloid accumulation typical of Alzheimer's disease. Among the enzymes known to degrade Aβ in vivo are endothelin-converting enzyme (ECE)-1, ECE-2, and neprilysin (NEP), and evidence suggests that they regulate independent pools of Aβ that may be functionally significant. To better understand the differential regulation of Aβ concentration by its physiological degrading enzymes, we characterized the cell and region-specific expression pattern of ECE-1, ECE-2, and NEP by in situ hybridization and immunohistochemistry in brain areas relevant to Alzheimer's disease. In contrast to the broader distribution of ECE-1, ECE-2 and NEP were found enriched in GABAergic neurons. ECE-2 was majorly expressed by somatostatin-expressing interneurons and was active in isolated synaptosomes. NEP messenger RNA was found mainly in parvalbumin-expressing interneurons, with NEP protein localized to perisomatic parvalbuminergic synapses. The identification of somatostatinergic and parvalbuminergic synapses as hubs for Aβ degradation is consistent with the possibility that Aβ may have a physiological function related to the regulation of inhibitory signaling.
MeSH term(s)	Alzheimer Disease/etiology ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/physiology ; Animals ; Endothelin-Converting Enzymes/genetics ; Endothelin-Converting Enzymes/metabolism ; Endothelin-Converting Enzymes/physiology ; GABAergic Neurons/enzymology ; Gene Expression ; Hippocampus/cytology ; Hippocampus/enzymology ; Mice, Transgenic ; Neocortex/cytology ; Neocortex/enzymology ; Neprilysin/genetics ; Neprilysin/metabolism ; Neprilysin/physiology ; RNA, Messenger/metabolism ; Synapses/enzymology
Chemical Substances	Amyloid beta-Peptides ; RNA, Messenger ; Neprilysin (EC 3.4.24.11) ; Ece2 protein, mouse (EC 3.4.24.71) ; Endothelin-Converting Enzymes (EC 3.4.24.71)
Language	English
Publishing date	2016-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	604505-4
ISSN	1558-1497 ; 0197-4580
ISSN (online)	1558-1497
ISSN	0197-4580
DOI	10.1016/j.neurobiolaging.2016.08.011
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Article ; Online: Intracellular metalloprotease activity controls intraneuronal Aβ aggregation and limits secretion of Aβ via exosomes.

Pacheco-Quinto, Javier / Clausen, Dana / Pérez-González, Rocío / Peng, Hui / Meszaros, Austin / Eckman, Christopher B / Levy, Efrat / Eckman, Elizabeth A

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2018 Volume 33, Issue 3, Page(s) 3758–3771

Abstract: ... Quinto, J., Clausen, D., Pérez-González, R., Peng, H., Meszaros, A., Eckman, C. B., Levy, E., Eckman, E ...

Abstract	Accumulating evidence suggests that the abnormal aggregation of amyloid-β (Αβ) peptide in Alzheimer's disease (AD) begins intraneuronally, within vesicles of the endosomal-lysosomal pathway where Aβ is both generated and degraded. Metalloproteases, including endothelin-converting enzyme (ECE)-1 and -2, reside within these vesicles and normally limit the accumulation of intraneuronally produced Aβ. In this study, we determined whether disruption of Aβ catabolism could trigger Aβ aggregation within neurons and increase the amount of Aβ associated with exosomes, small extracellular vesicles derived from endosomal multivesicular bodies. Using cultured cell lines, primary neurons, and organotypic brain slices from an AD mouse model, we found that pharmacological inhibition of the ECE family of metalloproteases increased intracellular and extracellular Aβ levels and promoted the intracellular formation of Aβ oligomers, a process that did not require internalization of secreted Aβ. In vivo, the accumulation of intraneuronal Aβ aggregates was accompanied by increased levels of both extracellular and exosome-associated Aβ, including oligomeric species. Neuronal exosomes were found to contain both ECE-1 and -2 activities, suggesting that multivesicular bodies are intracellular sites of Aβ degradation by these enzymes. ECE dysfunction could lead to the accumulation of intraneuronal Aβ aggregates and their subsequent release into the extracellular space via exosomes.-Pacheco-Quinto, J., Clausen, D., Pérez-González, R., Peng, H., Meszaros, A., Eckman, C. B., Levy, E., Eckman, E. A. Intracellular metalloprotease activity controls intraneuronal Aβ aggregation and limits secretion of Aβ via exosomes.
MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Brain/metabolism ; Cell Line, Tumor ; Endosomes/metabolism ; Endothelin-Converting Enzymes/metabolism ; Exosomes/metabolism ; Extracellular Space/metabolism ; Female ; Humans ; Lysosomes/metabolism ; Male ; Metalloendopeptidases/metabolism ; Mice ; Multivesicular Bodies/metabolism ; Neurons/metabolism ; Protein Aggregation, Pathological/metabolism ; Proteolysis
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Metalloendopeptidases (EC 3.4.24.-) ; Endothelin-Converting Enzymes (EC 3.4.24.71)
Language	English
Publishing date	2018-11-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.201801319R
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Article: An update on the amyloid hypothesis.

Eckman, Christopher B / Eckman, Elizabeth A

Neurologic clinics

2007 Volume 25, Issue 3, Page(s) 669–82, vi

Abstract: Alzheimer's disease (AD) is a devastating neurodegenerative disease. To rationally develop novel therapeutic and/or preventative agents for AD, an understanding of the etiology and pathogenesis of this complex disease is necessary. This article examines ... ...

Abstract	Alzheimer's disease (AD) is a devastating neurodegenerative disease. To rationally develop novel therapeutic and/or preventative agents for AD, an understanding of the etiology and pathogenesis of this complex disease is necessary. This article examines the evidence for the amyloid hypothesis of AD pathogenesis and discusses how it relates to the neurological and neuropathological features of AD, the known genetic risk factors and causative mutations, and the heightened risk associated with advanced age.
MeSH term(s)	Aged ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/genetics ; Amyloidosis/genetics ; Amyloidosis/pathology ; Animals ; Humans
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2007-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1013148-6
ISSN	1557-9875 ; 0733-8619
ISSN (online)	1557-9875
ISSN	0733-8619
DOI	10.1016/j.ncl.2007.03.007
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Article ; Online: Endothelin-converting enzymes and related metalloproteases in Alzheimer's disease.

Pacheco-Quinto, Javier / Herdt, Aimee / Eckman, Christopher B / Eckman, Elizabeth A

Journal of Alzheimer's disease : JAD

2012 Volume 33 Suppl 1, Page(s) S101–10

Abstract: The efficient clearance of amyloid-β (Aβ) is essential to modulate levels of the peptide in the brain and to prevent it from accumulating in senile plaques, a hallmark of Alzheimer's disease (AD) pathology.We and others have shown that failure in Aβ ... ...

Abstract	The efficient clearance of amyloid-β (Aβ) is essential to modulate levels of the peptide in the brain and to prevent it from accumulating in senile plaques, a hallmark of Alzheimer's disease (AD) pathology.We and others have shown that failure in Aβ catabolism can produce elevations in Aβ concentration similar to those observed in familial forms of AD. Based on the available evidence, it remains plausible that in late-onset AD, disturbances in the activity of Aβ degrading enzymes could induce Aβ accumulation, and that this increase could result in AD pathology. The following review presents a historical perspective of the parallel discovery of three vasopeptidases (neprilysin and endothelin-converting enzymes-1 and -2) as important Aβ degrading enzymes. The recognition of the role of these vasopeptidases in Aβ degradation, beyond bringing to light a possible explanation of how cardiovascular risk factors may influence AD risk, highlights a possible risk of the use of inhibitors of these enzymes for other clinical indications such as hypertension. We will discuss in detail the experiments conducted to assess the impact of vasopeptidase deficiency (through pharmacological inhibition or genetic mutation) on Aβ accumulation, as well as the cooperative effect of multiple Aβ degrading enzymes to regulate the concentration of the peptide at multiple sites, both intracellular and extracellular, throughout the brain.
MeSH term(s)	Alzheimer Disease/enzymology ; Animals ; Aspartic Acid Endopeptidases/metabolism ; Brain/enzymology ; Endothelin-Converting Enzymes ; Humans ; Metalloendopeptidases/metabolism ; Metalloproteases/metabolism ; Mice ; Neprilysin/metabolism ; Peptidyl-Dipeptidase A/metabolism
Chemical Substances	Metalloproteases (EC 3.4.-) ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; Aspartic Acid Endopeptidases (EC 3.4.23.-) ; Metalloendopeptidases (EC 3.4.24.-) ; Neprilysin (EC 3.4.24.11) ; Endothelin-Converting Enzymes (EC 3.4.24.71)
Language	English
Publishing date	2012-08-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-2012-129043
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Article ; Online: Reductions in levels of the Alzheimer's amyloid beta peptide after oral administration of ginsenosides.

Chen, Feng / Eckman, Elizabeth A / Eckman, Christopher B

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2006 Volume 20, Issue 8, Page(s) 1269–1271

Abstract: For millennia, ginseng and some of its components have been used to treat a wide variety of medical conditions, including age-related memory impairment. Because of its purported effects and apparently low rate of side effects, ginseng remains one of the ... ...

Abstract	For millennia, ginseng and some of its components have been used to treat a wide variety of medical conditions, including age-related memory impairment. Because of its purported effects and apparently low rate of side effects, ginseng remains one of the top selling natural product remedies in the United States. Given its potential role for improving age-related memory impairments and its common use in China for the treatment of Alzheimer's disease-like symptoms, we analyzed the effects of commercially available preparations of ginseng on the accumulation of the Alzheimer's amyloid beta peptide (Abeta) in a cell-based model system. In this model system, ginseng treatment resulted in a significant reduction in the levels of Abeta in the conditioned medium. We next examined the effects of several compounds isolated from ginseng and found that certain ginsenosides lowered Abeta concentration in a dose-dependent manner with ginsenoside Rg3 having an approximate IC50 of under 25 microM against Abeta42. Furthermore, we found that three of these isolated components, ginsenoside Rg1, Rg3, and RE, resulted in significant reductions in the amount of Abeta detected in the brains of animals after single oral doses of these agents. The results indicate that ginseng itself, or purified ginsenosides, may have similarly useful effects in human disease.
MeSH term(s)	Administration, Oral ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Animals ; Brain/drug effects ; Brain/metabolism ; CHO Cells ; Cricetinae ; Cricetulus ; Female ; Ginsenosides/administration & dosage ; Ginsenosides/pharmacology ; Humans ; Mice ; Mice, Transgenic ; Panax/chemistry ; Peptide Fragments/metabolism ; Plant Extracts/administration & dosage ; Plant Extracts/pharmacology
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Ginsenosides ; Peptide Fragments ; Plant Extracts ; amyloid beta-protein (1-40) ; amyloid beta-protein (1-42) ; ginsenoside Rg3 (227D367Y57)
Language	English
Publishing date	2006-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.05-5530fje
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Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Molecular characterization of mutations that cause globoid cell leukodystrophy and pharmacological rescue using small molecule chemical chaperones.

Lee, Wing C / Kang, Dongcheul / Causevic, Ena / Herdt, Aimee R / Eckman, Elizabeth A / Eckman, Christopher B

The Journal of neuroscience : the official journal of the Society for Neuroscience

2010 Volume 30, Issue 16, Page(s) 5489–5497

Abstract: Globoid cell leukodystrophy (GLD) (Krabbe disease) is an autosomal recessive, degenerative, lysosomal storage disease caused by a severe loss of galactocerebrosidase (GALC) enzymatic activity. Of the >70 disease-causing mutations in the GALC gene, most ... ...

Abstract	Globoid cell leukodystrophy (GLD) (Krabbe disease) is an autosomal recessive, degenerative, lysosomal storage disease caused by a severe loss of galactocerebrosidase (GALC) enzymatic activity. Of the >70 disease-causing mutations in the GALC gene, most are located outside of the catalytic domain of the enzyme. To determine how GALC mutations impair enzymatic activity, we investigated the impact of multiple disease-causing mutations on GALC processing, localization, and enzymatic activity. Studies in mammalian cells revealed dramatic decreases in GALC activity and a lack of appropriate protein processing into an N-terminal GALC fragment for each of the mutants examined. Consistent with this, we observed significantly less GALC localized to the lysosome and impairment in either the secretion or reuptake of mutant GALC. Notably, the D528N mutation was found to induce hyperglycosylation and protein misfolding. Reversal of these conditions resulted in an increase in proper processing and GALC activity, suggesting that glycosylation may play a critical role in the disease process in patients with this mutation. Recent studies have shown that enzyme inhibitors can sometimes "chaperone" misfolded polypeptides to their appropriate target organelle, bypassing the normal cellular quality control machinery and resulting in enhanced activity. To determine whether this may also work for GLD, we examined the effect of alpha-lobeline, an inhibitor of GALC, on D528N mutant cells. After treatment, GALC activity was significantly increased. This study suggests that mutations in GALC can cause GLD by impairing protein processing and/or folding and that pharmacological chaperones may be potential therapeutic agents for patients carrying certain mutations.
MeSH term(s)	Animals ; COS Cells ; Chlorocebus aethiops ; Enzyme Activation/drug effects ; Enzyme Activation/genetics ; Enzyme Precursors/genetics ; Enzyme Precursors/metabolism ; Galactosylceramidase/antagonists & inhibitors ; Galactosylceramidase/genetics ; Galactosylceramidase/metabolism ; Humans ; Leukodystrophy, Globoid Cell/drug therapy ; Leukodystrophy, Globoid Cell/enzymology ; Leukodystrophy, Globoid Cell/genetics ; Molecular Chaperones/genetics ; Molecular Chaperones/pharmacology ; Molecular Chaperones/therapeutic use ; Mutagenesis, Site-Directed ; Protein Folding/drug effects ; Protein Processing, Post-Translational/drug effects ; Protein Processing, Post-Translational/genetics
Chemical Substances	Enzyme Precursors ; Molecular Chaperones ; Galactosylceramidase (EC 3.2.1.46)
Language	English
Publishing date	2010-04-21
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.6383-09.2010
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Article ; Online: Agonist-induced restoration of hippocampal neurogenesis and cognitive improvement in a model of cholinergic denervation.

Van Kampen, Jackalina M / Eckman, Christopher B

Neuropharmacology

2009 Volume 58, Issue 6, Page(s) 921–929

Abstract: Loss of basal forebrain cholinergic innervation of the hippocampus and severe neuronal loss within the hippocampal CA1 region are early hallmarks of Alzheimer's disease, and are strongly correlated with cognitive status. Various therapeutic approaches ... ...

Abstract	Loss of basal forebrain cholinergic innervation of the hippocampus and severe neuronal loss within the hippocampal CA1 region are early hallmarks of Alzheimer's disease, and are strongly correlated with cognitive status. Various therapeutic approaches involve attempts to enhance neurotransmission or to provide some level of neuroprotection for remaining cells. An alternative approach may involve the generation of new cells to replace those lost in AD. Indeed, a simple shift in the balance between cell generation and cell loss may slow disease progression and possibly even reverse existing cognitive deficits. One potential neurogenic regulator might be acetylcholine, itself, which has been shown to play a critical role in hippocampal development. Here, we report the effects of various cholinergic compounds on indices of hippocampal neurogenesis, demonstrating a significant induction following pharmacological activation of muscarinic M1 receptors, located on hippocampal progenitors in the adult brain. This is the first report that a small-molecule agonist may induce neurogenesis in the hippocampal CA1 region. Furthermore, such treatment reversed deficits in markers of neurogenesis and spatial working memory triggered by cholinergic denervation in a rodent model. This study suggests the use of small molecule, receptor agonists may represent a novel means to trigger the restoration of specific neuronal populations lost to a variety of neurodegenerative disorders, such as Parkinson's, Alzheimer's, Huntington's and Amyotrophic Lateral Sclerosis.
MeSH term(s)	Acetylcholine/metabolism ; Animals ; Brain Diseases/drug therapy ; Brain Diseases/physiopathology ; CA1 Region, Hippocampal/drug effects ; CA1 Region, Hippocampal/physiopathology ; Cell Proliferation/drug effects ; Choline O-Acetyltransferase/metabolism ; Cholinergic Agents/pharmacology ; Cognition/drug effects ; Disease Models, Animal ; Female ; Hippocampus/drug effects ; Hippocampus/physiopathology ; Maze Learning/drug effects ; Memory/drug effects ; Muscarinic Agonists/pharmacology ; Muscarinic Antagonists/pharmacology ; Neurogenesis/drug effects ; Rats ; Rats, Sprague-Dawley ; Receptor, Muscarinic M1/agonists ; Receptor, Muscarinic M1/antagonists & inhibitors ; Receptor, Muscarinic M1/metabolism ; Receptors, Muscarinic/metabolism ; Space Perception/drug effects
Chemical Substances	Cholinergic Agents ; Muscarinic Agonists ; Muscarinic Antagonists ; Receptor, Muscarinic M1 ; Receptors, Muscarinic ; Choline O-Acetyltransferase (EC 2.3.1.6) ; Acetylcholine (N9YNS0M02X)
Language	English
Publishing date	2009-12-22
Publishing country	England
Document type	Journal Article
ZDB-ID	218272-5
ISSN	1873-7064 ; 0028-3908
ISSN (online)	1873-7064
ISSN	0028-3908
DOI	10.1016/j.neuropharm.2009.12.005
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