Výsledky vyhledávání - "Cecilio J. Vidal"

Cholinergic system and cell proliferation

Autor: Encarnación Muñoz-Delgado, María F. Montenegro, Cecilio J. Vidal, Francisco J. Campoy, Susana Nieto-Cerón, Juan Cabezas-Herrera

Publikováno v: Chemico-Biological Interactions. 259:257-265

The cholinergic system, comprising acetylcholine, the proteins responsible for acetylcholine synthesis and release, acetylcholine receptors and cholinesterases, is expressed by most human cell types. Acetylcholine is a neurotransmitter, but also a lo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f76b7d789d43b78a722964f5f04955b
https://doi.org/10.1016/j.cbi.2016.04.014

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Lipid rafts of mouse liver contain nonextended and extended acetylcholinesterase variants along with M3 muscarinic receptors

Autor: Cecilio J. Vidal, F. Javier Campoy, María F. Montenegro, Encarnación Muñoz-Delgado, Juan Cabezas-Herrera

Publikováno v: The FASEB Journal. 31:544-555

The observation of acetylcholinesterase (AChE) type H (AChEH), which is the predominant AChE variant in visceral organs and immune cells, in lipid rafts of muscle supports functional reasons for the raft targeting of glypiated AChEH The search for th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::004d94ff9062c81386733dbd521520a7
https://doi.org/10.1096/fj.201600609r

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Unbalanced acetylcholinesterase activity in larynx squamous cell carcinoma

Autor: Cecilio J. Vidal, Juan Pablo Pelegrín-Hernández, Juan Cabezas-Herrera, Antonio Piñero Madrona, Ana Cristina Castillo-González, José Neptuno Rodríguez-López, Susana Nieto-Cerón, José Antonio Noguera, María Fuensanta López-Moreno, Diego Hellín-Meseguer

Publikováno v: International Immunopharmacology. 29:81-86

Previous reports have demonstrated that a non-neuronal cholinergic system is expressed aberrantly in airways. A proliferative effect is exerted directly by cholinergic agonists through the activation of nicotinic and muscarinic receptors. In cancer,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3df9093683896e7dd9e016a7e3d36ef
https://doi.org/10.1016/j.intimp.2015.05.011

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Acetylcholinesterase activity of electric eel is increased or decreased by selected monoterpenoids and phenylpropanoids in a concentration-dependent manner

Autor: Francisco J. Campoy, María Dolores López, Encarnación Muñoz-Delgado, M.J. Pascual-Villalobos, Cecilio J. Vidal

Publikováno v: Chemico-Biological Interactions. 229:36-43

The profitable insecticidal action of monoterpenoids prompted us to test their efficiency against stored-grain beetle species, via inhibition of acetylcholinesterase (AChE). For this, we first studied the ability of the monoterpenoids geraniol, linal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43865c36032733dfed830fcec1e9e1ac
https://doi.org/10.1016/j.cbi.2015.01.006

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Most Acetylcholinesterase Activity of Non-Nervous Tissues and Cells Arises from the AChE-H Transcript

Autor: Susana Nieto Cerón, Juan Cabezas-Herrera, María Fernanda Montenegro, Francisco Javier Campoy, Cecilio J. Vidal, Encarnación Muñoz-Delgado

Publikováno v: Journal of Molecular Neuroscience. 53:429-435

While the functional implications of AChE-T, PRiMA and ColQ have been firmly established, those of glypiated AChE remain uncertain. Insights into the physiological meaning of glycosylphosphatidylinositol (GPI)-linked AChE-H were gained by comparing n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fe362c38f631e42fb74e4a29a6d2e0b
https://doi.org/10.1007/s12031-013-0172-8

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Expression of cholinesterases in human kidney and its variation in renal cell carcinoma types

Autor: María F. Montenegro, Cecilio J. Vidal, Juan Cabezas-Herrera, Encarnación Muñoz-Delgado, Francisco J. Campoy, M.T. Moral-Naranjo, Gyula Kovacs

Publikováno v: FEBS Journal. 277:4519-4529

Despite the aberrant expression of cholinesterases in tumours, the question of their possible contribution to tumorigenesis remains unsolved. The identification in kidney of a cholinergic system has paved the way to functional studies, but details on

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::91ac2e494eba43d91aa339574d1079d3
https://doi.org/10.1111/j.1742-4658.2010.07861.x

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The levels of both lipid rafts and raft-located acetylcholinesterase dimers increase in muscle of mice with muscular dystrophy by merosin deficiency

Autor: Encarnación Muñoz-Delgado, Francisco J. Campoy, Cecilio J. Vidal, María F. Montenegro, M.T. Moral-Naranjo

Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1802:754-764

Wild type and dystrophic (merosin-deficient) Lama2dy mice muscles were compared for their density of lipid rafts. The 5-fold higher level of caveolin-3 and the 2-3 times higher level of ecto-5’-nucleotidase activity in raft preparations (Triton X-1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7c84f84f2433d26e16a9ddbfbda83e1
https://doi.org/10.1016/j.bbadis.2010.05.011

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Cholinesterase activity in brain of senescence-accelerated-resistant mouse SAMR1 and its variation in brain of senescence-accelerated-prone mouse SAMP8

Autor: Cecilio J. Vidal, Joaquín Jordán, María F. Montenegro, Encarnación Muñoz-Delgado, Francisco J. Campoy, F.J. Fernandez-Gomez

Publikováno v: Journal of Neuroscience Research. 88:155-166

The early-onset, irreversible, severe deficits of learning and memory in the senescence-accelerated mouse (SAM)-prone/8 (SAMP8) support its use as an animal model for human dementias of early onset. Possible implication of acetylcholinesterase (AChE)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7d48254fc59f8d020a2c909915d673e2
https://doi.org/10.1002/jnr.22177

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Hydrolysis of acetylthiocoline, o-nitroacetanilide and o-nitrotrifluoroacetanilide by fetal bovine serum acetylcholinesterase

Autor: Francisco J. Campoy, Cecilio J. Vidal, María F. Montenegro, Encarnación Muñoz-Delgado, M.T. Moral-Naranjo

Publikováno v: FEBS Journal. 276:2074-2083

Besides esterase activity, acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) hydrolyze o-nitroacetanilides through aryl acylamidase activity. We have reported that BuChE tetramers and monomers of human blood plasma differ in o-nitroacetan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c5b1fa3fbb90f4d45628c8aa93becfd7
https://doi.org/10.1111/j.1742-4658.2009.06942.x

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