Výsledky vyhledávání - "Francisco J. Campoy"

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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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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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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The level of butyrylcholinesterase activity increases and the content of the mRNA remains unaffected in brain of senescence-accelerated mouse SAMP8

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

Publikováno v: Chemico-Biological Interactions. 175:332-335

Looking at cholinesterases (ChEs) changes in age-related mental impairment, the expression of ChEs in brain of senescence accelerated-resistant (SAMR1) and senescence accelerated-prone (SAMP8) mice was studied. Acetylcholinesterase (AChE) activity wa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::738b1510a6f59669f4abccb8e7f185e6
https://doi.org/10.1016/j.cbi.2008.05.010

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The level of aryl acylamidase activity displayed by human butyrylcholinesterase depends on its molecular distribution

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

Publikováno v: Chemico-Biological Interactions. 175:336-339

Butyrylcholinesterase (BuChE) and acetylcholinesterase (AChE) display both esterase and aryl acylamidase (AAA) activities. Their AAA activity can be measured using o-nitroacetanilide (ONA). In human samples depleted of acetylcholinesterase, we notice

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edfbfe808d29f49268233d414cb26835
https://doi.org/10.1016/j.cbi.2008.03.007

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The increased ecto-5′-nucleotidase activity in muscle, heart and liver of laminin α2-deficient mice is not caused by an elevation in the mRNA content

Autor: Luis F. Sánchez del Campo, Encarnación Muñoz-Delgado, Francisco J. Campoy, Julio C. Morote-García, Cecilio J. Vidal

Publikováno v: The International Journal of Biochemistry & Cell Biology. 38:1092-1101

We have previously shown that mouse muscle and liver contain catalytically active and inactive ecto-5′-nucleotidase (eNT) variants and that eNT activity in these tissues increases in laminin α2 (merosin)-deficient Lama2dy mice. These results promp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::385016d97a754979e98f7d9cd2a9b3cd
https://doi.org/10.1016/j.biocel.2005.11.002

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Acetyl- and Butyrylcholinesterase Activities Decrease in Human Colon Adenocarcinoma

Autor: Encarnación Muñoz-Delgado, María F. Montenegro, Juan Cabezas-Herrera, Francisco J. Campoy, Francisco Ruiz-Espejo, Cecilio J. Vidal, María Páez de la Cadena

Publikováno v: Journal of Molecular Neuroscience. 30:51-54

Apart from the hydrolysis of acetylcholine (ACh), acetyl- (AChE) and butyrylcholinesterase (BChE), through noncatalytic mechanisms, intervene in hematopoiesis, morphogenesis, and neurogenesis (Layer and Willbold, 1995; Soreq and Seidman, 2001). Choli

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63525877b494743e3e8a41159d5e8662
https://doi.org/10.1385/jmn:30:1:51

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