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Provedor de dados:  Anais da ABC (AABC)
País:  Brazil
Título:  Choline acetyltransferase detection in normal and denervated electrocyte from Electrophorus electricus (L.) using a Confocal Scanning Optical Microscopy Analysis
Autores:  NUNES-TAVARES,NILSON
CUNHA-E-SILVA,NARCISA LEAL
HASSÓN-VOLOCH,AÍDA
Data:  2000-09-01
Ano:  2000
Palavras-chave:  Choline acetyltransferase
Electrocyte
Denervation
Immunohistochemistry
Resumo:  Acetylcholine is the neurotransmitter responsible for the transmission of impulses from cholinergic neurons to cells of innervated tissues. Its biosynthesis is catalyzed by the enzyme Choline acetyltransferase that is considered to be a phenotypically specific marker for cholinergic system. It is well known that the regulation of Choline acetyltransferase activity under physiological and pathological conditions is important for development and neuronal activities of cholinergic functions. We observed the distribution of Choline acetyltransferase in sections from the normal and denervated main electric organ sections of Electrophorus electricus (L.) by immunofluorescence using a anti-Choline acetyltransferase antibody. The animals were submitted to a surgical procedure to remove about 20 nerves and after 30 and 60 days, they were sacrificed. After 30 days, the results from immunohistochemistry demonstrated an increase on the Choline acetyltransferase distribution at denervated tissue sections when compared with the sections from the normal contralateral organ. A very similar labeling was observed between normal and denervated tissue sections of the animals after 60 days. However, Choline acetyltransferase activity (nmolesACh/ min/ mg of protein) in extracts obtained from electrocyte microsomal preparation, estimated by Fonnun's method (Fonnun 1975), was 70% lower in the denervated extracts.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652000000300007
Editor:  Academia Brasileira de Ciências
Relação:  10.1590/S0001-37652000000300007
Formato:  text/html
Fonte:  Anais da Academia Brasileira de Ciências v.72 n.3 2000
Direitos:  info:eu-repo/semantics/openAccess
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