cDNA cloning and sequence analysis of Xenopus laevis preproendothelin-1.
J Cardiovasc Pharmacol
; 44 Suppl 1: S256-9, 2004 Nov.
Article
en En
| MEDLINE
| ID: mdl-15838294
ABSTRACT
Endothelin (ET)-like immunoreactivity has been observed not only in mammals, but also in amphibians. The biological actions of ET are similar in amphibians and mammals, and amphibian ET-related receptors have been cloned and characterized. The cDNA sequences of mature and precursor forms of ET-related peptides, however, have not been reported in any amphibian until now. To identify the ET-related peptides, we screened the Xenopus laevis intestine cDNA library using the rapid amplification of cDNA ends method and cloned cDNAs encoding preproendothelin-1. The deduced amino acid sequence of X. laevis preproendothelin-1 comprises 223 amino acids, including a putative signal sequence of 19 amino acids, a mature ET-1 of 21 amino acids, as well as big ET-1 and ET-1-like sequences. X. laevis ET-1 is identical to mammalian ET-1 as well as ET-1 peptide, recently purified from the stomach of the European green frog, Rana ridibunda. This is the first report describing the cDNA encoding preproendothelin-1 in an amphibian species.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Clonación Molecular
/
Análisis de Secuencia de ADN
/
Endotelina-1
/
Análisis de Secuencia de Proteína
/
Proteínas de Xenopus
/
Intestinos
Límite:
Animals
/
Humans
Idioma:
En
Revista:
J Cardiovasc Pharmacol
Año:
2004
Tipo del documento:
Article
País de afiliación:
Japón