cDNA cloning and sequence analysis of Xenopus laevis preproendothelin-1.
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.
Quan
Jiexia
J
Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Japan.
Uchide
Tsuyoshi
T
Takizawa
Satoshi
S
Adur
Javier
J
Nara
Ei-ichi
E
Saida
Kaname
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D019332:Endothelin-1 / Q000737:chemistry / Q000235:genetics*; D006801:Humans; D007422:Intestines / Q000737:chemistry*; D051379:Mice; D008969:Molecular Sequence Data; D011817:Rabbits; D051381:Rats; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D029867:Xenopus Proteins / Q000737:chemistry / Q000235:genetics*; D014982:Xenopus laevis
D019332:Endothelin-1; D029867:Xenopus Proteins