TY - JOUR
T1 - Isolation and characterization of porcine endothelin-like peptide
AU - Nakagawa, Osamu
AU - Nakao, Kazuwa
AU - Saito, Yoshihiko
AU - Shirakami, Gotaro
AU - Jougasaki, Michihisa
AU - Mukoyama, Masashi
AU - Hosoda, Kiminori
AU - Suga, Shin ichi
AU - Ogawa, Yoshihiro
AU - Kishimoto, Ichiro
AU - Komatsu, Yasato
AU - Hama, Norio
AU - Imura, Hiroo
PY - 1991
Y1 - 1991
N2 - Two endogenous molecules possessing an endothelin-like sequence with an apparent molecular weight of 7 kDa were isolated from serum-free culture medium of porcine aortic endothelial cells, using a specific radioimmunoassay. N-terminal sequences of two molecules were identical to each other and were Ser-Leu-Lys-Asp-Leu-Phe-Pro-Ala-Lys-Ala-Ala-Asp-Arg-Arg-Asp-Arg-X-Gln-X-Ala-X-Gln-Lys-Asp, which corresponds to the sequence [94-117] of preproendothelin-1. This finding indicates that these two molecules may be closely related peptides such as the oxidized form or disulfide analogues and also suggests that the endogenous peptide possessing an endothelin-like sequence is generated by proteolytic cleavage at paired basic amino acids Arg92-Arg93Further studies on the structure and function of new endogenous peptides possessing an endothelin-like sequence are ongoing in our laboratory.
AB - Two endogenous molecules possessing an endothelin-like sequence with an apparent molecular weight of 7 kDa were isolated from serum-free culture medium of porcine aortic endothelial cells, using a specific radioimmunoassay. N-terminal sequences of two molecules were identical to each other and were Ser-Leu-Lys-Asp-Leu-Phe-Pro-Ala-Lys-Ala-Ala-Asp-Arg-Arg-Asp-Arg-X-Gln-X-Ala-X-Gln-Lys-Asp, which corresponds to the sequence [94-117] of preproendothelin-1. This finding indicates that these two molecules may be closely related peptides such as the oxidized form or disulfide analogues and also suggests that the endogenous peptide possessing an endothelin-like sequence is generated by proteolytic cleavage at paired basic amino acids Arg92-Arg93Further studies on the structure and function of new endogenous peptides possessing an endothelin-like sequence are ongoing in our laboratory.
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U2 - 10.1097/00005344-199100177-00005
DO - 10.1097/00005344-199100177-00005
M3 - Article
C2 - 1725307
AN - SCOPUS:0026327146
VL - 17
SP - S13-S16
JO - Journal of Cardiovascular Pharmacology
JF - Journal of Cardiovascular Pharmacology
SN - 0160-2446
ER -