Isolation and characterization of porcine endothelin-like peptide.
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-Arg93. Further studies on the structure and function of new endogenous peptides possessing an endothelin-like sequence are ongoing in our laboratory.
Nakagawa
O
O
Department of Medicine, Kyoto University School of Medicine, Japan.
Nakao
K
K
Saito
Y
Y
Shirakami
G
G
Jougasaki
M
M
Mukoyama
M
M
Hosoda
K
K
Suga
S
S
Ogawa
Y
Y
Kishimoto
I
I
D000595:Amino Acid Sequence; D000818:Animals; D001013:Aorta, Thoracic / Q000378:metabolism; D002478:Cells, Cultured; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D019332:Endothelin-1; D016232:Endothelins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011498:Protein Precursors / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D011863:Radioimmunoassay; D013552:Swine
D019332:Endothelin-1; D016232:Endothelins; D011498:Protein Precursors