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Presence of endothelin-1 in porcine spinal cord: Isolation and sequence determination

1989; Elsevier BV; Volume: 162; Issue: 1 Linguagem: Inglês

10.1016/0006-291x(89)92001-9

1090-2104

Osamu Shinmi, Sadao Kimura, Toshihiro Yoshizawa, Tatsuya Sawamura, Yasuo Uchiyama, Yoshiki Sugita, Ichiro Kanazawa, Masashi Yanagisawa, Katsutoshi Goto, Tomoh Masaki,

Cardiovascular, Neuropeptides, and Oxidative Stress Research

We investigated the molecular forms of endothelin (ET) related peptides in porcine spinal cord by high performance liquid chromatography coupled with radioimmunoassays using three antisera raised against ET-1 and C-terminal fragments of ET-1 and big ET-1. ET-1 and its oxidized form were isolated as major immunoreactive peptides and sequenced. Furthermore, immunoreactivities like ET-3 and big ET-1(22–39) (contents: < 8% and < 1% of ET-1, respectively) were detected based on their chromatographic retention times and characteristics of immunoreactivity to the antisera. Big ET-1 was only scarecely detected. Immunohistochemical study showed the presence of ET-1-like immunoreactivity in motoneurons, dorsal horn neurons and dot- and fiber-like structures in the dorsal horn of lumbar spinal cord. These results indicate that ET-1 is present not only in endothelial cells but also in spinal cord, and that big ET-1 is converted into ET-1 in spinal cord by specific processing between Trp21-Val22. The data also indicate that ET-1 may act as a neuropeptide in the central nervous system.