TY - JOUR
T1 - Presence of endothelin-1 in porcine spinal cord
T2 - Isolation and sequence determination
AU - Shinmi, Osamu
AU - Kimura, Sadao
AU - Yoshizawa, Toshihiro
AU - Sawamura, Tatsuya
AU - Uchiyama, Yasuo
AU - Sugita, Yoshiki
AU - Kanazawa, Ichiro
AU - Yanagisawa, Masashi
AU - Goto, Katsutoshi
AU - Masaki, Tomoh
N1 - Funding Information:
Acknowlednments: We wish to thank Drs. M. Fallon and Y. Kasuya for reading the manuscript, Dr. K. Yamamotof or the peptide sequencing and A. Fujimori and Y. Tomobe for the technical assistance. This work was supported in part by grants from University of Tsukuba Project Research, the Ministries of Education, Science and Culture of Japan and Ciba Geigy Foundation.
PY - 1989/7/14
Y1 - 1989/7/14
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024381310&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024381310&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(89)92001-9
DO - 10.1016/0006-291X(89)92001-9
M3 - Article
C2 - 2665739
AN - SCOPUS:0024381310
VL - 162
SP - 340
EP - 346
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -