TY - JOUR
T1 - Occurrence of a novel cardiac natriuretic peptide in rats
AU - Itoh, Hiroshi
AU - Nakao, Kazuwa
AU - Kambayashi, Yoshikazu
AU - Hosoda, Kiminori
AU - Saito, Yoshihiko
AU - Yamada, Takayuki
AU - Mukoyama, Masashi
AU - Arai, Hiroshi
AU - Shirakami, Gotaro
AU - Suga, Shin ichi
AU - Yoshida, Ikuyo
AU - Inouye, Ken
AU - Imura, Hiroo
N1 - Funding Information:
We thank Ms. Hiroko Fumon and Ms. Atsuko assistance. This work was supported in part the Japanese Ministry of Education, Science Ministry of Health and Welfare "Disorders of Committee, Japan, 1989, Life Science Research Physical and Chemical Research (RIKEN), Yamanouchi Foundation Research on Metabolic
Funding Information:
Furu for the secretarial by research grants from and Culture, the Japanese Adrenal Hormone" Research Project of Institute of Japan Tobacco Inc. and Disorders, by research
PY - 1989/6/15
Y1 - 1989/6/15
N2 - We established a specific radioimmunoassay for the ring structure of "iso-ANP" and detected iso-ANP[23-46]-like immunoreactivity (-LI) in the rat atrium (2.76 ± 0.5 μg/g) and ventricle (13.9 ± 5.7 ng/g). High performance-gel permeation chromatography revealed that iso-ANP[23-46]-LI in the rat heart was composed of two components with molecular weights of 10K and 5K. In reverse phase-high performance liquid chromatography, the retention times of these components were clearly different from that of synthetic iso-ANP. The 5K peptide was demonstrated to be present in the perfusate from isolated rat hearts and possessed binding ability to ANP receptors. This natriuretic peptide was, however, not detectable in other tissues including the brain. We conclude that the novel cardiac natriuretic peptide distinct from iso-ANP and ANP occurs in the rat heart and is secreted from the heart.
AB - We established a specific radioimmunoassay for the ring structure of "iso-ANP" and detected iso-ANP[23-46]-like immunoreactivity (-LI) in the rat atrium (2.76 ± 0.5 μg/g) and ventricle (13.9 ± 5.7 ng/g). High performance-gel permeation chromatography revealed that iso-ANP[23-46]-LI in the rat heart was composed of two components with molecular weights of 10K and 5K. In reverse phase-high performance liquid chromatography, the retention times of these components were clearly different from that of synthetic iso-ANP. The 5K peptide was demonstrated to be present in the perfusate from isolated rat hearts and possessed binding ability to ANP receptors. This natriuretic peptide was, however, not detectable in other tissues including the brain. We conclude that the novel cardiac natriuretic peptide distinct from iso-ANP and ANP occurs in the rat heart and is secreted from the heart.
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U2 - 10.1016/0006-291X(89)92661-2
DO - 10.1016/0006-291X(89)92661-2
M3 - Article
C2 - 2525379
AN - SCOPUS:0024354122
SN - 0006-291X
VL - 161
SP - 732
EP - 739
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -