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Clinical Chemistry 38: 2136-2139, 1992;
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Clinical Chemistry, Vol 38, 2136-2139, Copyright © 1992 by American Association for Clinical Chemistry

Concentrations and molecular forms of C-type natriuretic peptide in brain and cerebrospinal fluid

K Togashi, T Kameya, T Kurosawa, N Hasegawa and M Kawakami
Department of Molecular Biology, Kitasato University School of Medicine, Kanagawa, Japan.

To develop a radioimmunoassay (RIA) specific for human C-type natriuretic peptide (hCNP), we used a highly specific antiserum raised in rabbits. Quantitative inhibition tests with various natriuretic peptides demonstrated that the 50% inhibitory dose of hCNP was 15 fmol, whereas those of other natriuretic peptides were 10(5)-fold higher, indicating a specificity satisfactory for determining concentrations of hCNP in tissues. Using this antiserum, we detected immunoreactive hCNP (ir-hCNP) in various regions of human brain and spinal cord, as well as in cerebrospinal fluid (CSF). The ir-hCNP concentrations in human neural tissues were approximately 10-fold higher than those of immunoreactive human atrial natriuretic peptide (ir-hANP). The mean (+/- SD) concentration of ir-hCNP (72.0 +/- 17.8 ng/L) in CSF also was 10- fold higher than that of ir-hANP (5.2 +/- 2.1 ng/L). Using gel- permeation chromatography, we identified two molecular forms of ir-hCNP in brain and CSF: a 2-kDa form corresponding to mature hCNP, which is composed of 22 amino acid residues (hCNP-22), and a 5- to 6-kDa form corresponding to an N-terminally extended molecule (hCNP-53). The latter form was predominant in brain; the former was the main constituent of hCNP in CSF. These results support the hypothesis that hCNP is a major natriuretic peptide, is synthesized in human brain, and functions in human central nervous tissues.


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Copyright © 1992 by the American Association for Clinical Chemistry.