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  • Title: Binding of CNP-22 and CNP-53 to cultured mouse astrocytes and effects on cyclic GMP.
    Author: Yeung VT, Ho SK, Nicholls MG, Cockram CS.
    Journal: Peptides; 1996; 17(1):101-6. PubMed ID: 8822517.
    Abstract:
    We examined the binding characteristics of the two endogenous forms of C-type natriuretic peptide (CNP-22 and CNP-53) and their effects on cyclic GMP (cGMP) accumulation in primary cultures of mouse astrocytes. CNP-22 and CNP-53 competitively inhibited the specific binding of [125I][Tyr0]CNP, with an IC50 value of 32 and 37 pM, respectively. They also induced cGMP production in a dose-dependent and similar fashion, with an EC50 of 32 nM and maximal cGMP responses of 189.6 +/- 21.6 pmol/mg protein for CNP-22, and 170.3 +/- 18.7 pmol/mg protein for CNP-53, respectively. The effect of CNP-53 could not be explained by conversion to CNP-22, because HPLC analysis did not show significant proteolytic conversion by astrocytes during the incubation. Our results suggest that CNP-53 could, in concert with other natriuretic peptides, have a neuromodulatory function and thereby contribute to the central regulation of hemodynamic and fluid homeostasis.
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