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Lack of interaction of vasopressin with its antisense peptides: a functional and immunological study

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Jurzak,  Mirek
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Pávó,  Imre
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Fahrenholz,  Falk
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Jurzak, M., Pávó, I., & Fahrenholz, F. (1993). Lack of interaction of vasopressin with its antisense peptides: a functional and immunological study. Journal of receptor research, 13(5), 881-902. doi:10.3109/10799899309073699.


Cite as: https://hdl.handle.net/21.11116/0000-0008-A54E-7
Abstract
The peptide encoded in the 5' to 3' direction by rat vasopressin complementary RNA, rat PVA (H-Ser-Ser-Trp-Ala-Val-Leu-Glu-Val-Ala- OH) and the corresponding bovine PVA (H-Ala-Pro-Trp-Ala-Val-Leu-Glu-Val-Ala-OH) were investigated with respect to their interaction with [8-arginine] vasopressin (AVP) and V2 vasopressin receptor binding and function. Rat or bovine PVA did neither affect the binding of the hormone to the V2 receptor of bovine kidney membranes and LLC-PK1 pig kidney cells nor influence the AVP-induced cAMP-production in LLC-PK1 cells. Rat PVA was further investigated by the use of vasopressin-specific polyclonal and monoclonal antibodies with different affinity and epitope specificity. Consistent with receptor binding studies no inhibition of [3H]AVP-binding in fluid- or solid-phase antibody binding tests after preincubation with PVA was found. Direct interaction of rat PVA and [3H]AVP measured on solid surface was not observed in contrast to specific binding of the hormone with NP II and antibodies. In our study no evidence for an interaction of AVP and its antisense peptides was found.