High affinity displacement of [3H]NPY binding to the crude venom of Conus anemone by insect neuropeptides
Le, M.T.; Vanderheyden, P.M.L.; De Backer, J.-P.; Vanquelin, G.; Vanden Broeck, J. (1999). High affinity displacement of [3H]NPY binding to the crude venom of Conus anemone by insect neuropeptides. Biochem. Biophys. Res. Commun. 262(1): 180-186. https://dx.doi.org/10.1006/bbrc.1999.1177
In: Biochemical and Biophysical Research Communications. ACADEMIC PRESS INC ELSEVIER SCIENCE: San Diego etc.. ISSN 0006-291X; e-ISSN 1090-2104, more
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| Keywords |
Conus anemone Lamarck, 1810 [WoRMS]
Marine/Coastal |
| Author keywords |
Conus anemone; insect peptide; NPY; Y-1 receptors; anti-NPY antibodies |
| Authors | | Top |
- Le, M.T.
- Vanderheyden, P.M.L.
- De Backer, J.-P.
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- Vanquelin, G.
- Vanden Broeck, J.
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| Abstract |
The venom from Conus anemone contains a protein, named ANPY toxin, which displayed high affinity (IC50 in nanomolar range) to neuropeptide Y (NPY), [Leu31, Pro34]NPY, peptide YY, pancreatic polypeptide, the Y1 antagonist 1229U91, and C-terminal NPY fragments. N-terminal fragments and the free acid form of NPY did not bind to ANPY. The truncated NPY fragments displayed very low affinity to Y1 receptors and partially inhibited [3H]NPY binding to anti-NPY antiserum. Several insect neuropeptides, the sequences of which related to the C-terminal fragments of NPY, were observed to bind with similar affinity or even 20 times higher (Lom-MS and Scg-NPF) affinity than NPY. In contrast, no significant binding of these insect peptides was observed for Y1 receptors and anti-NPY antiserum. Therefore, ANPY can be viewed as an acceptor that binds with very high affinity to a broad spectrum of vertebrate and invertebrate neuropeptides that share a similar C-terminal amino acid sequence. |
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