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Title: High affinity displacement of [H-3]NPY binding to the crude venom of Conus anemone by insect neuropeptides
Authors: Le, MT ×
Vanderheyden, PML
De Backer, JP
Vauquelin, G
Vanden Broeck, Jozef #
Issue Date: Aug-1999
Publisher: Academic press inc
Series Title: Biochemical and Biophysical Research Communications vol:262 issue:1 pages:180-186
Abstract: The venom from Conus anemone contains a protein, named ANPY toxin, which displayed high affinity (IC50 in nanomolar range) to neuropeptide Y (NPY), [Leu(31), Pro(34)]NPY, peptide YY, pancreatic polypeptide, the Y-1 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 Y-1 receptors and partially inhibited [H-3]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 Y-1 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. (C) 1999 Academic Press.
ISSN: 0006-291X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Animal Physiology and Neurobiology Section - miscellaneous
× corresponding author
# (joint) last author

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