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Asteropsin A: an unusual cystine-crosslinked peptide from porifera enhances neuronal Ca2+ influx.


ABSTRACT: Herein we report the discovery of a cystine-crosslinked peptide from Porifera along with high-quality spatial details accompanied by the description of its unique effect on neuronal calcium influx.Asteropsin A (ASPA) was isolated from the marine sponge Asteropus sp., and its structure was independently determined using X-ray crystallography (0.87 angstroms) and solution NMR spectroscopy.An N-terminal pyroglutamate modification, uncommon cis proline conformations, and absence of basic residues helped distinguish ASPA from other cystine-crosslinked knot peptides. ASPA enhanced Ca2+ influx in murine cerebrocortical neuron cells following the addition of the Na+ channel activator veratridine but did not modify the oscillation frequency or amplitude of neuronal Ca2+ currents alone. Allosterism at neurotoxin site 2 was not observed, suggesting an alternative to the known Na+ channel interaction.Together with a distinct biological activity, the origin of ASPA suggests a new subclass of cystine-rich knot peptides associated with Porifera.The discovery of ASPA represents a distinctive addition to an emerging subclass of cystine-crosslinked knot peptides from Porifera.

SUBMITTER: Li H 

PROVIDER: S-EPMC4137556 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Asteropsin A: an unusual cystine-crosslinked peptide from porifera enhances neuronal Ca2+ influx.

Li Huayue H   Bowling John J JJ   Fronczek Frank R FR   Hong Jongki J   Jabba Sairam V SV   Murray Thomas F TF   Ha Nam-Chul NC   Hamann Mark T MT   Jung Jee H JH  

Biochimica et biophysica acta 20130301 3


<h4>Background</h4>Herein we report the discovery of a cystine-crosslinked peptide from Porifera along with high-quality spatial details accompanied by the description of its unique effect on neuronal calcium influx.<h4>Methods</h4>Asteropsin A (ASPA) was isolated from the marine sponge Asteropus sp., and its structure was independently determined using X-ray crystallography (0.87 angstroms) and solution NMR spectroscopy.<h4>Results</h4>An N-terminal pyroglutamate modification, uncommon cis prol  ...[more]

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