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Onset of neurophysin self-association upon neurophysin/neuropeptide hormone precursor biosynthesis
Journal article   Peer reviewed

Onset of neurophysin self-association upon neurophysin/neuropeptide hormone precursor biosynthesis

Irwin M. Chaiken, Hidetsune Tamaoki, Michael J. Brownstein and Harold Gainer
FEBS letters, v 164(2), pp 361-365
1983
PMID: 6653793

Abstract

BNP-II, bovine neurophysin II (vasopressin-associated) Hormone—protein interaction KNPL, dissociation constant of unliganded, soluble NP for unliganded, immobilized NP KNPLL dissociation constant of liganded, soluble NP for liganded, immobilized NP KproNPL, dissociation constant of rat pro-NP/harmone for unliganded, immobilized NP LVP and AVP, lysine and arginine vasopressin Neuropeptide hormone Neurophysin NP, neurophysin OT, oxytocin pro-NP/AVP, pulse-labelled biosynthetic precursor for AVP and AVP-associated NP pro-NP/OT, pulse-labelled biosynthetic precursor for OT and OT-associated NP Prohormone association Quantitative affinity chromatography
The potential of the common biosynthetic precursor of neurophysin and neuropeptide hormones to self-associate has been assessed by quantitative affinity chromatographic analysis. The precursor form, with the hormone sequence in the amino terminal region and assumed able to interact intramolecularly with the hormone binding site of the neurophysin domain of the folded precursor, exhibits an affinity for neurophysin-agarose which is intermediate between those of unliganded neurophysin and non-covalently hormone-liganded neurophysin. The results lead to a prediction that neurophysin self-association is established upon precursor synthesis and prior to limited proteolysis of the precursor to release mature neurophysin and hormone components. Such self-association could play a role in packaging of the precursor into secretory granules and in regulating subsequent precursor processing events within the granules.

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Web of Science research areas
Biochemistry & Molecular Biology
Biophysics
Cell Biology
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