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EGFP-tagged vasopressin precursor protein sorting into large dense core vesicles and secretion from PC12 cells.

Abstract：

:1. Hypothalamic magnocellular neurons synthesize, store, and secrete large quantities of the neuropeptides, vasopressin (VP) and oxytocin (OT), which are synthesized as protein precursors also containing proteins called neurophysins. These protein precursors are sorted through the regulated secretory pathway (RSP), packaged into large dense core vesicles LDCVs, and their peptide products are secreted from nerve terminals in the posterior pituitary. 2. It has been hypothesized that this efficient packaging is dependent on the interaction of the peptide with neurophysin in a complex that forms the granule core. To test this, PC12 cells were transfected with vasopressin precursor DNA constructs that either contained or deleted the neurophysin moiety and tagged with enhanced green fluorescent protein (EGFP) as reporters. The intracellular routing and secretion of the EGFP-tagged VP precursor proteins were studied by in differentiated PC12 cells by fluorescence microscopy, electron microscopic immunocytochemistry, and fluorescent imaging techniques. 3. The data showed that only when the neurophysin was present in the VP precursor construct did the fluorescent fusion protein become routed to the RSP and get efficiently packaged into LDCVs and secreted. These data are consistent with the view that routing of the precursor to LDCVs requires the amino acids that encode the intravesicular chaperone, neurophysin.

journal_name

Cell Mol Neurobiol

journal_title

Cellular and molecular neurobiology

authors

Zhang BJ,Yamashita M,Fields R,Kusano K,Gainer H

doi

10.1007/s10571-005-3970-x

subject

Has Abstract

pub_date

2005-06-01 00:00:00

pages

581-605

issue

3-4

eissn

0272-4340

issn

1573-6830

journal_volume

25

pub_type

杂志文章

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