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NERP-3 and NERP-4

Molecular Characterization and Biological Function of Neuroendocrine Regulatory Peptide-3 in the Rat

Neuroendocrine regulatory peptide (NERP)-3, derived from the neurosecretory protein VGF (non-aconymic), is a new biologically active peptide identified through peptidomic analysis of the peptides secreted by an endocrine cell line. Using a specific antibody recognizing the C-terminal region of NERP-3, immunoreactive (ir)-NERP-3 was identified in acid extracts of rat brain and gut as a 30-residue NERP-3 with N-terminal pyroglutamylation. Assessed by radioimmunoassay, ir-NERP-3 was more abundant in the brain, including the posterior pituitary (PP), than in the gut. Immunohistochemistry demonstrated that ir-NERP-3 was significantly increased in the suprachiasmatic nucleus, the magnocellular division of the paraventricular nucleus, and the external layer of the median eminence, but not in the supraoptic nucleus, after dehydration. The immunoreactivity was, however, markedly decreased in all of these locations after chronic salt loading. Intracerebroventricular administration of NERP-3 in conscious rats induced Fos expression in a subset of arginine vasopressin (AVP)-containing neurons in the supraoptic nucleus and the magnocellular division of the paraventricular nucleus. On in vitro isolated rat PP preparations, NERP-3 caused a significant AVP release in a dose-related manner, suggesting that NERP-3 in the PP could be an autocrine activator of AVP release. Taken together, the present results suggest that NERP-3 in the hypothalamo-neurohypophyseal system may be involved in the regulation of body fluid balance.

Hiroaki Fujihara, Endocrinology,  153: 1377-1386, 2012.

 

Peptidomics-based Discovery of Bioactive Neuropeptides from the Neurosecretory Protein VGF

Peptide hormones and neuropeptides constitute an important class of naturally occurring peptides that are generated from precursor proteins by limited proteolytic processing. An important but unaddressed issue in peptidomics is to pin down novel bioactive peptides among a bulk of peptide sequences provided by tandem mass spectrometry. Here, we describe an approach to simultaneously screen for bioactive peptides and their target tissues. The principle behind this approach is to identify intact secretory peptides showing interspecies homology that have the ability to raise intracellular calcium levels. In practice, we used nanoflow liquid chromatography/tandem mass spectrometry to analyze peptides released by exocytosis from cultured cells. Peptide sequence information was utilized to deduce intact peptide forms, among which those highly conserved between species are selected and tested on an ex vivo calcium assay using tissue pieces from transgenic mice that systemically express the calcium indicator apoaequorin. The calcium assay can be applied to various cell types, including those not amenable to in vitro culture. We used this approach to identify novel bioactive peptides derived from the neurosecretory protein VGF, which evoke a calcium response in the pituitary and hypothalamus.

Peptides for Calcium Mobilization Using Tissues from Apoaequorin Transgenic Mice

NERP-3 NERP-4 Calcium Mobilization Using Tissues Mice

Sasaki K., et al. J. Proteome Res. 2010 Aug 4. [Epub ahead of print]


VGF Peptide Levels in Different Tissues

VGF Levels in Tissue

For more regarding NERP-1 and NERP-2, please visit the Big NERP-2 & TLQP-62 Information Page.

NERP-4 (Human, Rat, Mouse) RIA Kit (RK-007-71)

RK-007-71

 

Amino Acid Sequence Alignment of Rat/Mouse and Human NERP-3 (007-67)

NERP-3 Sequence

 

Amino Acid Sequence Alignment of Rat/Mouse and Human NERP-4 (007-71)

NERP-4 Sequence

 

Amino Acid Sequence of Rat and Human VGF

 

VGF;NERP-2-TLQP-62;TLQP21;AQEE-30

%007-67%;%007-71%


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