Secretoneurin

Secretoneurin, also called Chromogranin B (CHGB), is a 33-amino acid neuropeptide derived from secretogranin II (chromogranin C, CHGC) . Because of this secretogranin II is also called secretoneurin-included (SN, included).

Chromogranin B is a tyrosine-sulfated secretory protein found in a wide variety of peptidergic endocrine cells. Chromogranin functions as a neuroendocrine secretory granule protein which may be the precursor for other biologically active peptides.^[1]

Secretoneurin is involved in chemotaxis of monocytes and eosinophils (comparable in potency to IL8) and endothelial cells and in regulation of endothelial cell proliferation. Highest secretoneurin levels are found in anterior pituitary, followed by adrenal medulla and posterior pituitary hypothalamus (2- to 6-fold lower levels in other brain regions investigated). Secretoneurin has been shown to have potent angiogenic activity in vivo in mouse cornea model and in vitro in a 3-dimensional gel.

1 Signaling
2 References
3 Further reading
4 External links

Signaling

PI3 kinase, phosphodiesterase and phospholipase D inhibition inhibits its pro-migration effects, but blocking PKC and tyrosine kinases has not been shown to have effect. Downstream to these ERK type MAP kinase and AKT are activated.

References

^ "Entrez Gene: CHGB chromogranin B (secretogranin 1)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1114.

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