Secretoneurin

Secretogranin II
Identifiers
Symbols	SCG2 ; CHGC; EM66; SN; SgII
External IDs	OMIM: 118930 MGI: 103033 HomoloGene: 2591 GeneCards: SCG2 Gene
Gene ontology Molecular function • cytokine activity • protein binding • chemoattractant activity Cellular component • extracellular space • secretory granule Biological process • MAPK cascade • angiogenesis • negative regulation of endothelial cell proliferation • positive regulation of endothelial cell proliferation • inflammatory response • protein secretion • intracellular signal transduction • endothelial cell migration • eosinophil chemotaxis • positive chemotaxis • induction of positive chemotaxis • negative regulation of endothelial cell apoptotic process • negative regulation of extrinsic apoptotic signaling pathway Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7857	20254
Ensembl	ENSG00000171951	ENSMUSG00000050711
UniProt	P13521	Q03517
RefSeq (mRNA)	NM_003469	NM_009129
RefSeq (protein)	NP_003460	NP_033155
Location (UCSC)	Chr 2: 223.6 – 223.6 Mb	Chr 1: 79.43 – 79.44 Mb
PubMed search

Secretoneurin, is a 33-amino acid neuropeptide derived from secretogranin II (chromogranin C, CHGC).

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. Secretoneurin also stimulates dopamine release from the central striatal neurons and basal ganglia.

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

Further reading

• Stridsberg M, Oberg K, Li Q, et al. (1995). "Measurements of chromogranin A, chromogranin B (secretogranin I), chromogranin C (secretogranin II) and pancreastatin in plasma and urine from patients with carcinoid tumours and endocrine pancreatic tumours". J. Endocrinol. 144 (1): 49–59. doi:10.1677/joe.0.1440049. PMID 7891024.
• Kirchmair R, Hogue-Angeletti R, Gutierrez J, Fischer-Colbrie R, Winkler H (1993). "Secretoneurin–a neuropeptide generated inbrain,adrenalmedullaandotherendocrinetissues by proteolytic processing of secretogranin II (chromogranin C)". J. Neurosci. 53 (2): 359–65. doi:10.1016/0306-4522(93)90200-Y. PMID 8492910.
• Portela-Gomes GM, Stridsberg M, Johansson H, Grimelius L (1997). "Complex co-localization of chromogranins and neurohormones in the human gastrointestinal tract". J. Histochem. Cytochem. 45 (6): 815–22. doi:10.1177/002215549704500606. PMID 9199667.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Eder U, Leitner B, Kirchmair R, et al. (1998). "Levels and proteolytic processing of chromogranin A and B and secretogranin II in cerebrospinal fluid in neurological diseases". Journal of neural transmission (Vienna, Austria : 1996) 105 (1): 39–52. doi:10.1007/s007020050036. PMID 9588759.
• Tasiemski A, Hammad H, Vandenbulcke F, et al. (2002). "Presence of chromogranin-derived antimicrobial peptides in plasma during coronary artery bypass surgery and evidence of an immune origin of these peptides". Blood 100 (2): 553–559. doi:10.1182/blood.V100.2.553. PMID 12091348.

External links

• secretoneurin at the US National Library of Medicine Medical Subject Headings (MeSH)