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Secretoneurin

Introduction

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 epsinophils (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.

Singaling

Singaling

PI3 kinase, phosphodiesterase and phospholipase D inhibition inhobits its pro-migration effects, but blocking PKC and tyrosine kinases has notbeen shown to have effect. Downstream to these ERK type MAP kinase and AKT are activated.

References

References

Further reading

Further reading

  • Erickson JD, Lloyd R, Trojanowski JQ; et al. (1992). “Sites of synthesis of chromogranins A and B in the human brain”. Neuropeptides. 21 (4): 239–44. PMIDΒ 1518561.
  • Levine MA, Modi WS, O’Brien SJ (1992). “Mapping of the gene encoding the alpha subunit of the stimulatory G protein of adenylyl cyclase (GNAS1) to 20q13.2—-q13.3 in human by in situ hybridization”. Genomics. 11 (2): 478–9. PMIDΒ 1769666.
  • Gill BM, Barbosa JA, Dinh TQ; et al. (1991). “Chromogranin B: isolation from pheochromocytoma, N-terminal sequence, tissue distribution and secretory vesicle processing”. Regul. Pept. 33 (2): 223–35. PMIDΒ 1882087.
  • Benedum UM, Lamouroux A, Konecki DS; et al. (1987). “The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region”. EMBO J. 6 (5): 1203–11. PMIDΒ 3608978.
  • Benjannet S, Leduc R, Adrouche N; et al. (1988). “Chromogranin B (secretogranin I), a putative precursor of two novel pituitary peptides through processing at paired basic residues”. FEBS Lett. 224 (1): 142–8. PMIDΒ 3678488.
  • Benjannet S, Leduc R, Lazure C; et al. (1985). “GAWK, a novel human pituitary polypeptide: isolation, immunocytochemical localization and complete amino acid sequence”. Biochem. Biophys. Res. Commun. 126 (1): 602–9. PMIDΒ 3970711.
  • 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. PMIDΒ 7891024.
  • Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1–2): 171–4. PMIDΒ 8125298.
  • 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. PMIDΒ 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): 149–56. PMIDΒ 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, AustriaΒ : 1996). 105 (1): 39–51. PMIDΒ 9588759.
  • Marksteiner J, Bauer R, Kaufmann WA; et al. (1999). “PE-11, a peptide derived from chromogranin B, in the human brain”. Neuroscience. 91 (3): 1155–70. PMIDΒ 10391491.
  • Deloukas P, Matthews LH, Ashurst J; et al. (2002). “The DNA sequence and comparative analysis of human chromosome 20”. Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMIDΒ 11780052.
  • Yoo SH, You SH, Kang MK; et al. (2002). “Localization of the secretory granule marker protein chromogranin B in the nucleus. Potential role in transcription control”. J. Biol. Chem. 277 (18): 16011–21. doi:10.1074/jbc.M105594200. PMIDΒ 11854265.
  • Marksteiner J, Kaufmann WA, Gurka P, Humpel C (2002). “Synaptic proteins in Alzheimer’s disease”. J. Mol. Neurosci. 18 (1–2): 53–63. PMIDΒ 11931350.
  • Zhang B, Tan Z, Zhang C; et al. (2002). “Polymorphisms of chromogranin B gene associated with schizophrenia in Chinese Han population”. Neurosci. Lett. 323 (3): 229–33. PMIDΒ 11959426.
  • 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): 553–9. PMIDΒ 12091348.
  • Portela-Gomes GM, Stridsberg M (2002). “Region-specific antibodies to chromogranin B display various immunostaining patterns in human endocrine pancreas”. J. Histochem. Cytochem. 50 (8): 1023–30. PMIDΒ 12133905.
  • Kimura N, Yoshida R, Shiraishi S; et al. (2003). “Chromogranin A and chromogranin B in noninvasive and invasive breast carcinoma”. Endocr. Pathol. 13 (2): 117–22. PMIDΒ 12165659.
  • Portela-Gomes GM, Stridsberg M (2002). “Region-specific antibodies against chromogranin B display different immunoreactivity in the human pancreatic islet cell types”. Ann. N. Y. Acad. Sci. 971: 341–4. PMIDΒ 12438147.
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