Cortistatin (neuropeptide)

Not to be confused with the steroids also called cortistatins (chemical structures: cortistatin A, C, and J).

Cortistatin
Identifiers
Symbols	CORT; CST-14; CST-17; CST-29
External IDs	OMIM: 602784 MGI: 109538 HomoloGene: 997 GeneCards: CORT Gene
Gene Ontology Molecular function • G-protein-coupled receptor binding • neuropeptide hormone activity Cellular component • extracellular region • soluble fraction Biological process • inhibition of adenylate cyclase activity by G-protein signaling pathway • synaptic transmission Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1325	12854
Ensembl	ENSG00000241563	ENSMUSG00000028971
UniProt	O00230	P56469
RefSeq (mRNA)	NM_001302	NM_007745.3
RefSeq (protein)	NP_001293	NP_031771.1
Location (UCSC)	Chr 1: 10.51 – 10.51 Mb	Chr 4: 148.5 – 148.5 Mb
PubMed search	[1]	[2]

Precortistatin is a protein that in humans is encoded by the CORT gene.^[1][2] The 105 amino acid residue human precortistatin in turn is cleaved into cortistatin-17 and cortistatin-29. Cortistatin-17 is the only active peptide derived from the precursor.^[1] Cortistatin (or more specifically cortistatin-17) is a neuropeptide that is expressed in inhibitory neurons of the cerebral cortex, and which has a strong structural similarity to somatostatin. Unlike somatostatin, when infused into the brain, it enhances slow-wave sleep. It binds to sites in the cortex, hippocampus and the amygdala.

Function

Cortistatin is a neuropeptide with strong structural similarity to somatostatin (both peptides belong to the same family). It binds to all known somatostatin receptors, and shares many pharmacological and functional properties with somatostatin, including the depression of neuronal activity. However, it also has many properties distinct from somatostatin, such as induction of slow-wave sleep, apparently by antagonism of the excitatory effects of acetylcholine on the cortex, reduction of locomotor activity, and activation of cation selective currents not responsive to somatostatin.^[2]

References

1. ^ ^{a b} de Lecea L, Ruiz-Lozano P, Danielson PE, Peelle-Kirley J, Foye PE, Frankel WN, Sutcliffe JG (Sep 1997). "Cloning, mRNA expression, and chromosomal mapping of mouse and human preprocortistatin". Genomics 42 (3): 499–506. doi:10.1006/geno.1997.4763. PMID 9205124. 
2. ^ ^{a b} "Entrez Gene: CORT cortistatin". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1325. 

Further reading

• Spier AD, de Lecea L (2001). "Cortistatin: a member of the somatostatin neuropeptide family with distinct physiological functions.". Brain Res. Brain Res. Rev. 33 (2-3): 228–41. doi:10.1016/S0165-0173(00)00031-X. PMID 11011067. 
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
• Fukusumi S, Kitada C, Takekawa S, et al. (1997). "Identification and characterization of a novel human cortistatin-like peptide.". Biochem. Biophys. Res. Commun. 232 (1): 157–63. doi:10.1006/bbrc.1997.6252. PMID 9125122. 
• Puebla L, Mouchantaf R, Sasi R, et al. (1999). "Processing of rat preprocortistatin in mouse AtT-20 cells.". J. Neurochem. 73 (3): 1273–7. doi:10.1046/j.1471-4159.1999.0731273.x. PMID 10461921. 
• Ejeskär K, Abel F, Sjöberg R, et al. (2000). "Fine mapping of the human preprocortistatin gene (CORT) to neuroblastoma consensus deletion region 1p36.3→p36.2, but absence of mutations in primary tumors.". Cytogenet. Cell Genet. 89 (1-2): 62–6. doi:10.1159/000015566. PMID 10894940. 
• Deghenghi R, Papotti M, Ghigo E, Muccioli G (2001). "Cortistatin, but not somatostatin, binds to growth hormone secretagogue (GHS) receptors of human pituitary gland.". J. Endocrinol. Invest. 24 (1): RC1–3. PMID 11227737. 
• Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression.". Nat. Biotechnol. 19 (5): 440–5. doi:10.1038/88107. PMID 11329013. 
• Broglio F, Arvat E, Benso A, et al. (2002). "Endocrine activities of cortistatin-14 and its interaction with GHRH and ghrelin in humans.". J. Clin. Endocrinol. Metab. 87 (8): 3783–90. doi:10.1210/jc.87.8.3783. PMID 12161511. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Dalm VA, van Hagen PM, van Koetsveld PM, et al. (2003). "Cortistatin rather than somatostatin as a potential endogenous ligand for somatostatin receptors in the human immune system.". J. Clin. Endocrinol. Metab. 88 (1): 270–6. doi:10.1210/jc.2002-020950. PMID 12519865. 
• Dalm VA, van Hagen PM, van Koetsveld PM, et al. (2003). "Expression of somatostatin, cortistatin, and somatostatin receptors in human monocytes, macrophages, and dendritic cells.". Am. J. Physiol. Endocrinol. Metab. 285 (2): E344–53. doi:10.1152/ajpendo.00048.2003. PMID 12684217. 
• Robas N, Mead E, Fidock M (2004). "MrgX2 is a high potency cortistatin receptor expressed in dorsal root ganglion.". J. Biol. Chem. 278 (45): 44400–4. doi:10.1074/jbc.M302456200. PMID 12915402. 
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=403697. 
• Papotti M, Tarabra E, Allia E, et al. (2004). "Presence of cortistatin in the human pancreas.". J. Endocrinol. Invest. 26 (8): RC15–8. PMID 14669820. 
• Hernández C, Carrasco E, Casamitjana R, et al. (2005). "Somatostatin molecular variants in the vitreous fluid: a comparative study between diabetic patients with proliferative diabetic retinopathy and nondiabetic control subjects.". Diabetes Care 28 (8): 1941–7. doi:10.2337/diacare.28.8.1941. PMID 16043736. 

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