Pituitary adenylate cyclase activating peptide

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Adenylate cyclase activating polypeptide 1 (pituitary)
PDB rendering based on 2d2p.
Available structures: 2d2p, 2jod
Identifiers
Symbol(s) ADCYAP1; MGC126852; PACAP
External IDs OMIM: 102980 MGI: 105094 HomoloGene: 869
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 116 11516
Ensembl ENSG00000141433 ENSMUSG00000024256
Uniprot P18509 Q3UYH8
Refseq NM_001117 (mRNA)
NP_001108 (protein)		 NM_009625 (mRNA)
NP_033755 (protein)
Location Chr 18: 0.9 - 0.9 Mb Chr 17: 93.5 - 93.51 Mb
Pubmed search [1] [2]

Adenylate cyclase activating polypeptide 1 (pituitary), also known as ADCYAP1, is a human gene.[1]

Pituitary adenylate cyclase activating peptide is a peptide similar to vasoactive intestinal peptide. One of its effects is to stimulate enterochromaffin-like cells.

It binds to vasoactive intestinal peptide receptor.

This gene encodes adenylate cyclase activating polypeptide 1. Mediated by adenylate cyclase activating polypeptide 1 receptors, this polypeptide stimulates adenylate cyclase and subsequently increases the cAMP level in target cells. Adenylate cyclase activating polypeptide 1 is not only a hypophysiotropic hormone, but also functions as a neurotransmitter and neuromodulator. In addition, it plays a role in paracrine and autocrine regulation of certain types of cells. This gene is composed of five exons. Exons 1 and 2 encode the 5' UTR and signal peptide, respectively; exon 4 encodes an adenylate cyclase activating polypeptide 1-related peptide; and exon 5 encodes the mature peptide and 3' UTR. This gene encodes three different mature peptides, including two isotypes: a shorter form and a longer form.[1]

Contents

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: ADCYAP1 adenylate cyclase activating polypeptide 1 (pituitary).

[edit] Further reading

  • Geng L, Ju G (2000). "[The discovery of pituitary adenylate cyclase activating polypeptide (PACAP) and its research progress]". Sheng li ke xue jin zhan [Progress in physiology] 28 (1): 29–34. PMID 10921074. 
  • Fahrenkrug J (2002). "Gut/brain peptides in the genital tract: VIP and PACAP.". Scand. J. Clin. Lab. Invest. Suppl. 234: 35–9. PMID 11713978. 
  • Waschek JA (2002). "Multiple actions of pituitary adenylyl cyclase activating peptide in nervous system development and regeneration.". Dev. Neurosci. 24 (1): 14–23. PMID 12145407. 
  • Fahrenkrug J (2006). "PACAP--a multifacetted neuropeptide.". Chronobiol. Int. 23 (1-2): 53–61. doi:10.1080/07420520500464569. PMID 16687279. 
  • Conconi MT, Spinazzi R, Nussdorfer GG (2006). "Endogenous ligands of PACAP/VIP receptors in the autocrine-paracrine regulation of the adrenal gland.". Int. Rev. Cytol. 249: 1–51. doi:10.1016/S0074-7696(06)49001-X. PMID 16697281. 
  • Nakata M, Yada T (2007). "PACAP in the glucose and energy homeostasis: physiological role and therapeutic potential.". Curr. Pharm. Des. 13 (11): 1105–12. PMID 17430174. 
  • Felley CP, Qian JM, Mantey S, et al. (1993). "Chief cells possess a receptor with high affinity for PACAP and VIP that stimulates pepsinogen release.". Am. J. Physiol. 263 (6 Pt 1): G901–7. PMID 1335692. 
  • Inooka H, Endo S, Kitada C, et al. (1993). "Pituitary adenylate cyclase activating polypeptide (PACAP) with 27 residues. Conformation determined by 1H NMR and CD spectroscopies and distance geometry in 25% methanol solution.". Int. J. Pept. Protein Res. 40 (5): 456–64. PMID 1483839. 
  • Hosoya M, Kimura C, Ogi K, et al. (1992). "Structure of the human pituitary adenylate cyclase activating polypeptide (PACAP) gene.". Biochim. Biophys. Acta 1129 (2): 199–206. PMID 1730060. 
  • Ohkubo S, Kimura C, Ogi K, et al. (1992). "Primary structure and characterization of the precursor to human pituitary adenylate cyclase activating polypeptide.". DNA Cell Biol. 11 (1): 21–30. PMID 1739432. 
  • Kimura C, Ohkubo S, Ogi K, et al. (1990). "A novel peptide which stimulates adenylate cyclase: molecular cloning and characterization of the ovine and human cDNAs.". Biochem. Biophys. Res. Commun. 166 (1): 81–9. PMID 2302217. 
  • Cross SH, Charlton JA, Nan X, Bird AP (1994). "Purification of CpG islands using a methylated DNA binding column.". Nat. Genet. 6 (3): 236–44. doi:10.1038/ng0394-236. PMID 8012384. 
  • Inagaki N, Yoshida H, Mizuta M, et al. (1994). "Cloning and functional characterization of a third pituitary adenylate cyclase-activating polypeptide receptor subtype expressed in insulin-secreting cells.". Proc. Natl. Acad. Sci. U.S.A. 91 (7): 2679–83. PMID 8146174. 
  • Ohtaki T, Masuda Y, Ishibashi Y, et al. (1994). "Purification and characterization of the receptor for pituitary adenylate cyclase-activating polypeptide.". J. Biol. Chem. 268 (35): 26650–7. PMID 8253796. 
  • Pérez-Jurado LA, Francke U (1993). "Dinucleotide repeat polymorphism at the human pituitary adenylate cyclase activating polypeptide (PACAP) gene.". Hum. Mol. Genet. 2 (6): 827. PMID 8353512. 
  • Weber B, Riess O, Daneshvar H, et al. (1993). "(CA)n-dinucleotide repeat at the PDEB locus in 4p16.3.". Hum. Mol. Genet. 2 (6): 827. PMID 8394765. 
  • Wray V, Kakoschke C, Nokihara K, Naruse S (1993). "Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy.". Biochemistry 32 (22): 5832–41. PMID 8504103. 
  • Gourlet P, Vandermeers A, Robberecht P, Deschodt-Lanckman M (1997). "Vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating peptide (PACAP-27, but not PACAP-38) degradation by the neutral endopeptidase EC 3.4.24.11.". Biochem. Pharmacol. 54 (4): 509–15. PMID 9313778. 
  • Zeng N, Athmann C, Kang T, et al. (1999). "PACAP type I receptor activation regulates ECL cells and gastric acid secretion.". J. Clin. Invest. 104 (10): 1383–91. PMID 10562300. 
  • Dautzenberg FM, Mevenkamp G, Wille S, Hauger RL (2000). "N-terminal splice variants of the type I PACAP receptor: isolation, characterization and ligand binding/selectivity determinants.". J. Neuroendocrinol. 11 (12): 941–9. PMID 10583729. 

[edit] External links

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