Biology:Secretin receptor

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Short description: Protein-coding gene in the species Homo sapiens

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example


The secretin receptor is a protein that in humans is encoded by the SCTR gene. This protein is a G protein-coupled receptor which binds secretin and is the leading member (i.e., first cloned) of the secretin receptor family, also called class B GPCR subfamily.[1] SCTR belongs to the glucagon-VIP-secretin receptor family; its locus is 2q14.2.[2]

Interactions

The secretin receptor has been shown to interact with pituitary adenylate cyclase activating peptide.[3]

Clinical significance

Breast Cancer

SCTR neither uniformly upregulated or downregulated in tumors, hence, it has the potential to promote or suppress tumor proliferation.[4] In a study investigating methylation of the SCTR genes in breast cancer tissue, hypermethylation and downregulation were observed; pathway analysis in MCF-10A cells determined these most likely effect the G2/M stage checkpoint.[4] However, SCTR was overexpressed in MCF-7 cells, leading to increased proliferation and migration.[4] The study concluded that SCTR downregulates proliferation in normal breast cells and upregulates proliferation in breast cancer cells that have their proliferation downregulated by promoter methylation.[4]

Colorectal cancer

SCTR has been observed to be hypermethylated in colorectal cancer.[5] Moreover, because of the high frequency of hypermethylation at CpG islands in colorectal cancer, SCTR hypermethylation is an effective diagnostic marker that has achieved high diagnostic performance; colorectal cancer and precursor legions were able to be distinguished using SCTR methylation as a diagnostic tool.[6] Additionally, SCTR genes were found to be hypermethylated in cell-free DNA samples of colorectal cancer patients, but not in cells from healthy patients.[6]

References

  1. ↑ "Molecular pharmacology of the secretin receptor". Receptors & Channels 8 (3–4): 189–200. 2002. doi:10.1080/10606820213686. PMID 12529936. 
  2. ↑ "SCTR secretin receptor [Homo sapiens (human) - Gene - NCBI"]. https://www.ncbi.nlm.nih.gov/gene/6344. 
  3. ↑ "Chief cells possess a receptor with high affinity for PACAP and VIP that stimulates pepsinogen release". The American Journal of Physiology 263 (6 Pt 1): G901–7. December 1992. doi:10.1152/ajpgi.1992.263.6.G901. PMID 1335692. 
  4. ↑ 4.0 4.1 4.2 4.3 "SCTR regulates cell cycle-related genes toward anti-proliferation in normal breast cells while having pro-proliferation activity in breast cancer cells". International Journal of Oncology 47 (5): 1923–1931. November 2015. doi:10.3892/ijo.2015.3164. PMID 26397240. 
  5. ↑ "Epigenetic remodeling in colorectal cancer results in coordinate gene suppression across an entire chromosome band". Nature Genetics 38 (5): 540–549. May 2006. doi:10.1038/ng1781. PMID 16642018. 
  6. ↑ 6.0 6.1 "User:YonathanBiochemRec/Secretin receptor/Outline", Wikipedia, 2026-05-03, https://en.wikipedia.org/w/index.php?title=User:YonathanBiochemRec/Secretin_receptor/Outline&oldid=1352370022, retrieved 2026-05-03 

Further reading

  • "Secretin and vasoactive intestinal peptide receptors: members of a unique family of G protein-coupled receptors". Gastroenterology 114 (2): 382–397. February 1998. doi:10.1016/S0016-5085(98)70491-3. PMID 9453500. 
  • "Chief cells possess a receptor with high affinity for PACAP and VIP that stimulates pepsinogen release". The American Journal of Physiology 263 (6 Pt 1): G901–7. December 1992. doi:10.1152/ajpgi.1992.263.6.G901. PMID 1335692. 
  • "Molecular cloning and expression of a cDNA encoding the secretin receptor". The EMBO Journal 10 (7): 1635–1641. July 1991. doi:10.1002/j.1460-2075.1991.tb07686.x. PMID 1646711. 
  • "Secretin receptors in human pancreatic membranes". Pancreas 3 (5): 529–535. 1988. doi:10.1097/00006676-198810000-00004. PMID 3186683. 
  • "Molecular cloning and functional characterization of a human secretin receptor". Biochemical and Biophysical Research Communications 212 (1): 204–211. July 1995. doi:10.1006/bbrc.1995.1957. PMID 7612008. 
  • "Molecular cloning and expression of a human secretin receptor". Molecular Pharmacology 47 (3): 467–473. March 1995. doi:10.1016/S0026-895X(25)08566-9. PMID 7700244. 
  • "Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors". The Journal of Biological Chemistry 270 (24): 14394–14398. June 1995. doi:10.1074/jbc.270.24.14394. PMID 7782300. 
  • "Molecular cloning and functional expression of a human pancreatic secretin receptor". Biochemical and Biophysical Research Communications 207 (3): 883–890. February 1995. doi:10.1006/bbrc.1995.1268. PMID 7864894. 
  • "Cloning and functional expression of a human neuroendocrine vasoactive intestinal peptide receptor". Biochemical and Biophysical Research Communications 193 (2): 546–553. June 1993. doi:10.1006/bbrc.1993.1658. PMID 8390245. 
  • "Localization of the gene encoding the secretin receptor, SCTR, on human chromosome 2q14.1 by fluorescence in situ hybridization and chromosome morphometry". Genomics 29 (3): 817–818. October 1995. doi:10.1006/geno.1995.9922. PMID 8575789. 
  • "Lysine 173 residue within the first exoloop of rat secretin receptor is involved in carboxylate moiety recognition of Asp 3 in secretin". Biochemical and Biophysical Research Communications 218 (3): 842–846. January 1996. doi:10.1006/bbrc.1996.0150. PMID 8579602. 
  • "Functional antagonism of the human secretin receptor by a recombinant protein encoding the N-terminal ectodomain of the receptor". Receptors & Signal Transduction 7 (3): 143–150. 1998. PMID 9440501. 
  • "A role for receptor kinases in the regulation of class II G protein-coupled receptors. Phosphorylation and desensitization of the secretin receptor". The Journal of Biological Chemistry 273 (12): 6756–6762. March 1998. doi:10.1074/jbc.273.12.6756. PMID 9506976. 
  • "The human secretin receptor gene: genomic organization and promoter characterization". FEBS Letters 455 (3): 209–214. July 1999. doi:10.1016/S0014-5793(99)00864-9. PMID 10437774. 
  • "Role of N-linked glycosylation on the function and expression of the human secretin receptor". Endocrinology 140 (11): 5102–5111. November 1999. doi:10.1210/endo.140.11.7134. PMID 10537138. 
  • "Functional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptor". Endocrinology 142 (9): 3926–3934. September 2001. doi:10.1210/endo.142.9.8389. PMID 11517171. 
  • "CpG methylation and transcription factors Sp1 and Sp3 regulate the expression of the human secretin receptor gene". Molecular Endocrinology 18 (2): 471–483. February 2004. doi:10.1210/me.2003-0245. PMID 14645499. 



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