Biology:ASPH
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Short description: Protein and coding gene in humans
 Generic protein structure example |
Aspartyl/asparaginyl beta-hydroxylase (HAAH) is an enzyme that in humans is encoded by the ASPH gene.[1][2][3] ASPH is an alpha-ketoglutarate-dependent hydroxylase, a superfamily non-haem iron-containing proteins.
Function
This gene is thought to play an important role in calcium homeostasis. Alternative splicing of this gene results in five transcript variants which vary in protein translation, the coding of catalytic domains, and tissue expression. Variation among these transcripts impacts their functions which involve roles in the calcium storage and release process in the endoplasmic and sarcoplasmic reticulum as well as hydroxylation of aspartic acid and asparagine in epidermal growth factor-like domains of various proteins.[3]
Clinical significance
As early as 1996, the over-expression of HAAH was recognized as an indicator of carcinoma in humans. Further research has correlated elevated HAAH levels (variously in affected tissue or blood serum) with hepatocellular (liver) carcinoma[4][5] adenocarcinoma (pancreatic cancer),[6] colorectal cancer,[7] prostate cancer.[5] and lung cancer.[8] The pancreatic study[6] showed elevated HAAH only in diseased tissue, but not in adjacent normal and inflamed tissue.
Mutations in ASPH cause Traboulsi syndrome.[9]
References
- ↑ "Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase". Gene 150 (2): 395–9. December 1994. doi:10.1016/0378-1119(94)90460-X. PMID 7821814.
- ↑ "cDNA cloning and characterization of human cardiac junctin". Gene 255 (1): 35–42. September 2000. doi:10.1016/S0378-1119(00)00299-7. PMID 10974562.
- ↑ 3.0 3.1 "Entrez Gene: ASPH aspartate beta-hydroxylase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=444.
- ↑ "Overexpression of human aspartyl (asparaginyl) beta-hydroxylase is associated with malignant transformation". Cancer Research 60 (5): 1261–6. March 2000. PMID 10728685.
- ↑ 5.0 5.1 "Monoclonal antibodies against human aspartyl (asparaginyl) beta-hydroxylase developed by DNA immunization". Hybridoma 28 (4): 251–7. August 2009. doi:10.1089/hyb.2009.0017. PMID 19663697.
- ↑ 6.0 6.1 "Human aspartyl (asparaginyl) beta-hydroxylase monoclonal antibodies: potential biomarkers for pancreatic carcinoma". Pancreas 25 (1): 39–44. July 2002. doi:10.1097/00006676-200207000-00010. PMID 12131769.
- ↑ "CC Detect - Serum-Based Diagnostic Test For Colon Cancer Available". http://www.emaxhealth.com/100/18177.html.
- ↑ "New screening techniques show potential for early detection of lung cancer". JAMA 298 (17): 1997. November 2007. doi:10.1001/jama.298.17.1997. PMID 17986689.
- ↑ "Mutations in ASPH cause facial dysmorphism, lens dislocation, anterior-segment abnormalities, and spontaneous filtering blebs, or Traboulsi syndrome". American Journal of Human Genetics 94 (5): 755–9. May 2014. doi:10.1016/j.ajhg.2014.04.002. PMID 24768550.
External links
- Human ASPH genome location and ASPH gene details page in the UCSC Genome Browser.
- Overview of all the structural information available in the PDB for UniProt: Q12797 (Aspartyl/asparaginyl beta-hydroxylase) at the PDBe-KB.
Further reading
- "Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases". Biochemical and Biophysical Research Communications 338 (1): 610–6. December 2005. doi:10.1016/j.bbrc.2005.08.193. PMID 16154531.
- "Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma". The Journal of Clinical Investigation 98 (6): 1313–23. September 1996. doi:10.1172/JCI118918. PMID 8823296.
- "Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane". The Journal of Biological Chemistry 272 (37): 23389–97. September 1997. doi:10.1074/jbc.272.37.23389. PMID 9287354.
- "Molecular cloning of junctin from human and developing rabbit heart". Molecular Genetics and Metabolism 69 (3): 252–8. March 2000. doi:10.1006/mgme.2000.2966. PMID 10767180.
- "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin". The Journal of Biological Chemistry 275 (50): 39543–54. December 2000. doi:10.1074/jbc.M006753200. PMID 10956665.
- "Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane". The Journal of Biological Chemistry 275 (50): 39555–68. December 2000. doi:10.1074/jbc.M005473200. PMID 11007777.
- "Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1". The Journal of Biological Chemistry 276 (6): 4142–9. February 2001. doi:10.1074/jbc.M006443200. PMID 11069905.
- "Role of the aspartyl-asparaginyl-beta-hydroxylase gene in neuroblastoma cell motility". Laboratory Investigation; A Journal of Technical Methods and Pathology 82 (7): 881–91. July 2002. doi:10.1097/01.lab.0000020406.91689.7f. PMID 12118090.
- "Antisense oligonucleotides selectively regulate aspartyl beta-hydroxylase and its truncated protein isoform in vitro but distribute poorly into A549 tumors in vivo". The Journal of Pharmacology and Experimental Therapeutics 302 (2): 795–803. August 2002. doi:10.1124/jpet.302.2.795. PMID 12130746.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America 99 (26): 16899–903. December 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Antisense oligodeoxynucleotides directed against aspartyl (asparaginyl) beta-hydroxylase suppress migration of cholangiocarcinoma cells". Journal of Hepatology 38 (5): 615–22. May 2003. doi:10.1016/S0168-8278(03)00052-7. PMID 12713872.
- "Junctate is a key element in calcium entry induced by activation of InsP3 receptors and/or calcium store depletion". The Journal of Cell Biology 166 (4): 537–48. August 2004. doi:10.1083/jcb.200404079. PMID 15302852.
- "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America 101 (33): 12130–5. August 2004. doi:10.1073/pnas.0404720101. PMID 15302935. Bibcode: 2004PNAS..10112130B.
- "Expression of aspartyl beta-hydroxylase and its clinicopathological significance in hepatocellular carcinoma". Modern Pathology 19 (2): 280–6. February 2006. doi:10.1038/modpathol.3800530. PMID 16341145.
- "Aspartyl-(asparaginyl)-beta-hydroxylase regulates hepatocellular carcinoma invasiveness". Journal of Hepatology 44 (5): 971–83. May 2006. doi:10.1016/j.jhep.2006.01.038. PMID 16564107.
- "Detection of human aspartyl (asparaginyl) beta-hydroxylase and homeobox B7 mRNA in brush cytology specimens from patients with bile duct cancer". Endoscopy 38 (6): 604–9. June 2006. doi:10.1055/s-2006-925065. PMID 16673309.
- "Role of aspartyl-(asparaginyl) beta-hydroxylase in placental implantation: Relevance to early pregnancy loss". Human Pathology 38 (1): 50–9. January 2007. doi:10.1016/j.humpath.2006.06.005. PMID 16949909.
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