Biology:CELA1

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Short description: Enzyme-encoding gene in humans


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

Chymotrypsin-like elastase family member 1 (CELA1) also known as elastase-1 (ELA1) is an enzyme that in humans is encoded by the CELA1 gene. Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B.

Tissue distribution

Elastase-1 was formerly designated pancreatic elastase 1. However unlike other elastases, pancreatic elastase 1 is not expressed in the pancreas. Hence this enzyme has been renamed as elastase-1. To date, elastase 1 expression has only been detected in skin keratinocytes. Literature that describes human elastase 1 activity in the pancreas or fecal material is actually referring to chymotrypsin-like elastase family, member 3B CELA3B).

Clinical significance

This enzyme has been linked to chronic pancreatitis .[1]

References

  1. "Fecal elastase 1 determination in chronic pancreatitis". Digestive Diseases and Sciences 44 (1): 210–3. January 1999. doi:10.1023/A:1026691209094. PMID 9952246. 

Further reading

  • "Fecal elastase 1 determination in chronic pancreatitis". Digestive Diseases and Sciences 44 (1): 210–3. January 1999. doi:10.1023/A:1026691209094. PMID 9952246. 
  • "Use of fecal elastase-1 to classify pancreatic status in patients with cystic fibrosis". The Journal of Pediatrics 145 (3): 322–6. September 2004. doi:10.1016/j.jpeds.2004.04.049. PMID 15343184. 
  • "Polymorphonuclear cells isolated from human peripheral blood cleave lipoprotein(a) and apolipoprotein(a) at multiple interkringle sites via the enzyme elastase. Generation of mini-Lp(a) particles and apo(a) fragments". The Journal of Biological Chemistry 272 (17): 11079–87. April 1997. doi:10.1074/jbc.272.17.11079. PMID 9111002. 
  • "Interaction between human pancreatic elastase and plasma protease inhibitors". Hoppe-Seyler's Zeitschrift für Physiologische Chemie 361 (2): 169–76. 1980. doi:10.1515/bchm2.1980.361.1.169. PMID 6153632. 
  • "Characterization of a silent gene for human pancreatic elastase I: structure of the 5'-flanking region". Journal of Biochemistry 101 (3): 591–9. March 1987. doi:10.1093/jb/101.3.591. PMID 3648024. 
  • "Genomic organization of the human homologue of the rat pancreatic elastase I gene". DNA Sequence 2 (5): 303–12. 1992. doi:10.3109/10425179209030963. PMID 1633328. 
  • "Functional and metabolic differences between elastase-generated fragments of human lipoprotein[a] and apolipoprotein[a]". Journal of Lipid Research 37 (8): 1786–801. August 1996. doi:10.1016/S0022-2275(20)39122-7. PMID 8864963. 
  • "Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 A resolution". Biochemistry 35 (36): 11570–6. September 1996. doi:10.1021/bi960900l. PMID 8794736. 

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.