Pancreatic elastase

Pancreatic elastase
Identifiers
EC no.3.4.21.36
CAS no.848900-32-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Pancreatic elastase II
Identifiers
EC no.3.4.21.71
CAS no.75603-19-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Pancreatic endopeptidase E
Identifiers
EC no.3.4.21.70
CAS no.68073-27-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Although the recommended name is pancreatic elastase, it can also be referred to as elastase-1, pancreatopeptidase, PE, or serine elastase.

The first isozyme, pancreatic elastase 1, was initially thought to be expressed in the pancreas. However it was later discovered that it was the only chymotrypsin-like elastase that was not expressed in the pancreas. In fact, pancreatic elastase is expressed in basal layers of epidermis (at protein level). Hence pancreatic elastase 1 has been renamed elastase 1 (ELA1) or chymotrypsin-like elastase family, member 1 (CELA1).[1] For a period of time, it was thought that ELA1 / CELA1 was not transcribed into a protein.[2] However it was later discovered that it was expressed in skin keratinocytes.[3]

Clinical literature that describes human elastase 1 activity in the pancreas or fecal material is actually referring to chymotrypsin-like elastase family, member 3B (CELA3B).[1]

  1. ^ a b EntrezGene 1990
  2. ^ Rose SD, MacDonald RJ (June 1997). "Evolutionary silencing of the human elastase I gene (ELA1)". Hum. Mol. Genet. 6 (6): 897–903. doi:10.1093/hmg/6.6.897. PMID 9175736.
  3. ^ Talas U, Dunlop J, Khalaf S, Leigh IM, Kelsell DP (January 2000). "Human elastase 1: evidence for expression in the skin and the identification of a frequent frameshift polymorphism". J. Invest. Dermatol. 114 (1): 165–70. doi:10.1046/j.1523-1747.2000.00825.x. PMID 10620133.