CELA1

Chymotrypsin-like elastase family, member 1
Identifiers
Symbols	CELA1 ; ELA1
External IDs	OMIM: 130120 MGI: 95314 HomoloGene: 20454 IUPHAR: 2338 ChEMBL: 3000 GeneCards: CELA1 Gene
EC number	3.4.21.36
Gene ontology Molecular function • serine-type endopeptidase activity • metal ion binding Cellular component • extracellular region Biological process • negative regulation of transcription from RNA polymerase II promoter • proteolysis • inflammatory response • post-embryonic development • Wnt signaling pathway • exocrine pancreas development • multicellular organism growth • regulation of cell proliferation • regulation of cell differentiation • positive regulation of transcription from RNA polymerase II promoter • pancreas morphogenesis Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1990	109901
Ensembl	ENSG00000139610	ENSMUSG00000023031
UniProt	Q9UNI1	Q91X79
RefSeq (mRNA)	NM_001971	NM_033612
RefSeq (protein)	NP_001962	NP_291090
Location (UCSC)	Chr 12: 51.33 – 51.35 Mb	Chr 15: 100.67 – 100.69 Mb
PubMed search

Chymotrypsin-like elastase family member 1 (CELA1) commonly referred to as elastase-1 (ELA1).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. This enzyme has been linked to chronic pancreatitis . A study was done in which the concentration of elastase was measured in patients with chronic pancreattis and those with nonpancreatic digestive diseases. It was concluded that those who had the chronic pancreattis had elastase levels that were below 190 μg/g, (which was the cut off point in making that determination). ^[1]

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. 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).

Further studies have been conducted, which propose a progressive use of Elastase-1 and its role in distinguishing between cystic fibrosis and pancreatic inefficiencies.This was administered by having patients fill out questionnaires and submit stool specimen that were analyzed for fecal elastase-1 (FE-1). From these results it was concluded that those whose FE-1 was >200 μg/g stool and they had never had pancreatitis. The results showed a median of 0 μg/g stool. This data is crucial to prognostication, treatment, and to avoid misclassification in clinical research with those who have cystic fibrosis ^[2]

References

1. Gullo Lucio, Maurizio Ventrucci; et al. (February 2008). "Fecal Elastase 1 Determination in Chronic Pancreatitis". Digestive Diseases and Sciences 44 (1): 210–13. PMID 9952246.
2. Drucy Borowitz R (2005). "Use of fecal elastase-1 to classify pancreatic status in patients with cystic fibrosis". The journal of pediatrics 147 (1): 127. doi:10.1093/hmg/6.6.897. PMID 9175736.

Further reading

• Gullo Lucio, Maurizio Ventrucci; et al. (February 2008). "Fecal Elastase 1 Determination in Chronic Pancreatitis". Digestive Diseases and Sciences 44 (1): 210–13. PMID 9952246.
• Drucy Borowitz (2005). "Use of fecal elastase-1 to classify pancreatic status in patients with cystic fibrosis.". Journal of Pediatrics 147 (1): 127. PMID 6191979.
• Edelstein C, Italia JA, Scanu AM (1997). "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.". J. Biol. Chem. 272 (17): 11079–87. doi:10.1074/jbc.272.17.11079. PMID 9111002.
• Gustavsson EL, Ohlsson K, Olsson AS (1980). "Interaction between human pancreatic elastase and plasma protease inhibitors.". Hoppe-Seyler's Z. Physiol. Chem. 361 (2): 169–76. doi:10.1515/bchm2.1980.361.1.169. PMID 6153632.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Tani T, Kawashima I, Furukawa H; et al. (1987). "Characterization of a silent gene for human pancreatic elastase I: structure of the 5'-flanking region". J. Biochem. 101 (3): 591–9. doi:10.1093/jb/101.3.591. PMID 3648024.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Kawashima I, Tani T, Mita-Honjo K; et al. (1992). "Genomic organization of the human homologue of the rat pancreatic elastase I gene". DNA Seq. 2 (5): 303–12. doi:10.3109/10425179209030963. PMID 1633328.
• Edelstein C, Italia JA, Klezovitch O, Scanu AM (1996). "Functional and metabolic differences between elastase-generated fragments of human lipoprotein[a] and apolipoprotein[a]". J. Lipid Res. 37 (8): 1786–801. PMID 8864963.
• Tsunemi M, Matsuura Y, Sakakibara S, Katsube Y (1996). "Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 A resolution". Biochemistry 35 (36): 11570–6. doi:10.1021/bi960900l. PMID 8794736.

External links

• The MEROPS online database for peptidases and their inhibitors: S01.153

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