CELA1

CELA1
Identifiers
Aliases	CELA1, ELA1, chymotrypsin like elastase family member 1
External IDs	MGI: 95314 HomoloGene: 20454 GeneCards: CELA1
Genetically Related Diseases
obesity[1]
Targeted by Drug
telaprevir[2]
Gene ontology Molecular function • metal ion binding • peptidase activity • serine-type peptidase activity • serine-type endopeptidase activity • hydrolase activity Cellular component • extracellular space • extracellular region Biological process • exocrine pancreas development • digestive system development • pancreas morphogenesis • multicellular organism growth • negative regulation of transcription from RNA polymerase II promoter • Wnt signaling pathway • post-embryonic development • proteolysis • positive regulation of angiogenesis • regulation of cell proliferation • regulation of cell differentiation • elastin catabolic process • inflammatory response • tissue remodeling • positive regulation of transcription from RNA polymerase II promoter 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_001962.3	NP_291090.2
Location (UCSC)	Chr 12: 51.33 – 51.35 Mb	Chr 15: 100.67 – 100.69 Mb
PubMed search	[3]	[4]
Wikidata

View/Edit Human

View/Edit Mouse

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 .^[5]

References

1. "Diseases that are genetically associated with CELA1 view/edit references on wikidata".
2. "Drugs that physically interact with Chymotrypsin-like elastase family member 1 view/edit references on wikidata".
3. "Human PubMed Reference:".
4. "Mouse PubMed Reference:".
5. Gullo L, Ventrucci M, Tomassetti P, Migliori M, Pezzilli R (January 1999). "Fecal elastase 1 determination in chronic pancreatitis". Digestive Diseases and Sciences. 44 (1): 210–3. PMID 9952246.

Further reading

• Gullo L, Ventrucci M, Tomassetti P, Migliori M, Pezzilli R (January 1999). "Fecal elastase 1 determination in chronic pancreatitis". Digestive Diseases and Sciences. 44 (1): 210–3. PMID 9952246.
• Borowitz D, Baker SS, Duffy L, Baker RD, Fitzpatrick L, Gyamfi J, Jarembek K (September 2004). "Use of fecal elastase-1 to classify pancreatic status in patients with cystic fibrosis". The Journal of Pediatrics. 145 (3): 322–6. doi:10.1016/j.jpeds.2004.04.049. PMID 15343184.
• Edelstein C, Italia JA, Scanu AM (April 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". The Journal of Biological Chemistry. 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 Zeitschrift Für Physiologische Chemie. 361 (2): 169–76. doi:10.1515/bchm2.1980.361.1.169. PMID 6153632.
• Tani T, Kawashima I, Furukawa H, Ohmine T, Takiguchi Y (March 1987). "Characterization of a silent gene for human pancreatic elastase I: structure of the 5'-flanking region". Journal of Biochemistry. 101 (3): 591–9. doi:10.1093/jb/101.3.591. PMID 3648024.
• Kawashima I, Tani T, Mita-Honjo K, Shimoda-Takano K, Ohmine T, Furukawa H, Takiguchi Y (1992). "Genomic organization of the human homologue of the rat pancreatic elastase I gene". DNA Sequence. 2 (5): 303–12. doi:10.3109/10425179209030963. PMID 1633328.
• Edelstein C, Italia JA, Klezovitch O, Scanu AM (August 1996). "Functional and metabolic differences between elastase-generated fragments of human lipoprotein[a] and apolipoprotein[a]". Journal of Lipid Research. 37 (8): 1786–801. PMID 8864963.
• Tsunemi M, Matsuura Y, Sakakibara S, Katsube Y (September 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.