CELA1

CELA1
Identifiers
Aliases	CELA1, ELA1, chymotrypsin like elastase family member 1, chymotrypsin like elastase 1
External IDs	OMIM: 130120; MGI: 95314; HomoloGene: 20454; GeneCards: CELA1; OMA:CELA1 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q13.13 Start 51,328,442 bp End 51,346,679 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15 F1|15 56.38 cM Start 100,572,302 bp End 100,585,802 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle left adrenal gland right adrenal cortex granulocyte left adrenal cortex monocyte gonad stromal cell of endometrium blood lymph node Top expressed in pyloric antrum islet of Langerhans left colon right kidney transitional epithelium of urinary bladder duodenum human kidney lens epithelium of stomach epithelium of lens More reference expression data BioGPS n/a
Gene ontology Molecular function metal ion binding peptidase activity serine-type peptidase activity serine-type endopeptidase activity hydrolase activity Cellular component extracellular region extracellular space Biological process exocrine pancreas development digestive system development pancreas morphogenesis multicellular organism growth negative regulation of transcription by RNA polymerase II Wnt signaling pathway post-embryonic development proteolysis positive regulation of angiogenesis regulation of cell population proliferation regulation of cell differentiation elastin catabolic process inflammatory response tissue remodeling positive regulation of transcription by RNA polymerase II 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: 100.57 – 100.59 Mb PubMed search
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 .

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. doi:10.1023/A:1026691209094. PMID 9952246. S2CID 1137506.
• 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. doi:10.1016/S0022-2275(20)39122-7. 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
• Human CELA1 genome location and CELA1 gene details page in the UCSC Genome Browser.

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