CELA3B

CELA3B
Identifiers
Aliases	CELA3B , CBPP, E1, EL-1, ELA3B, chymotrypsin like elastase family member 3B, chymotrypsin like elastase 3B
External IDs	MGI: 1915118 HomoloGene: 128227 GeneCards: CELA3B
Gene location (Human)
Chr.	Chromosome 1 (human)
End	21,998,642 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	137,157,851 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; islet of Langerhans; ; body of stomach; ; fundus; ; duodenum; ; right coronary artery; ; right lobe of liver; ; placenta; ; left uterine tube; ; canal of the cervix;
	Top expressed in
	pyloric antrum; ; islet of Langerhans; ; duodenum; ; sexually immature organism; ; morula; ; esophagus; ; brown adipose tissue; ; gastric mucosa; ; mucous cell of stomach; ; large intestine;
	More reference expression data
	n/a
Gene ontology
Molecular function	peptidase activity ; serine-type peptidase activity ; hydrolase activity ; serine-type endopeptidase activity ;
Cellular component	extracellular space ;
Biological process	proteolysis ;
	Sources:Amigo / QuickGO
Orthologs
	23436
	67868
	ENSG00000219073
	ENSMUSG00000023433
	P08861
	Q9CQ52
	NM_007352
	NM_026419
	NP_031378
	NP_080695
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 19, 2023

Chymotrypsin-like elastase family member 3B also known as elastase-3B, protease E, or fecal elastase is an enzyme that in humans is encoded by the CELA3B gene.^[5]^[6]^[7]

Function

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. Unlike other elastases, elastase 3B has little elastolytic activity. Like most of the human elastases, elastase 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after alanine residues. Elastase 3B may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1, and excretion of this protein in fecal material is frequently used as a measure of pancreatic function in clinical assays.^[7]

Clinical significance

Fecal elastase is a medical test that measures how well the pancreas is functioning.

The fecal elastase test measures the concentration of the elastase-3B enzyme found in fecal matter with an enzyme-linked immunosorbent assay (ELISA). Results of this test can give a good indication of exocrine pancreatic status, and the test is less invasive and expensive than the current "gold standard", secretin-cholecystokinin test.^[9] Levels of fecal elastase lower than 200 μg / g of stool indicate an exocrine insufficiency. Correlations between low levels and chronic pancreatitis^[10] and cancer^{[ citation needed ]} have been reported.

Related Research Articles

Serine proteases are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.

Exocrine pancreatic insufficiency (EPI) is the inability to properly digest food due to a lack or reduction of digestive enzymes made by the pancreas. EPI can occur in humans and is prevalent in many conditions such as cystic fibrosis, Shwachman–Diamond syndrome, different types of pancreatitis, multiple types of diabetes mellitus, advanced renal disease, older adults, celiac disease, IBS-D, IBD, HIV, alcohol-related liver disease, Sjogren syndrome, tobacco use, and use of somatostatin analogues.

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.

Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Neutrophil elastase is secreted by neutrophils during inflammation, and destroys bacteria and host tissue. It also localizes to neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases.

Bile salt-dependent lipase, also known as carboxyl ester lipase is an enzyme produced by the adult pancreas and aids in the digestion of fats. Bile salt-stimulated lipase is an equivalent enzyme found within breast milk. BSDL has been found in the pancreatic secretions of all species in which it has been looked for. BSSL, originally discovered in the milk of humans and various other primates, has since been found in the milk of many animals including dogs, cats, rats, and rabbits.

Trypsin-1, also known as cationic trypsinogen, is a protein that in humans is encoded by the PRSS1 gene. Trypsin-1 is the main isoform of trypsinogen secreted by pancreas, the others are trypsin-2, and trypsin-3 (meso-trypsinogen).

Azurocidin also known as cationic antimicrobial protein CAP37 or heparin-binding protein (HBP) is a protein that in humans is encoded by the AZU1 gene.

Phospholipase A2, group 1B is an enzyme that in humans is encoded by the PLA2G1B gene.

Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene.

Beta-casein is a protein that in humans is encoded by the CSN2 gene. It is in the class of phosphoproteins and generally occurs in mammalian milk.

<span class="mw-page-title-main">SERPINB1</span> Protein-coding gene in the species Homo sapiens

Leukocyte elastase inhibitor (LEI) also known as serpin B1 is a protein that in humans is encoded by the SERPINB1 gene. It is a member of the clade B serpins or ov-serpins founded by ovalbumin.

Pancreatic secretory granule membrane major glycoprotein GP2 is a protein that in humans is encoded by the GP2 gene.

Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene.

Carboxypeptidase A1 is an enzyme that in humans is encoded by the CPA1 gene.

Pancreas transcription factor 1 subunit alpha is a protein that in humans is encoded by the PTF1A gene.

Chymotrypsin-like elastase family member 2A is an enzyme that in humans is encoded by the CELA2A gene.

Chymotrypsin-like elastase family member 3A is an enzyme that in humans is encoded by the CELA3A gene.

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.

Chymotrypsin-like elastase family member 2B is and enzyme that in humans is encoded by the CELA2B gene.

Chymotrypsin C, also known as caldecrin or elastase 4, is an enzyme that in humans is encoded by the CTRC gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000219073 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000023433 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Tani T, Ohsumi J, Mita K, Takiguchi Y (Feb 1988). "Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic gene cloning". J Biol Chem. 263 (3): 1231–9. doi: 10.1016/S0021-9258(19)57291-X . PMID 2826474.
↑ Shirasu Y, Takemura K, Yoshida H, Sato Y, Iijima H, Shimada Y, Mikayama T, Ozawa T, Ikeda N, Ishida A, et al. (Dec 1988). "Molecular cloning of complementary DNA encoding one of the human pancreatic protease E isozymes". J Biochem. 104 (2): 259–64. doi: 10.1093/oxfordjournals.jbchem.a122454 . PMID 2460440.
1 2 "Entrez Gene: ELA3B elastase 3B, pancreatic".
↑ "Entrez Gene: chymotrypsin-like elastase family, member 1".
↑ Molinari I.; et al. (September 2004). "Fecal chymotrypsin and elastase-1 determination on one single stool collected at random: diagnostic value for exocrine pancreatic status". Clin Biochem. 37 (9): 758–763. doi:10.1016/j.clinbiochem.2004.03.010. PMID 15329313.
↑ Fecal Elastase 1 ELISA For Exocrine Pancreatic Insufficiency: Comparison With ERCP-Morphology And Fecal Fat Excretion Archived 2007-09-27 at the Wayback Machine

External links

Human CELA3B genome location and CELA3B gene details page in the UCSC Genome Browser .

Avilés FX, Pascual R, Salva M, et al. (1989). "Generation of a subunit III-like protein by autolysis of human and porcine proproteinase e in a binary complex with procarboxypeptidase A.". Biochem. Biophys. Res. Commun. 163 (3): 1191–6. doi:10.1016/0006-291X(89)91104-2. PMID 2675835.
Wendorf P, Geyer R, Sziegoleit A, Linder D (1989). "Localization and characterization of the glycosylation site of human pancreatic elastase 1". FEBS Lett. 249 (2): 275–8. doi:10.1016/0014-5793(89)80640-4. PMID 2737288.
Moulard M, Kerfelec B, Mallet B, Chapus C (1989). "Identification of a procarboxypeptidase A-truncated protease E binary complex in human pancreatic juice". FEBS Lett. 250 (2): 166–70. doi: 10.1016/0014-5793(89)80712-4 . PMID 2753124.
Guy-Crotte O, Barthe C, Basso D, et al. (1988). "Characterization of two glycoproteins of human pancreatic juice: P35, a truncated protease E and P19, precursor of protein X.". Biochem. Biophys. Res. Commun. 156 (1): 318–22. doi:10.1016/S0006-291X(88)80842-8. PMID 3178837.
Shen WF, Fletcher TS, Largman C (1987). "Primary structure of human pancreatic protease E determined by sequence analysis of the cloned mRNA". Biochemistry. 26 (12): 3447–52. doi:10.1021/bi00386a030. PMID 3477287.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID 14702039.
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.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi: 10.1038/nature04727 . PMID 16710414.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000219073 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000023433 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2826474-5] Tani T, Ohsumi J, Mita K, Takiguchi Y (Feb 1988). "Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic gene cloning". J Biol Chem. 263 (3): 1231–9. doi: 10.1016/S0021-9258(19)57291-X . PMID 2826474.

[pmid2460440-6] Shirasu Y, Takemura K, Yoshida H, Sato Y, Iijima H, Shimada Y, Mikayama T, Ozawa T, Ikeda N, Ishida A, et al. (Dec 1988). "Molecular cloning of complementary DNA encoding one of the human pancreatic protease E isozymes". J Biochem. 104 (2): 259–64. doi: 10.1093/oxfordjournals.jbchem.a122454 . PMID 2460440.

[entrez-7] 1 2 "Entrez Gene: ELA3B elastase 3B, pancreatic".

[entrez2-8] "Entrez Gene: chymotrypsin-like elastase family, member 1".

[9] Molinari I.; et al. (September 2004). "Fecal chymotrypsin and elastase-1 determination on one single stool collected at random: diagnostic value for exocrine pancreatic status". Clin Biochem. 37 (9): 758–763. doi:10.1016/j.clinbiochem.2004.03.010. PMID 15329313.

[10] Fecal Elastase 1 ELISA For Exocrine Pancreatic Insufficiency: Comparison With ERCP-Morphology And Fecal Fat Excretion Archived 2007-09-27 at the Wayback Machine

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v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)