CELA3B

Last updated
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
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_007352

NM_026419

RefSeq (protein)

NP_031378

NP_080695

Location (UCSC) Chr 1: 21.98 – 22 Mb Chr 4: 137.15 – 137.16 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]

Contents

Clinical literature that describes human elastase 1 activity in the pancreas or fecal material is actually referring to chymotrypsin-like elastase family member 3B (i.e. the enzyme / protein this article focuses on). [8]

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

<span class="mw-page-title-main">Serine protease</span> Class of enzymes

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.

<span class="mw-page-title-main">Exocrine pancreatic insufficiency</span> Human disease

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.

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

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.

<span class="mw-page-title-main">Bile salt-dependent lipase</span> Mammalian protein found in Homo sapiens

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.

<span class="mw-page-title-main">Trypsin 1</span> Protein-coding gene in the species Homo sapiens

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).

<span class="mw-page-title-main">Azurocidin 1</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">PLA2G1B</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">AMY2A</span> Mammalian protein found in Homo sapiens

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

<span class="mw-page-title-main">CSN2</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">GP2 (gene)</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">CPN1</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">Carboxypeptidase A1</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">PTF1A</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">CELA2A</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">CELA3A</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">CELA1</span> Enzyme-encoding gene in humans

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.

<span class="mw-page-title-main">CELA2B</span> Protein-coding gene in the species Homo sapiens

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

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

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

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000219073 - Ensembl, May 2017
  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.
  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.
  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.
  7. 1 2 "Entrez Gene: ELA3B elastase 3B, pancreatic".
  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

Further reading