SERPINB1

Last updated
SERPINB1
1HLE.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SERPINB1 , EI, ELANH2, HEL57, LEI, M/NEI, MNEI, PI-2, PI2, HEL-S-27, serpin family B member 1
External IDs OMIM: 130135; MGI: 1913472; HomoloGene: 133768; GeneCards: SERPINB1; OMA:SERPINB1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_030666

NM_025429

RefSeq (protein)

NP_109591

NP_079705

Location (UCSC) Chr 6: 2.83 – 2.84 Mb Chr 13: 33.03 – 33.04 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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 (ovalbumin related serpins) founded by ovalbumin. [5] [6] [7]

Contents

MNEI (monocyte/neutrophil elastase inhibitor) is the mouse orthologue of human SerpinB1. [7]

Function

SerpinB1 is a cytoplasmic serine protease inhibitor of polymorphonuclear neutrophils. Among other serine proteases, it specifically inhibits neutrophil elastase, PR3 and cathepsin G, all found in neutrophil granules, by a suicide inhibition mechanism. SerpinB1 was found to reduce tissue damage caused by the mentioned proteases during inflammation and has a role in neutrophil homeostasis in mice. In various infection models (e.g. pneumonia) correlation of SerpinB1 absence and lack of microbial clearance have been shown. Different knockout strains serve as model to investigate the role of SerpinB1 in vivo. [8] [9] [10]

See also

Related Research Articles

<span class="mw-page-title-main">Alpha-1 antitrypsin</span> Mammalian protein found in Homo sapiens

Alpha-1 antitrypsin or α1-antitrypsin is a protein belonging to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. A protease inhibitor, it is also known as alpha1–proteinase inhibitor (A1PI) or alpha1-antiproteinase (A1AP) because it inhibits various proteases. As a type of enzyme inhibitor, it protects tissues from enzymes of inflammatory cells, especially neutrophil elastase.

<span class="mw-page-title-main">Serpin</span> Superfamily of proteins with similar structures and diverse functions

Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases. They are notable for their unusual mechanism of action, in which they irreversibly inhibit their target protease by undergoing a large conformational change to disrupt the target's active site. This contrasts with the more common competitive mechanism for protease inhibitors that bind to and block access to the protease active site.

<span class="mw-page-title-main">Proteinase 3</span> Mammalian protein found in Homo sapiens

Proteinase 3, also known as PRTN3, is an enzyme that in humans is encoded by the PRTN3 gene.

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

Heparin cofactor II (HCII), a protein encoded by the SERPIND1 gene, is a coagulation factor that inhibits IIa, and is a cofactor for heparin and dermatan sulfate.

<span class="mw-page-title-main">Plasminogen activator inhibitor-2</span> Coagulation factor protein found in humans

Plasminogen activator inhibitor-2, a serine protease inhibitor of the serpin superfamily, is a coagulation factor that inactivates tissue plasminogen activator and urokinase. It is present in most cells, especially monocytes/macrophages. PAI-2 exists in two forms, a 60-kDa extracellular glycosylated form and a 43-kDa intracellular form.

<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">Alpha 1-antichymotrypsin</span> Protein-coding gene in the species Homo sapiens

Alpha 1-antichymotrypsin is an alpha globulin glycoprotein that is a member of the serpin superfamily. In humans, it is encoded by the SERPINA3 gene.

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

Cathepsin G is a protein that in humans is encoded by the CTSG gene. It is one of the three serine proteases of the chymotrypsin family that are stored in the azurophil granules, and also a member of the peptidase S1 protein family. Cathepsin G plays an important role in eliminating intracellular pathogens and breaking down tissues at inflammatory sites, as well as in anti-inflammatory response.

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

Maspin is a protein that in humans is encoded by the SERPINB5 gene. This protein belongs to the serpin superfamily. SERPINB5 was originally reported to function as a tumor suppressor gene in epithelial cells, suppressing the ability of cancer cells to invade and metastasize to other tissues. Furthermore, and consistent with an important biological function, Maspin knockout mice were reported to be non-viable, dying in early embryogenesis. However, a subsequent study using viral transduction as a method of gene transfer was not able to reproduce the original findings and found no role for maspin in tumour biology. Furthermore, the latter study demonstrated that maspin knockout mice are viable and display no obvious phenotype. These data are consistent with the observation that maspin is not expressed in early embryogenesis. The precise molecular function of maspin is thus currently unknown.

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

Elafin, also known as peptidase inhibitor 3 or skin-derived antileukoprotease (SKALP), is a protein that in humans is encoded by the PI3 gene.

<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">SERPINB9</span> Protein-coding gene in the species Homo sapiens

Serpin B9 is a protein that in humans is encoded by the SERPINB9 gene. PI9 belongs to the large superfamily of serine proteinase inhibitors (serpins), which bind to and inactivate serine proteinases. These interactions are involved in many cellular processes, including coagulation, fibrinolysis, complement fixation, matrix remodeling, and apoptosis .[supplied by OMIM]

<span class="mw-page-title-main">SERPINE2</span> Protein-coding gene in the species Homo sapiens

Glia-derived nexin is a protein that in humans is encoded by the SERPINE2 gene.

<span class="mw-page-title-main">SERPINB4</span> Protein-coding gene in the species Homo sapiens

Serpin B4 is a protein that in humans is encoded by the SERPINB4 gene.

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

Lympho-epithelial Kazal-type-related inhibitor (LEKTI) also known as serine protease inhibitor Kazal-type 5 (SPINK5) is a protein that in humans is encoded by the SPINK5 gene.

<span class="mw-page-title-main">SERPINB6</span> Protein-coding gene in the species Homo sapiens

Serpin B6 is a protein that in humans is encoded by the SERPINB6 gene.

<span class="mw-page-title-main">SERPINB13</span> Gene of the species Homo sapiens

Serpin B13 is a protein that in humans is encoded by the SERPINB13 gene.

<span class="mw-page-title-main">SERPINB8</span> Protein-coding gene in the species Homo sapiens

Serpin B8 is a protein that in humans is encoded by the SERPINB8 gene.

<span class="mw-page-title-main">SERPINA9</span> Protein-coding gene in the species Homo sapiens

Serpin A9 also known as centerin or GCET1 is a protein that in humans is encoded by the SERPINA9 gene located on chromosome 14q32.1. Serpin A9 is a member of the serpin family of serine protease inhibitors.

<span class="mw-page-title-main">SERPINB10</span> Protein-coding gene in the species Homo sapiens

Serpin peptidase inhibitor, clade B (ovalbumin), member 10 is a protein that in humans is encoded by the SERPINB10 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000021355 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000044734 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. Remold-O'Donnell E, Chin J, Alberts M (Jul 1992). "Sequence and molecular characterization of human monocyte/neutrophil elastase inhibitor". Proc Natl Acad Sci U S A. 89 (12): 5635–9. Bibcode:1992PNAS...89.5635R. doi: 10.1073/pnas.89.12.5635 . PMC   49347 . PMID   1376927.
  6. "Entrez Gene: SERPINB1 serpin peptidase inhibitor, clade B (ovalbumin), member 1".
  7. 1 2 Benarafa C, Remold-O'Donnell E (August 2005). "The ovalbumin serpins revisited: perspective from the chicken genome of clade B serpin evolution in vertebrates". Proc. Natl. Acad. Sci. U.S.A. 102 (32): 11367–72. Bibcode:2005PNAS..10211367B. doi: 10.1073/pnas.0502934102 . PMC   1183561 . PMID   16055559.
  8. Gong D, Farley K, White M, Hartshorn KL, Benarafa C, Remold-O'Donnell E (August 2011). "Critical role of serpinB1 in regulating inflammatory responses in pulmonary influenza infection". J. Infect. Dis. 204 (4): 592–600. doi:10.1093/infdis/jir352. PMC   3144176 . PMID   21791661.
  9. Benarafa C, LeCuyer TE, Baumann M, Stolley JM, Cremona TP, Remold-O'Donnell E (July 2011). "SerpinB1 protects the mature neutrophil reserve in the bone marrow". J. Leukoc. Biol. 90 (1): 21–9. doi:10.1189/jlb.0810461. PMC   3114599 . PMID   21248149.
  10. Benarafa C, Priebe GP, Remold-O'Donnell E (August 2007). "The neutrophil serine protease inhibitor serpinb1 preserves lung defense functions in Pseudomonas aeruginosa infection". J. Exp. Med. 204 (8): 1901–9. doi:10.1084/jem.20070494. PMC   2118684 . PMID   17664292.

Further reading

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