Wikipedia

Interleukin 16

Interleukin 16 is a pro-inflammatory pleiotropic cytokine. Its precursor, pro-interleukin-16 is a protein that in humans is encoded by the IL16 gene.[5][6] This gene was discovered in 1982 at Boston University by Dr. David Center and Dr. William Cruikshank.[7]

IL16
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesIL16, LCF, NPRprIL-16, IL-16, interleukin 16
External IDsOMIM: 603035; MGI: 1270855; HomoloGene: 18157; GeneCards: IL16; OMA:IL16 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3603

16170

Ensembl

ENSG00000172349

ENSMUSG00000001741

UniProt

Q14005

O54824

RefSeq (mRNA)

NM_010551
NM_001360087
NM_001360088
NM_001360089

RefSeq (protein)

NP_034681
NP_001347016
NP_001347017
NP_001347018

Location (UCSC)Chr 15: 81.16 – 81.31 MbChr 7: 83.29 – 83.39 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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The cytokine encoded by this gene is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of this cytokine is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. The cytokine function is exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two alternatively spliced transcript variants encoding distinct isoforms have been reported.[6] Interleukin 16 (IL-16) is released by a variety of cells (including lymphocytes and some epithelial cells) that has been characterized as a chemoattractant for certain immune cells expressing the cell surface molecule CD4. IL-16 was originally described as a factor that could attract activated T cells in humans, it was previously called lymphocyte chemoattractant factor (LCF).[7] Since then, this interleukin has been shown to recruit and activate many other cells expressing the CD4 molecule, including monocytes, eosinophils, and dendritic cells.[8]

The structure of IL-16 was determined following its cloning in 1994.[9] This cytokine is produced as a precursor peptide (pro-IL-16) that requires processing by an enzyme called caspase-3 to become active. CD4 is the cell signaling receptor for mature IL-16.

Interactions

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Interleukin 16 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172349 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001741 – 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. ^ Baier M, Bannert N, Werner A, Lang K, Kurth R (May 1997). "Molecular cloning, sequence, expression, and processing of the interleukin 16 precursor". Proceedings of the National Academy of Sciences of the United States of America. 94 (10): 5273–5277. Bibcode:1997PNAS...94.5273B. doi:10.1073/pnas.94.10.5273. PMC 24668. PMID 9144227.
  6. ^ a b "Entrez Gene: IL16 interleukin 16 (lymphocyte chemoattractant factor)".
  7. ^ a b Cruikshank W, Center DM (June 1982). "Modulation of lymphocyte migration by human lymphokines. II. Purification of a lymphotactic factor (LCF)". Journal of Immunology. 128 (6): 2569–2574. doi:10.4049/jimmunol.128.6.2569. PMID 7042841. S2CID 33890529.
  8. ^ Cruikshank WW, Kornfeld H, Center DM (June 2000). "Interleukin-16". Journal of Leukocyte Biology. 67 (6): 757–766. doi:10.1002/jlb.67.6.757. PMID 10857846.
  9. ^ Cruikshank WW, Center DM, Nisar N, Wu M, Natke B, Theodore AC, Kornfeld H (May 1994). "Molecular and functional analysis of a lymphocyte chemoattractant factor: association of biologic function with CD4 expression". Proceedings of the National Academy of Sciences of the United States of America. 91 (11): 5109–5113. Bibcode:1994PNAS...91.5109C. doi:10.1073/pnas.91.11.5109. PMC 43941. PMID 7910967.
  10. ^ a b c d e Kurschner C, Yuzaki M (September 1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". The Journal of Neuroscience. 19 (18): 7770–7780. doi:10.1523/JNEUROSCI.19-18-07770.1999. PMC 6782450. PMID 10479680.
  11. ^ a b Bannert N, Vollhardt K, Asomuddinov B, Haag M, König H, Norley S, Kurth R (October 2003). "PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits". The Journal of Biological Chemistry. 278 (43): 42190–42199. doi:10.1074/jbc.M306669200. PMID 12923170.

Further reading

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  • Overview of all the structural information available in the PDB for UniProt: Q14005 (Interleukin-16) at the PDBe-KB.

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

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