Interleukin 16

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IL16
Protein IL16 PDB 1i16.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases IL16, LCF, NPRprIL-16, IL-16, interleukin 16
External IDs OMIM: 603035 MGI: 1270855 HomoloGene: 18157 GeneCards: IL16
Gene location (Human)
Chromosome 15 (human)
Chr. Chromosome 15 (human)[1]
Chromosome 15 (human)
Genomic location for IL16
Genomic location for IL16
Band 15q25.1 Start 81,159,575 bp[1]
End 81,314,058 bp[1]
RNA expression pattern
PBB GE IL16 209827 s at fs.png

PBB GE IL16 209828 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_010551

RefSeq (protein)

NP_034681

Location (UCSC) Chr 15: 81.16 – 81.31 Mb Chr 15: 83.64 – 83.75 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]

Function[edit]

The protein 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 a cytokine that 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[edit]

Interleukin 16 has been shown to interact with:

References[edit]

  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:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Baier M, Bannert N, Werner A, Lang K, Kurth R (Jun 1997). "Molecular cloning, sequence, expression, and processing of the interleukin 16 precursor". Proc Natl Acad Sci U S A. 94 (10): 5273–7. doi:10.1073/pnas.94.10.5273. PMC 24668Freely accessible. PMID 9144227. 
  6. ^ a b "Entrez Gene: IL16 interleukin 16 (lymphocyte chemoattractant factor)". 
  7. ^ a b Cruikshank W, Center DM (1982). "Modulation of lymphocyte migration by human lymphokines. II. Purification of a lymphotactic factor (LCF)". J. Immunol. 128 (6): 2569–74. PMID 7042841. 
  8. ^ Cruikshank WW, Kornfeld H, Center DM (2000). "Interleukin-16". J. Leukoc. Biol. 67 (6): 757–66. PMID 10857846. 
  9. ^ Cruikshank WW, Center DM, Nisar N, Wu M, Natke B, Theodore AC, Kornfeld H (1994). "Molecular and functional analysis of a lymphocyte chemoattractant factor: association of biologic function with CD4 expression". Proc. Natl. Acad. Sci. U.S.A. 91 (11): 5109–13. doi:10.1073/pnas.91.11.5109. PMC 43941Freely accessible. PMID 7910967. 
  10. ^ a b c d e Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". J. Neurosci. 19 (18): 7770–80. PMID 10479680. 
  11. ^ a b Bannert N, Vollhardt K, Asomuddinov B, Haag M, König H, Norley S, Kurth R (2003). "PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits". J. Biol. Chem. 278 (43): 42190–9. doi:10.1074/jbc.M306669200. PMID 12923170. 

Further reading[edit]

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