Interleukin 16

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Interleukin 16
Protein IL16 PDB 1i16.png
PDB rendering based on 1i16.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols IL16 ; LCF; NIL16; PRIL16; prIL-16
External IDs OMIM603035 MGI1270855 HomoloGene18157 GeneCards: IL16 Gene
RNA expression pattern
PBB GE IL16 209827 s at tn.png
PBB GE IL16 209828 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3603 16170
Ensembl ENSG00000172349 ENSMUSG00000001741
UniProt Q14005 O54824
RefSeq (mRNA) NM_001172128 NM_010551
RefSeq (protein) NP_001165599 NP_034681
Location (UCSC) Chr 15:
81.45 – 81.61 Mb
Chr 7:
83.64 – 83.75 Mb
PubMed search [1] [2]

Pro-interleukin-16 is a protein that in humans is encoded by the IL16 gene.[1][2] This gene was discovered in 1982 at Boston University by Dr. David Center and Dr. William Cruikshank.[3]

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.[2]

Interleukin 16 (IL-16) is a cytokine that 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).[3] Since then, this interleukin has been shown to recruit and activate many other cells expressing the CD4 molecule, including monocytes, eosinophils, and dendritic cells.[4]

The structure of IL-16 was determined following its cloning in 1994.[5] 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. ^ 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 24668. PMID 9144227. 
  2. ^ a b "Entrez Gene: IL16 interleukin 16 (lymphocyte chemoattractant factor)". 
  3. ^ 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. 
  4. ^ Cruikshank WW, Kornfeld H, Center DM (2000). "Interleukin-16". J. Leukoc. Biol. 67 (6): 757–66. PMID 10857846. 
  5. ^ 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 43941. PMID 7910967. 
  6. ^ 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. 
  7. ^ 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.