Interleukin 16

From Wikipedia, the free encyclopedia

Interleukin 16 (lymphocyte chemoattractant factor)

PDB rendering based on 1i16.

Available structures: 1i16, 1x6d

Identifiers

Symbol(s)

IL16; FLJ16806; FLJ42735; FLJ44234; HsT19289; IL-16; LCF; prIL-16

External IDs

OMIM: 603035 MGI: 1270855 HomoloGene: 18157

Gene ontology
Molecular Function:	• cytokine activity • protein binding
Cellular Component:	• extracellular space • intracellular
Biological Process:	• immune response • leukocyte chemotaxis • induction of positive chemotaxis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004513 (mRNA)
NP_004504 (protein)

NM_010551 (mRNA)
NP_034681 (protein)

Location

Chr 15: 79.26 - 79.39 Mb

Chr 7: 83.52 - 83.61 Mb

Pubmed search

[1]

[2]

Interleukin 16 (lymphocyte chemoattractant factor), also known as IL16, is a human gene.^[1] This gene was discovered in 1982 at Boston University by Dr. David Center and Dr. William Cruikshank.^[2]

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.^[1]

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).^[2] Since then, this interleukin has been shown to recruit and activate many other cells expressing the CD4 molecule, including monocytes, eosinophils, and dendritic cells.^[3]

The structure of IL-16 was determined following its cloning in 1994.^[4] 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.

[edit] References

^ ^a ^b Entrez Gene: IL16 interleukin 16 (lymphocyte chemoattractant factor).
^ ^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.
^ Cruikshank WW, Kornfeld H, Center DM (2000). "Interleukin-16". J. Leukoc. Biol. 67 (6): 757–66. PMID 10857846.
^ 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. PMID 7910967.

[edit] Further reading

Wilson KC, Center DM, Cruikshank WW (2005). "The effect of interleukin-16 and its precursor on T lymphocyte activation and growth.". Growth Factors 22 (2): 97–104. PMID 15253385.
Copeland KF (2006). "Modulation of HIV-1 transcription by cytokines and chemokines.". Mini reviews in medicinal chemistry 5 (12): 1093–101. PMID 16375755.
Rand TH, Cruikshank WW, Center DM, Weller PF (1991). "CD4-mediated stimulation of human eosinophils: lymphocyte chemoattractant factor and other CD4-binding ligands elicit eosinophil migration.". J. Exp. Med. 173 (6): 1521–8. PMID 1851800.
Ryan TC, Cruikshank WW, Kornfeld H, et al. (1995). "The CD4-associated tyrosine kinase p56lck is required for lymphocyte chemoattractant factor-induced T lymphocyte migration.". J. Biol. Chem. 270 (29): 17081–6. PMID 7615501.
Cruikshank WW, Center DM, Nisar N, et al. (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. PMID 7910967.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Parada NA, Cruikshank WW, Danis HL, et al. (1996). "IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C.". Cell. Immunol. 168 (1): 100–6. doi:10.1006/cimm.1996.0054. PMID 8599832.
Bannert N, Baier M, Werner A, Kurth R (1996). "Interleukin-16 or not?". Nature 381 (6577): 30. doi:10.1038/381030a0. PMID 8609984.
Maciaszek JW, Parada NA, Cruikshank WW, et al. (1997). "IL-16 represses HIV-1 promoter activity.". J. Immunol. 158 (1): 5–8. PMID 8977168.
Baier M, Bannert N, Werner A, et al. (1997). "Molecular cloning, sequence, expression, and processing of the interleukin 16 precursor.". Proc. Natl. Acad. Sci. U.S.A. 94 (10): 5273–7. PMID 9144227.
Laberge S, Ernst P, Ghaffar O, et al. (1997). "Increased expression of interleukin-16 in bronchial mucosa of subjects with atopic asthma.". Am. J. Respir. Cell Mol. Biol. 17 (2): 193–202. PMID 9271307.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Zhang Y, Center DM, Wu DM, et al. (1998). "Processing and activation of pro-interleukin-16 by caspase-3.". J. Biol. Chem. 273 (2): 1144–9. PMID 9422780.
Mühlhahn P, Zweckstetter M, Georgescu J, et al. (1998). "Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site.". Nat. Struct. Biol. 5 (8): 682–6. doi:10.1038/1376. PMID 9699630.
Chupp GL, Wright EA, Wu D, et al. (1998). "Tissue and T cell distribution of precursor and mature IL-16.". J. Immunol. 161 (6): 3114–9. PMID 9743378.
Bannert N, Avots A, Baier M, et al. (1999). "GA-binding protein factors, in concert with the coactivator CREB binding protein/p300, control the induction of the interleukin 16 promoter in T lymphocytes.". Proc. Natl. Acad. Sci. U.S.A. 96 (4): 1541–6. PMID 9990060.
Kim HS (1999). "Assignment of human interleukin 16 (IL16) to chromosome 15q26.3 by radiation hybrid mapping.". Cytogenet. Cell Genet. 84 (1-2): 93. PMID 10343113.
Liu Y, Cruikshank WW, O'Loughlin T, et al. (1999). "Identification of a CD4 domain required for interleukin-16 binding and lymphocyte activation.". J. Biol. Chem. 274 (33): 23387–95. PMID 10438516.
Kaser A, Dunzendorfer S, Offner FA, et al. (1999). "A role for IL-16 in the cross-talk between dendritic cells and T cells.". J. Immunol. 163 (6): 3232–8. PMID 10477592.
Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein.". J. Neurosci. 19 (18): 7770–80. PMID 10479680.

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

v • d • e Cytokines: interleukins

IL-1 superfamily	IL-1 (IL-1Ra) - IL-18 - IL-33

IL-6 like/gp130 utilizing	IL-6 - IL-11 - IL-27 - IL-30 - IL-31 (+non IL Oncostatin M, Leukemia inhibitory factor, Ciliary neurotrophic factor, Cardiotrophin 1)

IL-10 family	IL-10 - IL-19 - IL-20 - IL-22 - IL-24 - IL-26

Interferon type III	IL-28 - IL-29

Common γ-chain family	IL-2/IL-15 - IL-3 - IL-4 - IL-7 - IL-9 - IL-13 - IL-21

IL-12 family	IL-12 - IL-23 - IL-27 - IL-35

Other	IL-5 - IL-8 - IL-14 - IL-16 - IL-17/IL-25 (A) - IL-32