User:Kacinska/Interleukin 16

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An Error has occurred retrieving Wikidata item for infoboxInterleukin 16 is a pro-inflammatory pleiotropic cytokine. It's precursor, 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 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.[2]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).[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.

The CD4 molecule is its primary receptor, although the chemokine receptor CCR5 enhances IL-16 binding. IL-16 is chemotactic for T cells, eosinophils, mast cells, and monocytes. Among the CD4+ T cells subsets, IL-16 preferentially induces migration of Th1 and Foxp3+ regulatory T lymphocytes (Tregs). In addition, IL-16 promotes Th1 and inhibits Th2 responses through CD3/T cell receptor mediated modulation of cytokine activity, possibly contributing against Th2-cell mediated diseases such as allergic asthma.[6]

Interactions[edit]

Interleukin 16 has been shown to interact with:

Gene structure and expression[edit]

Interleukin-16 (IL-16) is located on chromosome 15q26.1–q26.3 in humans and on chromosome 7 D2–D3 in mice. The IL-16 gene contains seven exons and six introns and encodes a large precursor protein, pro-IL-16, which is enzymatically processed to generate mature (secreted) IL-16 from the C-terminal of pro-IL-16. The gene is highly conservative, there is high gene sequence homology for both pro-IL-16 and mature IL-16 when the human is compared with mouse, rat, feline, or simian, greater than 84% for all species. The IL-16 promoter contains two CAAT-box-like motifs and multiple binding sites for GA-binding protein (GABP) and GATA-1, GATA-2, and GATA-3 transcription factors. Two of the motifs constitute a dyad symmetry element that complexes with GABPa and GABPb. Activation then occurs when the co-activator, CREB-binding protein/p300 (where CREB is Ca2þ/cAMP-response element-binding protein), binds to GABPa and induces the IL-16 gene promoter. The promoter lacks a TATA-box.[9]

The IL-16 m RNA is constitutively expressed at high levels. Under nondisease conditions, IL-16 mRNA is limited almost exclusively to lymphatic tissue and circulating immune cells such as CD4 + and CD8 + T cells, eosinophils, mast cells, and dendritic cells, but synthesis is not restricted to these cell types only.[9] Nonimmune cells must be induced to transcribe IL-16 message. During an inflammatory response, in situ IL-16 mRNA is also detected in other cell types, such as bronchial epithelial cells and fibroblasts [10][11].

Interaction with HIV[edit]

IL-16 has been shown to strongly suppress HIV-1 LTR-mediated transcription in T cells, monocytic cells and dendritic cells [12]. IL-16 improves macrophage phagocytosis ability with the down-expression of IL-10 and up-expression of pro-inflammatory cytokines such as IL-1a and IL-6, hence increases the antimicrobial effect and inhibits HIV replication in macrophages. [13]

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. Bibcode:1997PNAS...94.5273B. 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. doi:10.1002/jlb.67.6.757. 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. Bibcode:1994PNAS...91.5109C. doi:10.1073/pnas.91.11.5109. PMC 43941. PMID 7910967.
  6. ^ Steinke, John W.; Rosenwasser, Lanny J.; Borish, Larry (2014-01-01), Adkinson, N. Franklin; Bochner, Bruce S.; Burks, A. Wesley; Busse, William W. (eds.), "5 - Cytokines in Allergic Inflammation", Middleton's Allergy (Eighth Edition), London: W.B. Saunders, pp. 65–82, ISBN 978-0-323-08593-9, retrieved 2022-09-07
  7. ^ 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. doi:10.1523/JNEUROSCI.19-18-07770.1999. PMC 6782450. PMID 10479680.
  8. ^ 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.
  9. ^ a b Wilson, Kevin; Zhang, Yujun; Kornfeld, Hardy; Center, David; Cruikshank, William (2003-01-01), Henry, Helen L.; Norman, Anthony W. (eds.), "Interleukin-16", Encyclopedia of Hormones, New York: Academic Press, pp. 484–493, ISBN 978-0-12-341103-7, retrieved 2022-09-06
  10. ^ Rumsaeng, V.; Cruikshank, W. W.; Foster, B.; Prussin, C.; Kirshenbaum, A. S.; Davis, T. A.; Kornfeld, H.; Center, D. M.; Metcalfe, D. D. (1997-09-15). "Human mast cells produce the CD4+ T lymphocyte chemoattractant factor, IL-16". Journal of Immunology (Baltimore, Md.: 1950). 159 (6): 2904–2910. ISSN 0022-1767. PMID 9300714.
  11. ^ Lim, K. G.; Wan, H. C.; Bozza, P. T.; Resnick, M. B.; Wong, D. T.; Cruikshank, W. W.; Kornfeld, H.; Center, D. M.; Weller, P. F. (1996-04-01). "Human eosinophils elaborate the lymphocyte chemoattractants. IL-16 (lymphocyte chemoattractant factor) and RANTES". Journal of Immunology (Baltimore, Md.: 1950). 156 (7): 2566–2570. ISSN 0022-1767. PMID 8786320.
  12. ^ Zhou, P.; Goldstein, S.; Devadas, K.; Tewari, D.; Notkins, A. L. (1997-06). "Human CD4+ cells transfected with IL-16 cDNA are resistant to HIV-1 infection: inhibition of mRNA expression". Nature Medicine. 3 (6): 659–664. doi:10.1038/nm0697-659. ISSN 1078-8956. PMID 9176493. {{cite journal}}: Check date values in: |date= (help)
  13. ^ Huang, Ying; Du, Kai Li; Guo, Pei Yu; Zhao, Run Min; Wang, Bing; Zhao, Xue Lin; Zhang, Chun Qiang (2019-03). "IL-16 regulates macrophage polarization as a target gene of mir-145-3p". Molecular Immunology. 107: 1–9. doi:10.1016/j.molimm.2018.12.027. ISSN 1872-9142. PMID 30634164. {{cite journal}}: Check date values in: |date= (help)

Further reading[edit]

External links[edit]

  • 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.


Category:Interleukins

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