Interleukin 16 is a
pro-inflammatory pleiotropic
cytokine. Its precursor, pro-interleukin-16 is a
protein that in humans is encoded by the IL16gene.[5][6] This gene was discovered in 1982 at
Boston University by Dr. David Center and Dr. William Cruikshank.[7]
Function
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-terminalpeptide, 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 signalingreceptor for mature IL-16.
Wilson KC, Center DM, Cruikshank WW (June 2004). "The effect of interleukin-16 and its precursor on T lymphocyte activation and growth". Growth Factors. 22 (2): 97–104.
doi:
10.1080/08977190410001704679.
PMID15253385.
S2CID16860935.
Copeland KF (December 2005). "Modulation of HIV-1 transcription by cytokines and chemokines". Mini Reviews in Medicinal Chemistry. 5 (12): 1093–1101.
doi:
10.2174/138955705774933383.
PMID16375755.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Maciaszek JW, Parada NA, Cruikshank WW, Center DM, Kornfeld H, Viglianti GA (January 1997). "IL-16 represses HIV-1 promoter activity". Journal of Immunology. 158 (1): 5–8.
doi:
10.4049/jimmunol.158.1.5.
PMID8977168.
S2CID28041095.
Laberge S, Ernst P, Ghaffar O, Cruikshank WW, Kornfeld H, Center DM, Hamid Q (August 1997). "Increased expression of interleukin-16 in bronchial mucosa of subjects with atopic asthma". American Journal of Respiratory Cell and Molecular Biology. 17 (2): 193–202.
CiteSeerX10.1.1.319.2157.
doi:
10.1165/ajrcmb.17.2.2750.
PMID9271307.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Kim HS (1999). "Assignment of human interleukin 16 (IL16) to chromosome 15q26.3 by radiation hybrid mapping". Cytogenetics and Cell Genetics. 84 (1–2): 93.
doi:
10.1159/000015224.
PMID10343113.
S2CID83880527.