Interleukin 16 is apro-inflammatory pleiotropiccytokine. Its precursor, pro-interleukin-16 is aprotein that in humans is encoded by theIL16gene.[5][6] This gene was discovered in 1982 atBoston University by Dr. David Center and Dr. William Cruikshank.[7]
The cytokine encoded by this gene is a pleiotropic cytokine that functions as a chemoattractant, a modulator ofT cell activation, and an inhibitor ofHIV replication. The signaling process of this cytokine is mediated byCD4. The product of this gene undergoesproteolytic processing, which is found to yield two functional proteins. The cytokine function is exclusively attributed to the secretedC-terminalpeptide, while theN-terminal product may play a role incell cycle control.Caspase 3 is reported to be involved in the proteolytic processing of this protein. Twoalternatively spliced transcript variants encoding distinctisoforms have been reported.[6] Interleukin 16 (IL-16) is released by a variety of cells (includinglymphocytes and someepithelial cells) that has been characterized as achemoattractant for certain immune cells expressing the cell surface moleculeCD4. IL-16 was originally described as a factor that could attract activatedT 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, includingmonocytes,eosinophils, anddendritic cells.[8]
The structure of IL-16 was determined following itscloning in 1994.[9] This cytokine is produced as a precursor peptide (pro-IL-16) that requires processing by anenzyme calledcaspase-3 to become active. CD4 is thecell signalingreceptor for mature IL-16.
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