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KMID : 0923620190190020008
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Immune Network
2019 Volume.19 No. 2 p.8 ~ p.8
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Structural Characteristics of Seven IL-32 Variants
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Sohn Dong-Hyun
Nguyen Tam T.
Kim Sin-Ae
Shim Sae-Rok
Lee Si-Young
Lee Young-Min
Jhun Hyun-Jhung
Azam Tania
Kim Joo-Hee
Kim Soo-Hyun
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Abstract
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IL-32 exists as seven mRNA transcripts that can translate into distinct individual IL-32 variants with specific protein domains. These translated protein domains of IL-32 variants code for specific functions that allow for interaction with different molecules intracellularly or extracellularly. The longest variant is IL-32γ possessing 234 amino acid residues with all 11 protein domains, while the shortest variant is IL-32α possessing 131 amino acid residues with three of the protein domains. The first domain exists in 6 variants except IL-32δ variant, which has a distinct translation initiation codon due to mRNA splicing. The last eleventh domain is common domain for all seven IL-32 variants. Numerous studies in different fields, such as inflammation, autoimmunity, pathogen infection, and cancer biology, have claimed the specific biological activity of individual IL-32 variant despite the absence of sufficient data. There are 4 additional IL-32 variants without proper transcripts. In this review, the structural characteristics of seven IL-32 transcripts are described based on the specific protein domains.
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KEYWORD
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IL-32, Variants, mRNA transcript, Protein domains, mRNA splicing
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