Sohn Dong Hyun, Nguyen Tam T, Kim Sinae, Shim Saerok, Lee Siyoung, Lee Youngmin, Jhun Hyunjhung, Azam Tania, Kim Joohee, Kim Soohyun
Department of Microbiology and Immunology, Pusan National University School of Medicine, Yangsan 50612, Korea.
Laboratory of Cytokine Immunology, Department of Biomedical Science and Technology, Konkuk University, Seoul 05029, Korea.
Immune Netw. 2019 Apr 16;19(2):e8. doi: 10.4110/in.2019.19.e8. eCollection 2019 Apr.
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.
白细胞介素-32（IL-32）以七种信使核糖核酸（mRNA）转录本的形式存在，这些转录本可翻译为具有特定蛋白质结构域的不同个体白细胞介素-32变体。白细胞介素-32变体的这些翻译后的蛋白质结构域编码特定功能，使其能够在细胞内或细胞外与不同分子相互作用。最长的变体是IL-32γ，拥有234个氨基酸残基和所有11个蛋白质结构域，而最短的变体是IL-32α，拥有131个氨基酸残基和三个蛋白质结构域。第一个结构域存在于除IL-32δ变体之外的6个变体中，由于mRNA剪接，IL-32δ变体具有独特的翻译起始密码子。最后一个第十一个结构域是所有七种白细胞介素-32变体的共同结构域。尽管缺乏足够的数据，但在炎症、自身免疫、病原体感染和癌症生物学等不同领域的大量研究都声称了单个白细胞介素-32变体的特定生物学活性。还有4种额外的白细胞介素-32变体没有合适的转录本。在这篇综述中，基于特定的蛋白质结构域描述了七种白细胞介素-32转录本的结构特征。
