Immune Netw.
2019 Apr;19(2):e8. 10.4110/in.2019.19.e8.
Structural Characteristics of Seven IL-32 Variants
- Affiliations
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- 1Department of Microbiology and Immunology, Pusan National University School of Medicine, Yangsan 50612, Korea.
- 2Laboratory of Cytokine Immunology, Department of Biomedical Science and Technology, Konkuk University, Seoul 05029, Korea. soohyun@konkuk.ac.kr, joohee4085@naver.com
- 3College of Veterinary Medicine, Konkuk University, Seoul 05029, Korea.
- 4YbdYbiotech Research Center, Seoul 08589, Korea.
- 5Department of Medicine, Pusan Paik Hospital, Collage of Medicine, Inje University, Busan 47392, Korea.
- 6Technical Assistance Center, Korea Food Research Institute, Wanju 55365, Korea.
- 7Department of Clinical Pathology, Kyungdong University Medical Campus, Wonju 24695, Korea.
- 8Veterinary Science Research Institute, Konkuk University, Seoul 05029, Korea.
- KMID: 2444156
- DOI: http://doi.org/10.4110/in.2019.19.e8
Abstract
- 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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