Structural Characteristics of Seven IL-32 Variants
- Author:
Dong Hyun SOHN
1
;
Tam T NGUYEN
;
Sinae KIM
;
Saerok SHIM
;
Siyoung LEE
;
Youngmin LEE
;
Hyunjhung JHUN
;
Tania AZAM
;
Joohee KIM
;
Soohyun KIM
Author Information
- Publication Type:Review
- Keywords: IL-32; Variants; mRNA transcript; Protein domains; mRNA splicing
- MeSH: Autoimmunity; Biology; Codon, Initiator; Inflammation; Protein Structure, Tertiary; RNA, Messenger
- From:Immune Network 2019;19(2):e8-
- CountryRepublic of Korea
- Language:English
- 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.
