Cloning and characterization of bovine interleukin-32 beta isoform

Jaekal, Jun; Jhun, Hyunjhung; Hong, Jaewoo; Park, Seung-Young; Lee, Joong‐Bok; Yoon, Do‐Young; Lee, Siyoung; Her, Erk; Yang, Young; Rho, Gyu‐Jin; Kim, Soohyun

doi:10.1016/j.vetimm.2010.04.019

Cited by 7 publications

(9 citation statements)

References 25 publications

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“…Authors demonstrated high polymorphism of the NK4 gene. Sequence analysis revealed that the NK4 -encoded protein had a predicted molecular mass of 27 kDa (12)(13)(14). In addition, it was suggested that the NK4 protein contained ArgGly-Asp (RGD) motif, important in cell adhesion (15).…”

Section: History Of the Il-32mentioning

confidence: 99%

“…In addition, it was suggested that the NK4 protein contained ArgGly-Asp (RGD) motif, important in cell adhesion (15). The NK4 transcript contains a potential signal sequence cleavage site between amino acid 31 and 32, indicating that NK4 can be secreted by the classical secretion pathway (12,13). Nevertheless, for the next 13 years, the biological function of NK4 was not known.…”

Section: History Of the Il-32mentioning

confidence: 99%

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Interleukin-32 in Infection, Inflammation and Cancer Biology

Pavlovic

Jovanović

Arsenijević

2020

Serbian Journal of Experimental and Clinical Research

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Section: History Of the Il-32mentioning

confidence: 99%

Section: History Of the Il-32mentioning

confidence: 99%

Interleukin-32 in Infection, Inflammation and Cancer Biology

Pavlovic

Jovanović

Arsenijević

2020

Serbian Journal of Experimental and Clinical Research

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“…These studies explained the importance of IL-32 role in cell growth by different mechanisms including cell apoptosis. IL-32 genes have been found in most mammals except rodent (15). Mouse IL-32 gene exists in chromosome, but its transcript has not found yet (unpublished data).…”

Section: Il-32 Variants In Different Diseasesmentioning

confidence: 99%

Structural Characteristics of Seven IL-32 Variants

et al. 2019

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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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“…Although proinflammatory activities are key features of IL-32 and are enhanced by the different IL-32 isoforms, which induce the expression of cytokines such as TNF- α [ 3 ], IL-1 β [ 87 ], IL-6 [ 53 ], IL-8 [ 88 ], and COX-2 [ 75 ], the mechanism of IL-32-based signaling remains unknown. The potential signaling pathways of macrophages induced by IL-32 are summarized in Figure 1 .…”

Section: The Function Of Il-32 In the Activation Of Signaling Pathmentioning

confidence: 99%

The Biology and Role of Interleukin-32 in Tuberculosis

Deng

Xie

2018

Journal of Immunology Research

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Tuberculosis, caused by Mycobacterium tuberculosis, remains a leading cause of morbidity and mortality globally, with nearly 10.4 million new cases of incidence and over 1.7 million deaths annually. Drug-resistant M. tuberculosis strains, especially multidrug-resistant or extensively drug-resistant strains, have further intensified the problem associated with tuberculosis control. Host-directed therapy is a promising alternative for tuberculosis control. IL-32 is increasingly recognized as an important host molecule against tuberculosis. In this review, we highlight the proinflammatory properties of IL-32 and the mode of action of IL-32 in mycobacterial infections to inspire the development of novel immunity-based countermeasures and host-directed therapies against tuberculosis.

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Cloning and characterization of bovine interleukin-32 beta isoform

Cited by 7 publications

References 25 publications

Interleukin-32 in Infection, Inflammation and Cancer Biology

Interleukin-32 in Infection, Inflammation and Cancer Biology

Structural Characteristics of Seven IL-32 Variants

The Biology and Role of Interleukin-32 in Tuberculosis

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