T lymphocytes constitutively produce an interferonlike cytokine limitin characterized as a heat- and acid-stable and heparin-binding glycoprotein

Oritani, Kenji; Hirota, Seiichi; Nakagawa, Taishirou; Takahashi, Isao; Kawamoto, Shin-ichiro; Yamada, Masahide; Ishida, Naoko; Kadoya, Toshihiko; Tomiyama, Yoshiaki; Kincade, Paul W.; Matsuzawa, Yūji

doi:10.1182/blood-2002-01-0045

Cited by 19 publications

(12 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The deduced protein is composed of 182 amino acid residues, which contain a signal peptide of 21 amino acids at the N-terminal end and a N-linked glycosylation site at the amino acid residue 68. The cleavage site of the signal peptide was confirmed by N-terminal amino acid sequencing, and the N-linked glycosylation was confirmed by the fact that treatment of IFN-ζ/limitin protein with N-glycosydase F changed its mobility in SDS-PAGE [4]. A computer modeling based on the refined crystal structure of IFNs has suggested that IFN-ζ/limitin shows a globular structure with five α-helices (A-E) and four loops and that there are two disulfide bonds between cysteine residues 52 and 157 and between cysteine residues 80 and 130 (Fig.…”

Section: Ifn-ζ/limitinmentioning

confidence: 89%

IFN-? limitin: a member of type I IFN with mild lympho-myelosuppression

Oritani

Kanakura

2005

J Cellular Mol Med

Self Cite

View full text Add to dashboard Cite

Interferon (IFN)‐ζlimitin has been considered as a novel type I IFN by the Nomenclature Committee of the International Society for Interferon and Cytokine Research. IFN‐ζlimitin shows some sequence homology with IFN‐α and IFN‐β, has a globular structure with five α‐helices and four loops, and recognizes IFN‐α/β receptor. Although IFN‐ζlimitin displays antiviral, immunomodulatory, and antitumor effects, it has much less lymphomyelosuppressive activities than IFN‐α. Treatment of cells with type I IFNs induces and/or activates a number of molecules, which regulate cell cycle and apoptosis. It is noteworthy that IFN‐ζlimitin activates the Tyk2‐Daxx and Tyk2‐Crk pathways weaker than IFN‐α. Because experiments using antisense oligonucleotides have revealed their essential role in type I IFN‐related suppression of lympho‐hematopoiesis, little ability of IFN‐ζlimitin to activate the Tyk2‐dependent signaling pathway may explain its uniquely narrow range of biological activities. Further analysis of structure‐function relationship of type I IFNs will establish an engineered cytokine with useful features of IFN‐ζlimitin.

show abstract

Section: Ifn-ζ/limitinmentioning

confidence: 89%

IFN-? limitin: a member of type I IFN with mild lympho-myelosuppression

Oritani

Kanakura

2005

J Cellular Mol Med

Self Cite

View full text Add to dashboard Cite

show abstract

“…The first one proposes that interferonlike cytokines secreted by different cell groups (including bone marrow stromal cells and thymic T-cells) would affect the growth and differentiation of B-cell precursors (5,6). This theory comes from murine models, and it has not been proven in patients with thymoma.…”

Section: Discussionmentioning

confidence: 99%

Persistence of immunological alterations after thymectomy in Good's syndrome: A clue to its pathogenesis

Vega

Velasco‐Tirado

Pozo-Rosado

et al. 2011

Cytometry Part B Clinical

View full text Add to dashboard Cite

Analyzing the phenotypic characterization of the immune system cells involved in the pathogenesis of immunodeficiency with thymoma (Good's syndrome) is difficult due to the low number of studies on that subject. We describe the immunological alterations observed in a case of Good's syndrome, and we summarize the pathogenic explanations found in the literature. V C 2011 International Clinical Cytometry Society

show abstract

“…Eukaryotic mRNAs are also often characterized by a suboptimal context of the predicted translation start site (Rogozin et al 2001), which provides an opportunity for the initiation of translation at downstream AUG triplets. In particular, the initiation of translation at several in-frame AUGs could result in the synthesis of protein variants with different N-termini (N-truncated or N-extended) and these protein variants could be of functional importance (Bab et al 1999;Tanaka and Ueda 2000;Watanabe et al 2001;Pedrajas et al 2002;Logette et al 2003;Oritani et al 2003;Kochetov et al 2003;Outten and Culotta 2004;Kochetov and Sarai 2004).…”

Section: Introductionmentioning

confidence: 99%

The role of alternative translation start sites in the generation of human protein diversity

et al. 2005

View full text Add to dashboard Cite

According to the scanning model, 40S ribosomal subunits initiate translation at the first (5' proximal) AUG codon they encounter. However, if the first AUG is in a suboptimal context, it may not be recognized, and translation can then initiate at downstream AUG(s). In this way, a single RNA can produce several variant products. Earlier experiments suggested that some of these additional protein variants might be functionally important. We have analysed human mRNAs that have AUG triplets in 5' untranslated regions and mRNAs in which the annotated translational start codon is located in a suboptimal context. It was found that 3% of human mRNAs have the potential to encode N-terminally extended variants of the annotated proteins and 12% could code for N-truncated variants. The predicted subcellular localizations of these protein variants were compared: 31% of the N-extended proteins and 30% of the N-truncated proteins were predicted to localize to subcellular compartments that differed from those targeted by the annotated protein forms. These results suggest that additional AUGs may frequently be exploited for the synthesis of proteins that possess novel functional properties.

show abstract

T lymphocytes constitutively produce an interferonlike cytokine limitin characterized as a heat- and acid-stable and heparin-binding glycoprotein

Cited by 19 publications

References 50 publications

IFN-? limitin: a member of type I IFN with mild lympho-myelosuppression

IFN-? limitin: a member of type I IFN with mild lympho-myelosuppression

Persistence of immunological alterations after thymectomy in Good's syndrome: A clue to its pathogenesis

The role of alternative translation start sites in the generation of human protein diversity

Contact Info

Product

Resources

About