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Prepublished online as a Blood First Edition Paper on June 28, 2002; DOI 10.1182/blood-2002-01-0045.
Submitted January 16, 2002
Accepted June 13, 2002
T lymphocytes constitutively produce limitin, an interferon-like cytokine characterized as a heat- and acid-stable and heparin-binding glycoprotein
Kenji Oritani*, Seiichi Hirota, Taishirou Nakagawa, Isao Takahashi, Shin-ichiro Kawamoto, Masahide Yamada, Naoko Ishida, Toshihiko Kadoya, Yoshiaki Tomiyama, Paul W Kincade, and Yuji Matsuzawa
Department of Internal Medicine and Molecular Science, Osaka University Graduate School of Medicine, Osaka, Japan
Department of Pathology, Osaka University Medical School, Osaka, Japan
Pharmaceutical Development Laboratory, Kirin Brewery Co Ltd, Gunma, Japan
Pharmaceutical Research Laboratory, Kirin Brewery Co Ltd, Gunma, Japan
Oklahoma Medical Research Foundation, Oklahoma City, OK, USA
* Corresponding author; email: oritani{at}imed2.med.osaka-u.ac.jp.
Several reports have described "multifunctional" eukaryotic mRNAs producing more than one protein through alternative translational initiation at multiple AUG codons. There are two such codons in the 5'-region of our recently cloned limitin gene where two open reading frames overlap by 34 nucleotides. The deduced protein translated from the first ATG contains 33 amino acids, lacks a signal peptide and has no obvious effects on transfected 293T cells. We found that the second ATG is more effective as a translational initiation site than the first ATG and yields a 182 amino acid secreted protein with the same activity as products made with full-length limitin cDNA. Immunohistochemical and RT-PCR analysis revealed that the longer limitin protein is produced by mature T lymphocytes in spleen and thymus as well as by bronchial epithelial and salivary duct cells in healthy mice. Properties of recombinant limitin were determined, revealing it to be a serologically distinct, heat- and acid-stable, heparin-binding glycoprotein. Although the longer limitin protein is structurally and characteristically related to type I interferons, its production is uniquely regulated by translation as well as transcription.
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