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Prepublished online as a Blood First Edition Paper on June 28, 2002; DOI 10.1182/blood-2002-01-0045.
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Blood, 1 January 2003, Vol. 101, No. 1, pp. 178-185
IMMUNOBIOLOGY
T lymphocytes constitutively produce an interferonlike
cytokine limitin 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
From the Department of Internal Medicine and Molecular
Science, Graduate School of Medicine, Osaka University, and Department
of Pathology, Osaka University Medical School, Osaka,
Japan; Pharmaceutical Development Laboratory and
Pharmaceutical Research Laboratory, Kirin Brewery Co Ltd, Takasaki,
Gunma, Japan; and Oklahoma Medical Research Foundation,
825 Northeast, 13th St, Oklahoma City.
Several reports have described "multifunctional"
eukaryotic mRNAs producing more than one protein through alternative
translational initiation at multiple AUG codons. There are 2 such
codons in the 5' region of our recently cloned limitin gene
where 2 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 the transfected 293T
cells. We found that the second ATG is more effective as a
translational initiation site than the first ATG and yields a secreted
protein of 182 amino acids with the same activity as products made with
full-length limitin cDNA. Immunohistochemical and reverse
transcription-polymerase chain reaction 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 with the potential for dimerization.
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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