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

被引:17
作者
Oritani, K
Hirota, S
Nakagawa, T
Takahashi, I
Kawamoto, S
Yamada, M
Ishida, N
Kadoya, T
Tomiyama, Y
Kincade, PW
Matsuzawa, Y
机构
[1] Osaka Univ, Grad Sch Med, Dept Internal Med & Mol Sci, Suita, Osaka 5650871, Japan
[2] Osaka Univ, Sch Med, Dept Pathol, Osaka, Japan
[3] Kirin Brewery Co Ltd, Pharmaceut Dev Lab, Takasaki, Gumma, Japan
[4] Kirin Brewery Co Ltd, Pharmaceut Res Lab, Takasaki, Gumma, Japan
[5] Oklahoma Med Res Fdn, Oklahoma City, OK USA
关键词
D O I
10.1182/blood-2002-01-0045
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
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. (C) 2003 by The American Society of Hematology.
引用
收藏
页码:178 / 185
页数:8
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