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Cutting Edge: Primary Structure of the Light Chain of Fusion Regulatory Protein-1/CD98/4F2 Predicts a Protein with Multiple Transmembrane Domains That Is Almost Identical to the Amino Acid Transporter E16^{1 ,2}

Masato Tsurudome^3,*, Morihiro Ito^*, Shin-Ichiro Takebayashi, Katsuzumi Okumura, Machiko Nishio^*, Mitsuo Kawano^*, Shigeru Kusagawa^*, Hiroshi Komada and Yasuhiko Ito^*

^* Department of Microbiology, Mie University School of Medicine, and Laboratory of Biological Chemistry, Faculty of Bioresources, Mie University, Tsu, Japan; and Department of Microbiology, Suzuka University of Medical Science and Technology, Suzuka, Japan

The CD98 light chain (CD98LC) was copurified from HeLa S3 cells by an affinity chromatography using a mAb specific for the fusion regulatory protein-1 (FRP-1) which is identical to the CD98 heavy chain. On the basis of the N-terminal sequence (63 amino acids) of purified CD98LC polypeptide, we have cloned a PCR fragment (155 bp) from a HeLa S3 cDNA library and finally obtained a full cDNA clone encoding the CD98LC. Fluorescence in situ hybridization analysis using the cDNA assigned the CD98LC gene to the long arm of human chromosome 16 (16q24). The predicted amino acid sequence suggested that CD98LC is a protein with multiple transmembrane domains and is almost identical to the amino acid transporter E16. Resting monocytes and lymphocytes expressed CD98LC as analyzed by a newly isolated anti-CD98LC mAb, which showed cross-reactivity with insect Sf9 cells as well as with various mammalian cell lines.

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