Work

The Light Chain of CD98 Is Identified as E16/TA1 Protein

Year: 1998

Type: article

Abstract: The 80/40-kDa CD98 protein complex was purified using an anti-CD98 heavy chain monoclonal antibody coupled to Sepharose beads. Eluted proteins were subjected to preparative SDS-polyacrylamide gel electrophoresis, and protein corresponding to the 40-kDa CD98 light chain was excised. Following proteolysis with trypsin, a peptide fragment was sequenced by mass spectrometry. The nine residues obtained were identical to established C-terminal sequences of the human E16 and rat TA1 proteins, suggesting that TA1/E16 protein is the CD98 light chain. Consistent with this, anti-TA1/E16 antibodies specifically immunoblotted the approximately 35-40-kDa light chain present upon immunoprecipitation of the human CD98 complex. Furthermore, anti-CD98 heavy chain antibody specifically co-immunoprecipitated hemagglutinin-tagged light chain from cells transfected with hemagglutinin-tagged E16 cDNA. In conclusion, the CD98 light chain is identical to the TA1/E16 protein, based on partial amino acid sequence identity, antibody cross-reactivity, genetic reconstitution evidence, similar molecular size, and comparable cell distribution.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.273.50.33127

Authors: Brian A. Mannion, Tatiana V. Kolesnikova, Sue Hwa Lin, Shuo Wang, Nancy L. Thompson, Martin E. Hemler

Institutions: Harvard University, Dana-Farber Cancer Institute, Dana-Farber/Harvard Cancer Center, Rhode Island Hospital

Language: English

Topic: Amino Acid Enzymes and Metabolism

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430