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Characterization of human homologue of 4-1BB and its ligand

Cited 37 time in Web of Science Cited 41 time in Scopus
Authors
Zhou, Zhen; Kim, Seung; Hurtado, José; Lee, Zang H.; Kim, Kack K.; Pollok, Karen E.; Kwon, Byoung S.
Issue Date
1995-02
Publisher
Elsevier
Citation
Immunology Letters, 45, 67-73
Keywords
Human 4-1BBHuman 4-1BB ligandBinding siteDissociation constant
Abstract
The human homologue of 4-1BB (H4-1BB) cDNA was isolated from PMA plus ionomycin-treated human peripheral T-cell cDNA libraries. The amino acid sequence deduced from the nucleotide sequence showed that the protein is composed of 255 amino acids with 2 potential N-linked glycosylation sites. The molecular weight of its protein backbone is calculated to be 27 kDa. The H4-1BB contains features such as signal sequence and transmembrane domain, indicating that it is a receptor protein. This protein showed 60% identity of amino acid sequence to mouse 4-1BB. In the cytoplasmic domain there are 5 regions of amino acid sequences conserved from mouse to human, indicating that these residues might be important in the 4-1BB function. H4-1BB mRNA was detected in unstimulated peripheral blood T cells and was inducible in T-cell lines such as Jurkat and CEM. H4-1BB-AP, a fusion protein between the H4-1BB extracellular domain and alkaline phosphatase, was used to identify the ligand for the H4-1BB. Although the H4-1BB ligand was detected in both T and B cells of human peripheral blood, the ligand was preferentially expressed in primary B cells and B-cell lines. Daudi, a B-cell lymphoma, was one of the B-cell lines that carried a higher number of ligands. Scatchard analysis showed that the Kd = 1.4 × 109 M and the number of ligands in Daudi cell was 4.2 × 103.
ISSN
0165-2478
Language
English
URI
https://hdl.handle.net/10371/68602
DOI
https://doi.org/10.1016/0165-2478(94)00227-I
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College of Dentistry/School of Dentistry (치과대학/치의학대학원)Dept. of Dentistry (치의학과)Journal Papers (저널논문_치의학과)
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