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Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: Sequence homology with animal lectins

Authors :
Kawamura Tamio
Shikata Yasushi
Ohya Yukio
Seto Toshio
Tanaka Isao
Toyoshima Satoshi
Osawa Toshiaki
Yoshimatsu Kentaro
Hasegawa Yoshikazu
Kitoh Kyousuke
Source :
Molecular Immunology. 29:537-546
Publication Year :
1992
Publisher :
Elsevier BV, 1992.

Abstract

We have purified a novel immunoregulatory factor (BMPG: bone-marrow proteoglycan) produced by a T-cell hybridoma, with a monoclonal antibody column. Using an oligonucleotide probe corresponding to the partial amino acid sequence of BMPG, we cloned, sequenced, and expressed a cDNA for BMPG. BMPG has 222 amino acid residues with a 16 N-terminal signal sequence, so the mature form has 206 amino acid residues. BMPG was found to have unique characteristics: it has three types of sugar chains and it shows a marked homology with animal lectins including the human asialoglycoprotein receptor, chicken hepatic lectin and the homing receptor of lymphocytes.

Details

ISSN :
01615890
Volume :
29
Database :
OpenAIRE
Journal :
Molecular Immunology
Accession number :
edsair.doi.dedup.....32d5741b163b431a5bb459d5ab256d8e
Full Text :
https://doi.org/10.1016/0161-5890(92)90012-m