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Novel structures CTLA‐2α and CTLA‐2β expressed in mouse activated T cells and mast cells and homologous to cysteine proteinase proregions
Author(s) -
Denizot François,
Brunet JeanFrançois,
Roustan Paul,
Harper Katherine,
Suzan Marie,
Luciani MarieFrançoise,
Mattei MarieGeneviéve,
Golstein Pierre
Publication year - 1989
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.1830190409
Subject(s) - biology , complementary dna , gene , homologous chromosome , microbiology and biotechnology , cdna library , open reading frame , cysteine protease , cysteine , peptide sequence , genetics , biochemistry , enzyme
Abstract Differential screening of a subtracted cDNA library led to the detection of two distinct but homologous mouse cDNA, called CTLA‐2α and CTLA‐2β. The corresponding transcripts have a tissue distribution restricted to T lymphocytes, where they are inducible upon activation, and to mast cells. The open‐frame regions of both cDNA encode proteins homologous to cysteine proteinase precursors, remarkably, however, only to the proregion of these. The ctla‐2α and ctla‐β genes both map to the C1 band of mouse chromosome 13. Sequence comparisons suggest that the proregion of an ancestor proteinase gene evolved to the ctla‐2 genes by successive duplications, first to autonomy, then to amplification. These results raise the question of the possible role of cysteine proteinase proregions, of cysteine proteinases themselves and of inhibitors thereof in activated T lymphocytes; from a different point of view, they also show that some protease proregions may have evolved as autonomous modules.