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J. Biol. Chem., Vol. 267, Issue 4, 2200-2208, Feb, 1992
D Marguet, AM Bernard, I Vivier, D Darmoul, P Naquet and M Pierres
Thymocyte-activating molecule (THAM) was initially characterized as a
developmentally regulated, dimeric cell-surface molecule capable of
activating mouse thymocytes and T lymphocytes upon monoclonal antibody
(mAb)-mediated cross-linking. We recently obtained structural evidence
indicating that this molecule is the mouse homologue of the human T
cell-activating ectoenzyme CD26 (dipeptidyl peptidase IV, DPP IV). We
describe here the cloning and the characterization of THAM cDNA. Two clones
(3.3 and 2.8 kilobases) were isolated. THAM-3.3 cDNA contains an open
reading frame of 2,280 nucleotides that encodes a protein of 760 amino
acids having a calculated size of 87,500 Da. Complete N- glycosylation at
each of the nine potential sites would result in a mature 110,000-Da
molecule. Protein sequence comparisons revealed a significant homology (in
particular in the COOH-terminal domain) between THAM and the rat or human
DPP IV or the yeast dipeptidyl aminopeptidase B molecules (92, 85, and 30%
sequence identity, respectively). Structural comparison of serine proteases
(i.e. acyl- amino acid hydrolase or prolyl endopeptidase) with the most
conserved domain of THAM identified a stretch of 200 amino acids containing
a putative catalytic triad arranged in a novel topological order (Ser- 624,
Asp-702, and His-734) thereby defining a subfamily of nonclassical serine
proteases. Expression of THAM during thymus ontogeny was found to be mainly
regulated at the transcriptional level as determined by RNase protection
assay. To investigate directly some of the functions which have been
ascribed to DPP IV, we transfected an ovalbumin/Aq- reactive, THAM- T
hybridoma cell line with THAM-3.3 cDNA. The resultant transfectants
acquired (i) DPP IV enzymatic activity that precisely paralleled the
density of surface-expressed THAM; (ii) an Mr = 115,000 (reduced) and
110,000/128,000 (nonreduced) molecule that could be immunoprecipitated by
the THAM-specific mAb H194-112; and (iii) the capacity of being triggered
by this mAb to release interleukin-2. These data indicate that a single
cDNA species can encode a multifunctional molecule (e.g. activation
signal-transducing structure and ectopeptidase), the heterodimeric state of
which very likely results from a differential post-translational
modification of the same protein core.
cDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases
Centre d'Immunologie-Institut National de la Sante et de la Recherche Medicale-Centre National de la Recherche Scientifique de Marseille- Luminy, France.
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