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The Th1-Specific Costimulatory Molecule, M150, Is a Posttranslational Isoform of Lysosome-Associated Membrane Protein-1
Author(s) -
Durbaka V. R. Prasad,
Vrajesh V. Parekh,
Bimba N. Joshi,
Pinaki P. Banerjee,
Pradeep B. Parab,
Samit Chattopadhyay,
Anil Kumar,
Gyan C. Mishra
Publication year - 2002
Publication title -
the journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.737
H-Index - 372
eISSN - 1550-6606
pISSN - 0022-1767
DOI - 10.4049/jimmunol.169.4.1801
Subject(s) - lysosome , microbiology and biotechnology , glycosylation , glycoprotein , membrane glycoproteins , t cell , biology , gene isoform , chemistry , biochemistry , immune system , immunology , enzyme , gene
In an earlier report, we had shown a 150-kDa protein termed as M150, isolated from the surface of activated macrophages, to possess costimulatory activity for CD4(+) T cells. Significantly, this protein was found to specifically elicit Th1 responses. In this study, we characterize M150, which belongs to a unique subset of the lysosome-associated membrane protein-1 glycoprotein. Interestingly, the costimulatory activity of M150 depends on its posttranslational modification, which has a distinct glycosylation pattern restricted to macrophages. Furthermore, it has been demonstrated that in addition to stimulating Th1-specific responses, M150 is also capable of driving differentiation of naive CD4(+) T cells into the Th1 subset. This altered posttranslational modification of housekeeping protein appears to represent a novel pathway by which APCs can additionally regulate T cell responses.

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